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Conserved domains on  [gi|1069468527|ref|XP_018131795|]
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uncharacterized protein VE01_03749 [Pseudogymnoascus verrucosus]

Protein Classification

aldehyde dehydrogenase family protein( domain architecture ID 10002945)

aldehyde dehydrogenase family protein is an NAD(P)(+)-dependent enzyme that may oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and may play an important role in detoxification

CATH:  3.40.605.10|3.40.309.10
EC:  1.2.1.-
Gene Ontology:  GO:0004030
PubMed:  11168411|18611112|10210192|12604184
SCOP:  4000806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 1-474 1.38e-178

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


:

Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 508.90  E-value: 1.38e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   1 MSASpiETRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLF 80
Cdd:COG1012     1 MTTP--EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  81 AEHSAELAQLEAKSMGRPVT-SFFDAGAASDYFRYFSEAAYPMG--TSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFF 157
Cdd:COG1012    79 EERREELAALLTLETGKPLAeARGEVDRAADFLRYYAGEARRLYgeTIPSDAPGTRAYVRREPLGVVGAITPWNFPLALA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 158 SKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQK 236
Cdd:COG1012   159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSeVGAALVAHPDVDKISFTGSTAVGRRIAA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 237 AAADsNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPT 316
Cdd:COG1012   239 AAAE-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 317 QAGTTQGPQADKVQHETVKRYLALAEKSGTKIT---EDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEA 393
Cdd:COG1012   318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLtggRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEE 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 394 EAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:COG1012   398 EAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477


                  .
gi 1069468527 474 K 474
Cdd:COG1012   478 R 478
 
Name Accession Description Interval E-value
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 1-474 1.38e-178

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 508.90  E-value: 1.38e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   1 MSASpiETRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLF 80
Cdd:COG1012     1 MTTP--EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  81 AEHSAELAQLEAKSMGRPVT-SFFDAGAASDYFRYFSEAAYPMG--TSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFF 157
Cdd:COG1012    79 EERREELAALLTLETGKPLAeARGEVDRAADFLRYYAGEARRLYgeTIPSDAPGTRAYVRREPLGVVGAITPWNFPLALA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 158 SKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQK 236
Cdd:COG1012   159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSeVGAALVAHPDVDKISFTGSTAVGRRIAA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 237 AAADsNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPT 316
Cdd:COG1012   239 AAAE-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 317 QAGTTQGPQADKVQHETVKRYLALAEKSGTKIT---EDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEA 393
Cdd:COG1012   318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLtggRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEE 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 394 EAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:COG1012   398 EAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477


                  .
gi 1069468527 474 K 474
Cdd:COG1012   478 R 478
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 20-471 1.24e-168

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 482.80  E-value: 1.24e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  20 DESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPV 99
Cdd:pfam00171   4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 100 T-SFFDAGAASDYFRYFSEAA-YPMGTSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSE 177
Cdd:pfam00171  84 AeARGEVDRAIDVLRYYAGLArRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 178 KAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAAdSNLKNCIFELGGKSPA 256
Cdd:pfam00171 164 LTPLTALLLAELFEEAGLPAGVLNVVTGSGAeVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKRVTLELGGKNPL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 257 LVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKR 336
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 337 YLALAEKSGTKI----TEDLPNvsGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFT 412
Cdd:pfam00171 323 YVEDAKEEGAKLltggEAGLDN--GYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFT 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1069468527 413 KDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAV 471
Cdd:pfam00171 401 SDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
 6-471 8.43e-164

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.


Pssm-ID: 143410  Cd Length: 476  Bit Score: 471.31  E-value: 8.43e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   6 IETRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWS--ALSPKERSVYLARLGVLFAEH 83
Cdd:cd07091     2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWwrKMDPRERGRLLNKLADLIERD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  84 SAELAQLEAKSMGRPVT--SFFDAGAASDYFRYFSEAAYPMGTSSLNTPG-FVNMGVKQPYGVCGIIIPWNAPLIFFSKK 160
Cdd:cd07091    82 RDELAALESLDNGKPLEesAKGDVALSIKCLRYYAGWADKIQGKTIPIDGnFLAYTRREPIGVCGQIIPWNFPLLMLAWK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 161 GAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAA 239
Cdd:cd07091   162 LAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPtAGAAISSHMDVDKIAFTGSTAVGRTIMEAAA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 240 DSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAG 319
Cdd:cd07091   242 KSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPD 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 320 TTQGPQADKVQHETVKRYLALAEKSGTKIT---EDLPNvSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAI 396
Cdd:cd07091   322 TFQGPQVSKAQFDKILSYIESGKKEGATLLtggERHGS-KGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1069468527 397 AKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNdMPFGGWKGSGIGRESYIGGVESFMEDKAV 471
Cdd:cd07091   401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAA-VPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
8-474 5.94e-124

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 369.62  E-value: 5.94e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   8 TRLFINGKFQAiDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAEL 87
Cdd:PRK13473    3 TKLLINGELVA-GEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  88 AQLEAKSMGRPV--TSFFDAGAASDYFRYFSEAAYPMGTSSLN--TPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAA 163
Cdd:PRK13473   82 ARLESLNCGKPLhlALNDEIPAIVDVFRFFAGAARCLEGKAAGeyLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 164 ALAAGNTVVLKSSEKAPLTCAKAAELVAKAgFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADSn 242
Cdd:PRK13473  162 ALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGAtVGDALVGHPKVRMVSLTGSIATGKHVLSAAADS- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 243 LKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQ 322
Cdd:PRK13473  240 VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTEL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 323 GPQADKVQHETVKRYL--ALAEKSGTKIT-EDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKA 399
Cdd:PRK13473  320 GPLISAAHRDRVAGFVerAKALGHIRVVTgGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWA 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1069468527 400 NDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKgNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLIK 474
Cdd:PRK13473  400 NDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLV-SEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
 11-469 1.73e-115

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 347.57  E-value: 1.73e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  11 FINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQL 90
Cdd:TIGR01804   1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  91 EAKSMGRPV--TSFFDAGAASDYFRYFSEAAYPMGTSSLNTPG--FVNMgVKQPYGVCGIIIPWNAPLIFFSKKGAAALA 166
Cdd:TIGR01804  81 ETLDTGKTLqeTIVADMDSGADVFEFFAGLAPALNGEIIPLGGpsFAYT-IREPLGVCVGIGAWNYPLQIASWKIAPALA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 167 AGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAA-GAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKN 245
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEvGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAG-HLKH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 246 CIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQ 325
Cdd:TIGR01804 239 VTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 326 ADKVQHETVKRYLALAEKSGTKITE--DLPNVSGL----YISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKA 399
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATggGRPENVGLqngfFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 400 NDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGnDMPFGGWKGSGIGRESYIGGVESFMEDK 469
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPA-EAPFGGYKQSGIGRENGKAALAHYTEVK 467
 
Name Accession Description Interval E-value
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 1-474 1.38e-178

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 508.90  E-value: 1.38e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   1 MSASpiETRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLF 80
Cdd:COG1012     1 MTTP--EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  81 AEHSAELAQLEAKSMGRPVT-SFFDAGAASDYFRYFSEAAYPMG--TSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFF 157
Cdd:COG1012    79 EERREELAALLTLETGKPLAeARGEVDRAADFLRYYAGEARRLYgeTIPSDAPGTRAYVRREPLGVVGAITPWNFPLALA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 158 SKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQK 236
Cdd:COG1012   159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSeVGAALVAHPDVDKISFTGSTAVGRRIAA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 237 AAADsNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPT 316
Cdd:COG1012   239 AAAE-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 317 QAGTTQGPQADKVQHETVKRYLALAEKSGTKIT---EDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEA 393
Cdd:COG1012   318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLtggRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEE 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 394 EAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:COG1012   398 EAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477


                  .
gi 1069468527 474 K 474
Cdd:COG1012   478 R 478
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 20-471 1.24e-168

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 482.80  E-value: 1.24e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  20 DESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPV 99
Cdd:pfam00171   4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 100 T-SFFDAGAASDYFRYFSEAA-YPMGTSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSE 177
Cdd:pfam00171  84 AeARGEVDRAIDVLRYYAGLArRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 178 KAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAAdSNLKNCIFELGGKSPA 256
Cdd:pfam00171 164 LTPLTALLLAELFEEAGLPAGVLNVVTGSGAeVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKRVTLELGGKNPL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 257 LVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKR 336
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 337 YLALAEKSGTKI----TEDLPNvsGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFT 412
Cdd:pfam00171 323 YVEDAKEEGAKLltggEAGLDN--GYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFT 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1069468527 413 KDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAV 471
Cdd:pfam00171 401 SDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
 6-471 8.43e-164

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.


Pssm-ID: 143410  Cd Length: 476  Bit Score: 471.31  E-value: 8.43e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   6 IETRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWS--ALSPKERSVYLARLGVLFAEH 83
Cdd:cd07091     2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWwrKMDPRERGRLLNKLADLIERD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  84 SAELAQLEAKSMGRPVT--SFFDAGAASDYFRYFSEAAYPMGTSSLNTPG-FVNMGVKQPYGVCGIIIPWNAPLIFFSKK 160
Cdd:cd07091    82 RDELAALESLDNGKPLEesAKGDVALSIKCLRYYAGWADKIQGKTIPIDGnFLAYTRREPIGVCGQIIPWNFPLLMLAWK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 161 GAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAA 239
Cdd:cd07091   162 LAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPtAGAAISSHMDVDKIAFTGSTAVGRTIMEAAA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 240 DSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAG 319
Cdd:cd07091   242 KSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPD 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 320 TTQGPQADKVQHETVKRYLALAEKSGTKIT---EDLPNvSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAI 396
Cdd:cd07091   322 TFQGPQVSKAQFDKILSYIESGKKEGATLLtggERHGS-KGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1069468527 397 AKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNdMPFGGWKGSGIGRESYIGGVESFMEDKAV 471
Cdd:cd07091   401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAA-VPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
 28-473 1.81e-160

Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.


Pssm-ID: 143412 [Multi-domain]  Cd Length: 455  Bit Score: 462.03  E-value: 1.81e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  28 HSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVTSF--FDA 105
Cdd:cd07093     2 FNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLArtRDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 106 GAASDYFRYFSEAAYPMGTSSLNTP-GFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCA 184
Cdd:cd07093    82 PRAAANFRFFADYILQLDGESYPQDgGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 185 KAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDAD 263
Cdd:cd07093   162 LLAELANEAGLPPGVVNVVHGFGPeAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVFADAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 264 IEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEK 343
Cdd:cd07093   241 LDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 344 SGTKI------TEDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDR 417
Cdd:cd07093   321 EGATIltgggrPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGR 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1069468527 418 AMRVSKQLEAGTVGVNCsspTKGND--MPFGGWKGSGIGREsyiGGVES---FMEDKAVLI 473
Cdd:cd07093   401 AHRVARRLEAGTVWVNC---WLVRDlrTPFGGVKASGIGRE---GGDYSlefYTELKNVCI 455
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
 58-473 1.38e-156

NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.


Pssm-ID: 143397 [Multi-domain]  Cd Length: 432  Bit Score: 451.28  E-value: 1.38e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  58 FPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVTSF-FDAGAASDYFRYFSEAAY-PMGTSSLNT-PGFVN 134
Cdd:cd07078    11 FKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAlGEVARAADTFRYYAGLARrLHGEVIPSPdPGELA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 135 MGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVM 213
Cdd:cd07078    91 IVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDeVGAAL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 214 SSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHK 293
Cdd:cd07078   171 ASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 294 SIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKIT---EDLPNVSGLYISPTIFTDTPE 370
Cdd:cd07078   250 SIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLcggKRLEGGKGYFVPPTVLTDVDP 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 371 DAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKG 450
Cdd:cd07078   330 DMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPSAPFGGVKQ 409

                         410       420
                  ....*....|....*....|...
gi 1069468527 451 SGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07078   410 SGIGREGGPYGLEEYTEPKTVTI 432
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
 8-473 2.68e-150

Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.


Pssm-ID: 143462  Cd Length: 484  Bit Score: 437.22  E-value: 2.68e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   8 TRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPA-WSALSPKERSVYLARLGVLFAEHSAE 86
Cdd:cd07144     8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  87 LAQLEAKSMGRPVTSFFDAGAASDY--FRYFSEAAYPM-GTSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAA 163
Cdd:cd07144    88 LAAIEALDSGKPYHSNALGDLDEIIavIRYYAGWADKIqGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAP 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 164 ALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAAdSN 242
Cdd:cd07144   168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAvAGSALAEHPDVDKIAFTGSTATGRLVMKAAA-QN 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 243 LKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSA-KLGDPTQAGTT 321
Cdd:cd07144   247 LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDTV 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 322 QGPQADKVQHETVKRYLALAEKSGTK-ITEDLPNVSGL----YISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAI 396
Cdd:cd07144   327 VGPQVSKTQYDRVLSYIEKGKKEGAKlVYGGEKAPEGLgkgyFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAI 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 397 AKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSsptkgND----MPFGGWKGSGIGRESYIGGVESFMEDKAVL 472
Cdd:cd07144   407 KKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSS-----NDsdvgVPFGGFKMSGIGRELGEYGLETYTQTKAVH 481


                  .
gi 1069468527 473 I 473
Cdd:cd07144   482 I 482
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
 30-473 1.72e-148

Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.


Pssm-ID: 143432 [Multi-domain]  Cd Length: 457  Bit Score: 431.59  E-value: 1.72e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  30 PSTGEFIAKVPEATAKDVDAAVAAAKAAF--PAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVT-SFFDAG 106
Cdd:cd07114     4 PATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIReTRAQVR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 107 AASDYFRYFSEAAYPMGTSSL--NTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCA 184
Cdd:cd07114    84 YLAEWYRYYAGLADKIEGAVIpvDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 185 KAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDAD 263
Cdd:cd07114   164 ELAKLAEEAGFPPGVVNVVTGFGPeTGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIVFDDAD 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 264 IEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEK 343
Cdd:cd07114   243 LDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARARE 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 344 SGTKI------TEDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDR 417
Cdd:cd07114   323 EGARVltggerPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLAR 402

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1069468527 418 AMRVSKQLEAGTVGVNC---SSPTkgndMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07114   403 AHRVARAIEAGTVWVNTyraLSPS----SPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
 10-472 2.82e-140

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.


Pssm-ID: 143456 [Multi-domain]  Cd Length: 466  Bit Score: 411.13  E-value: 2.82e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  10 LFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQ 89
Cdd:cd07138     1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  90 LEAKSMGRPVTSFFDA--GAASDYFRYFSEAA------YPMGTSSLntpgfvnmgVKQPYGVCGIIIPWNAPLIFFSKKG 161
Cdd:cd07138    81 AITLEMGAPITLARAAqvGLGIGHLRAAADALkdfefeERRGNSLV---------VREPIGVCGLITPWNWPLNQIVLKV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 162 AAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAAD 240
Cdd:cd07138   152 APALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPvVGEALSAHPDVDMVSFTGSTRAGKRVAEAAAD 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 241 SnLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGT 320
Cdd:cd07138   232 T-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPAT 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 321 TQGPQADKVQHETVKRYLALAEKSGTK-IT--EDLPNV--SGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEA 395
Cdd:cd07138   311 TLGPLASAAQFDRVQGYIQKGIEEGARlVAggPGRPEGleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1069468527 396 IAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGndMPFGGWKGSGIGRESYIGGVESFMEDKAVL 472
Cdd:cd07138   391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPG--APFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
 23-473 1.30e-139

Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.


Pssm-ID: 143430 [Multi-domain]  Cd Length: 462  Bit Score: 409.30  E-value: 1.30e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  23 QTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPA--WSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVT 100
Cdd:cd07112     2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 101 SFF--DAGAASDYFRYFSEAAYPM-GTSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSE 177
Cdd:cd07112    82 DALavDVPSAANTFRWYAEAIDKVyGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 178 KAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADSNLKNCIFELGGKSPA 256
Cdd:cd07112   162 QSPLTALRLAELALEAGLPAGVLNVVPGFGHtAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSPN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 257 LVFEDA-DIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVK 335
Cdd:cd07112   242 IVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 336 RYLALAEKSGTKI----TEDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVF 411
Cdd:cd07112   322 GYIESGKAEGARLvaggKRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVW 401

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069468527 412 TKDIDRAMRVSKQLEAGTVGVNCSSptkGNDM--PFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07112   402 TSDLSRAHRVARRLRAGTVWVNCFD---EGDIttPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
 30-473 4.27e-136

Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.


Pssm-ID: 143421 [Multi-domain]  Cd Length: 451  Bit Score: 399.88  E-value: 4.27e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  30 PSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVT-SFFDAGAA 108
Cdd:cd07103     4 PATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAeARGEVDYA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 109 SDYFRYFSEAA---YPMgTSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAK 185
Cdd:cd07103    84 ASFLEWFAEEArriYGR-TIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 186 AAELVAKAGFPPGVFNILSGHGAA-GAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADI 264
Cdd:cd07103   163 LAELAEEAGLPAGVLNVVTGSPAEiGEALCASPRVRKISFTGSTAVGKLLMAQAAD-TVKRVSLELGGNAPFIVFDDADL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 265 EQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKS 344
Cdd:cd07103   242 DKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAK 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 345 GTKIT---EDLPNvSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRV 421
Cdd:cd07103   322 GAKVLtggKRLGL-GGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1069468527 422 SKQLEAGTVGVNCSSPTkGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07103   401 AEALEAGMVGINTGLIS-DAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
 11-477 1.32e-135

Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.


Pssm-ID: 143437  Cd Length: 482  Bit Score: 399.76  E-value: 1.32e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  11 FINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAF--PAWSALSPKERSVYLARLGVLFAEHSAELA 88
Cdd:cd07119     1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  89 QLEAKSMGRP-VTSFFDAGAASDYFRYFSEAAYPMGTSSLNTPGFV-NMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALA 166
Cdd:cd07119    81 RLETLNTGKTlRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHViSRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 167 AGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKN 245
Cdd:cd07119   161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGAtVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NVKK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 246 CIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQ 325
Cdd:cd07119   240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 326 ADKVQHETVKRYLALAEKSGTKIT------EDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKA 399
Cdd:cd07119   320 VSAEHREKVLSYIQLGKEEGARLVcggkrpTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1069468527 400 NDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKgNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLIKVAP 477
Cdd:cd07119   400 NDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYF-AEAPWGGYKQSGIGRELGPTGLEEYQETKHININLSP 476
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
 6-475 2.30e-134

Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.


Pssm-ID: 143461  Cd Length: 481  Bit Score: 396.51  E-value: 2.30e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   6 IETRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAF--PAWSALSPKERSVYLARLGVLFAEH 83
Cdd:cd07143     5 QPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFetDWGLKVSGSKRGRCLSKLADLMERN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  84 SAELAQLEAKSMGRPVTSF--FDAGAASDYFRYFSEAAYPMGTSSLNT-PGFVNMGVKQPYGVCGIIIPWNAPLIFFSKK 160
Cdd:cd07143    85 LDYLASIEALDNGKTFGTAkrVDVQASADTFRYYGGWADKIHGQVIETdIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 161 GAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHG-AAGAVMSSHMDIRIISFTGSTRTGRAIQKAAA 239
Cdd:cd07143   165 IAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGrTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 240 DSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAG 319
Cdd:cd07143   245 KSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 320 TTQGPQADKVQHETVKRYLALAEKSGTKITE--DLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIA 397
Cdd:cd07143   325 TFQGPQVSQIQYERIMSYIESGKAEGATVETggKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1069468527 398 KANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSpTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLIKV 475
Cdd:cd07143   405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYN-LLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
 8-474 6.60e-132

NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.


Pssm-ID: 143459  Cd Length: 481  Bit Score: 390.17  E-value: 6.60e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   8 TRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAF---PAWSALSPKERSVYLARLGVLFAEHS 84
Cdd:cd07141     7 TKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  85 AELAQLEAKSMGRPVT--SFFDAGAASDYFRYFSEAAYPMGTSSLNTPG-FVNMGVKQPYGVCGIIIPWNAPLIFFSKKG 161
Cdd:cd07141    87 AYLASLETLDNGKPFSksYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGdFFTYTRHEPVGVCGQIIPWNFPLLMAAWKL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 162 AAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAAD 240
Cdd:cd07141   167 APALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPtAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGK 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 241 SNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGT 320
Cdd:cd07141   247 SNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKT 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 321 TQGPQADKVQHETVKRYLALAEKSGTKIT---EDLPNVsGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIA 397
Cdd:cd07141   327 EQGPQIDEEQFKKILELIESGKKEGAKLEcggKRHGDK-GYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIE 405

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1069468527 398 KANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTkGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLIK 474
Cdd:cd07141   406 RANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVV-SPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
 10-473 1.90e-131

Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.


Pssm-ID: 143457 [Multi-domain]  Cd Length: 471  Bit Score: 388.47  E-value: 1.90e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  10 LFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAF--PAWSALSPKERSVYLARLGVLFAEHSAEL 87
Cdd:cd07139     1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  88 AQLEAKSMGRPVTSF--FDAGAASDYFRYFSEAAYPMGTSSLNTPGFVNMG--VKQPYGVCGIIIPWNAPLIFFSKKGAA 163
Cdd:cd07139    81 ARLWTAENGMPISWSrrAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVlvRREPVGVVAAIVPWNAPLFLAALKIAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 164 ALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNL 243
Cdd:cd07139   161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE-RL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 244 KNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQG 323
Cdd:cd07139   240 ARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 324 PQADKVQHETVKRYLALAEKSGTKIT------EDLPNvsGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIA 397
Cdd:cd07139   320 PLASARQRERVEGYIAKGRAEGARLVtgggrpAGLDR--GWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1069468527 398 KANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNcsSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07139   398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN--GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
 8-472 3.26e-129

Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.


Pssm-ID: 143460  Cd Length: 476  Bit Score: 383.00  E-value: 3.26e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   8 TRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFP--AWSALSPKERSVYLARLGVLFAEHSA 85
Cdd:cd07142     4 TKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHAD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  86 ELAQLEAKSMGRP--VTSFFDAGAASDYFRYFSEAAYPMGTSSLNTPG-FVNMGVKQPYGVCGIIIPWNAPLIFFSKKGA 162
Cdd:cd07142    84 ELAALETWDNGKPyeQARYAEVPLAARLFRYYAGWADKIHGMTLPADGpHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 163 AALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADS 241
Cdd:cd07142   164 PALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPtAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKS 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 242 NLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTT 321
Cdd:cd07142   244 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 322 QGPQADKVQHETVKRYLALAEKSGTKITE--DLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKA 399
Cdd:cd07142   324 QGPQVDKEQFEKILSYIEHGKEEGATLITggDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRA 403

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1069468527 400 NDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGnDMPFGGWKGSGIGRESYIGGVESFMEDKAVL 472
Cdd:cd07142   404 NNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDA-SIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
 29-473 9.60e-129

Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.


Pssm-ID: 143411 [Multi-domain]  Cd Length: 450  Bit Score: 380.90  E-value: 9.60e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  29 SPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRP--VTSFFDAG 106
Cdd:cd07092     3 DPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPlhLVRDDELP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 107 AASDYFRYFSEAAYPMGTSSLN--TPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCA 184
Cdd:cd07092    83 GAVDNFRFFAGAARTLEGPAAGeyLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 185 KAAELVAKaGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDAD 263
Cdd:cd07092   163 LLAELAAE-VLPPGVVNVVCGGGAsAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAPVIVFDDAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 264 IEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEK 343
Cdd:cd07092   241 LDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAPA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 344 -----SGTKITEDlpnvSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRA 418
Cdd:cd07092   321 harvlTGGRRAEG----PGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRA 396

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1069468527 419 MRVSKQLEAGTVGVNCSSPTKgNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07092   397 MRLSARLDFGTVWVNTHIPLA-AEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
 29-475 1.21e-126

Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.


Pssm-ID: 143433 [Multi-domain]  Cd Length: 453  Bit Score: 375.62  E-value: 1.21e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  29 SPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPV--TSFFDAG 106
Cdd:cd07115     3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIraARRLDVP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 107 AASDYFRYFSEAAYPMGTSSLNT-PGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAK 185
Cdd:cd07115    83 RAADTFRYYAGWADKIEGEVIPVrGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 186 AAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADI 264
Cdd:cd07115   163 IAELMAEAGFPAGVLNVVTGFGEvAGAALVEHPDVDKITFTGSTAVGRKIMQGAAG-NLKRVSLELGGKSANIVFADADL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 265 EQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKS 344
Cdd:cd07115   242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 345 GTKITE--DLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVS 422
Cdd:cd07115   322 GARLLTggKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVA 401

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1069468527 423 KQLEAGTVGVNCSSPTKgNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLIKV 475
Cdd:cd07115   402 AALKAGTVWINTYNRFD-PGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
 58-473 3.59e-126

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143395 [Multi-domain]  Cd Length: 367  Bit Score: 371.56  E-value: 3.59e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  58 FPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVTSF-FDAGAASDYFRYFSEAAY-PMGTSSLNT-PGFVN 134
Cdd:cd06534     7 FKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAlGEVARAIDTFRYAAGLADkLGGPELPSPdPGGEA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 135 MGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVM 213
Cdd:cd06534    87 YVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDeVGAAL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 214 SSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHK 293
Cdd:cd06534   167 LSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 294 SIAQTFIEGFKtkfmsaklgdptqagttqgpqadkvqhetvkrylalaeksgtkitedlpnvsglyispTIFTDTPEDAQ 373
Cdd:cd06534   246 SIYDEFVEKLV----------------------------------------------------------TVLVDVDPDMP 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 374 IMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGI 453
Cdd:cd06534   268 IAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFGGVKNSGI 347

                         410       420
                  ....*....|....*....|
gi 1069468527 454 GRESYIGGVESFMEDKAVLI 473
Cdd:cd06534   348 GREGGPYGLEEYTRTKTVVI 367
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
 30-472 3.79e-126

Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.


Pssm-ID: 143428 [Multi-domain]  Cd Length: 456  Bit Score: 374.77  E-value: 3.79e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  30 PSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPV-TSFFDAGAA 108
Cdd:cd07110     4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLdEAAWDVDDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 109 SDYFRYFSEAAYPMGTSS-----LNTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTC 183
Cdd:cd07110    84 AGCFEYYADLAEQLDAKAeravpLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 184 AKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAAdSNLKNCIFELGGKSPALVFEDA 262
Cdd:cd07110   164 LELAEIAAEAGLPPGVLNVVTGTGDeAGAPLAAHPGIDKISFTGSTATGSQVMQAAA-QDIKPVSLELGGKSPIIVFDDA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 263 DIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAE 342
Cdd:cd07110   243 DLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGK 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 343 KSGTKIT------EDLPnvSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDID 416
Cdd:cd07110   323 EEGARLLcggrrpAHLE--KGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1069468527 417 RAMRVSKQLEAGTVGVNCSSPTKgNDMPFGGWKGSGIGRESYIGGVESFMEDKAVL 472
Cdd:cd07110   401 RCDRVAEALEAGIVWINCSQPCF-PQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
 29-473 3.79e-125

Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.


Pssm-ID: 143425 [Multi-domain]  Cd Length: 456  Bit Score: 372.09  E-value: 3.79e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  29 SPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVTSFF-DAGA 107
Cdd:cd07107     3 NPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLgDVMV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 108 ASDYFRYFSEAAYPMGTSSL-NTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKA 186
Cdd:cd07107    83 AAALLDYFAGLVTELKGETIpVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 187 AELVAKAgFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADSnLKNCIFELGGKSPALVFEDADIE 265
Cdd:cd07107   163 AELAREV-LPPGVFNILPGDGAtAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFPDADPE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 266 QAIQATVPSI--GWnSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEK 343
Cdd:cd07107   241 AAADAAVAGMnfTW-CGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 344 SGTKI--------TEDLPNvsGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDI 415
Cdd:cd07107   320 EGARLvtgggrpeGPALEG--GFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1069468527 416 DRAMRVSKQLEAGTVGVNCSSpTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07107   398 SQAHRTARRVEAGYVWINGSS-RHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
 27-473 4.82e-125

Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.


Pssm-ID: 143427 [Multi-domain]  Cd Length: 454  Bit Score: 371.57  E-value: 4.82e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  27 LHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPA-WSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVT-SFFD 104
Cdd:cd07109     1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTqARAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 105 AGAASDYFRYFSEAA-------YPMGtsslntPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSE 177
Cdd:cd07109    81 VEAAARYFEYYGGAAdklhgetIPLG------PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 178 KAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPA 256
Cdd:cd07109   155 DAPLTALRLAELAEEAGLPAGALNVVTGLGAeAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQ 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 257 LVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGdPTQAGTTQGPQADKVQHETVKR 336
Cdd:cd07109   234 IVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEG 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 337 YLALAEKSGTKIT-----EDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVF 411
Cdd:cd07109   313 FVARARARGARIVaggriAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVW 392

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1069468527 412 TKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07109   393 TRDGDRALRVARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
 11-473 9.37e-125

Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.


Pssm-ID: 143407 [Multi-domain]  Cd Length: 468  Bit Score: 371.60  E-value: 9.37e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  11 FINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQL 90
Cdd:cd07088     1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  91 EAKSMGRPVT-SFFDAGAASDYFRYFSEAAYP-----MGTSSLNTPGFVNmgvKQPYGVCGIIIPWNAPLIFFSKKGAAA 164
Cdd:cd07088    81 IVEEQGKTLSlARVEVEFTADYIDYMAEWARRiegeiIPSDRPNENIFIF---KVPIGVVAGILPWNFPFFLIARKLAPA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 165 LAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNL 243
Cdd:cd07088   158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSvVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-NI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 244 KNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQG 323
Cdd:cd07088   237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMG 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 324 P-----QADKVqHETVKRylalAEKSGTKIT---EDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEA 395
Cdd:cd07088   317 PlvneaALDKV-EEMVER----AVEAGATLLtggKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEA 391

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1069468527 396 IAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMpFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07088   392 IELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGF-HAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
8-474 5.94e-124

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 369.62  E-value: 5.94e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   8 TRLFINGKFQAiDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAEL 87
Cdd:PRK13473    3 TKLLINGELVA-GEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  88 AQLEAKSMGRPV--TSFFDAGAASDYFRYFSEAAYPMGTSSLN--TPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAA 163
Cdd:PRK13473   82 ARLESLNCGKPLhlALNDEIPAIVDVFRFFAGAARCLEGKAAGeyLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 164 ALAAGNTVVLKSSEKAPLTCAKAAELVAKAgFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADSn 242
Cdd:PRK13473  162 ALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGAtVGDALVGHPKVRMVSLTGSIATGKHVLSAAADS- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 243 LKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQ 322
Cdd:PRK13473  240 VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTEL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 323 GPQADKVQHETVKRYL--ALAEKSGTKIT-EDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKA 399
Cdd:PRK13473  320 GPLISAAHRDRVAGFVerAKALGHIRVVTgGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWA 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1069468527 400 NDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKgNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLIK 474
Cdd:PRK13473  400 NDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLV-SEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
 8-478 1.64e-122

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 367.98  E-value: 1.64e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   8 TRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFP--AWSALSPKERSVYLARLGVLFAEHSA 85
Cdd:PLN02466   58 TQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHND 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  86 ELAQLEAKSMGRPV--TSFFDAGAASDYFRYFseAAYPMGTSSLNTPGFVNMGVK---QPYGVCGIIIPWNAPLIFFSKK 160
Cdd:PLN02466  138 ELAALETWDNGKPYeqSAKAELPMFARLFRYY--AGWADKIHGLTVPADGPHHVQtlhEPIGVAGQIIPWNFPLLMFAWK 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 161 GAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAA 239
Cdd:PLN02466  216 VGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPtAGAALASHMDVDKLAFTGSTDTGKIVLELAA 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 240 DSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAG 319
Cdd:PLN02466  296 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKG 375

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 320 TTQGPQADKVQHETVKRYLALAEKSGTKITE--DLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIA 397
Cdd:PLN02466  376 VEQGPQIDSEQFEKILRYIKSGVESGATLECggDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIR 455

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 398 KANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNdMPFGGWKGSGIGRESYIGGVESFMEDKAVlikVAP 477
Cdd:PLN02466  456 RANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAA-IPFGGYKMSGIGREKGIYSLNNYLQVKAV---VTP 531


                  .
gi 1069468527 478 L 478
Cdd:PLN02466  532 L 532
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
 30-473 2.06e-121

Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.


Pssm-ID: 143424 [Multi-domain]  Cd Length: 446  Bit Score: 362.23  E-value: 2.06e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  30 PSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVT-SFFDAGAA 108
Cdd:cd07106     4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAeAQFEVGGA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 109 SDYFRYFSEAAYPMGTSSLNTPGFVNMgVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAE 188
Cdd:cd07106    84 VAWLRYTASLDLPDEVIEDDDTRRVEL-RRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 189 LVAKAgFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADIEqai 268
Cdd:cd07106   163 LAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVLPDVDID--- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 269 qATVPSIGW----NSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKS 344
Cdd:cd07106   238 -AVAPKLFWgafiNSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAK 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 345 GTKITE--DLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVS 422
Cdd:cd07106   317 GAKVLAggEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVA 396

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1069468527 423 KQLEAGTVGVNCS---SPtkgnDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07106   397 RRLEAGTVWINTHgalDP----DAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
 8-478 4.78e-121

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 362.99  E-value: 4.78e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   8 TRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFP--AWSALSPKERSVYLARLGVLFAEHSA 85
Cdd:PLN02766   21 TKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  86 ELAQLEAKSMGRPVT--SFFDAGAASDYFRYFSEAAYPMGTSSLNTPG-FVNMGVKQPYGVCGIIIPWNAPLIFFSKKGA 162
Cdd:PLN02766  101 ELAALDTIDAGKLFAlgKAVDIPAAAGLLRYYAGAADKIHGETLKMSRqLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 163 AALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHG-AAGAVMSSHMDIRIISFTGSTRTGRAIQKAAADS 241
Cdd:PLN02766  181 PALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGpTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATS 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 242 NLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTT 321
Cdd:PLN02766  261 NLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRAR 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 322 QGPQADKVQHETVKRYLALAEKSG-TKITEDLP-NVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKA 399
Cdd:PLN02766  341 QGPQVDKQQFEKILSYIEHGKREGaTLLTGGKPcGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKA 420

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1069468527 400 NDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSpTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVlikVAPL 478
Cdd:PLN02766  421 NNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYF-AFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV---VTPL 495
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
 28-471 3.54e-120

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.


Pssm-ID: 143408 [Multi-domain]  Cd Length: 459  Bit Score: 359.25  E-value: 3.54e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  28 HSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWS-ALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVTS---FF 103
Cdd:cd07089     2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTaraMQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 104 DAGAAsDYFRYFSEAA----YPMGTSSLNTPGFVNMGV--KQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSE 177
Cdd:cd07089    82 VDGPI-GHLRYFADLAdsfpWEFDLPVPALRGGPGRRVvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 178 KAPLTCAKAAELVAKAGFPPGVFNILSGHG-AAGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPA 256
Cdd:cd07089   161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDnAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSAN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 257 LVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKR 336
Cdd:cd07089   240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 337 YLALAEKSGTKIT------EDLPNvsGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASV 410
Cdd:cd07089   320 YIARGRDEGARLVtgggrpAGLDK--GFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1069468527 411 FTKDIDRAMRVSKQLEAGTVGVNcSSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAV 471
Cdd:cd07089   398 WSADVDRAYRVARRIRTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
 29-473 8.07e-119

Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.


Pssm-ID: 143426  Cd Length: 457  Bit Score: 355.90  E-value: 8.07e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  29 SPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMG-------RPvts 101
Cdd:cd07108     3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGnalrtqaRP--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 102 ffDAGAASDYFRYF----SEA---AYPMGtsslntPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLK 174
Cdd:cd07108    80 --EAAVLADLFRYFgglaGELkgeTLPFG------PDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 175 SSEKAPLTCAKAAELVAKAgFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGK 253
Cdd:cd07108   152 AAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEeCGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGK 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 254 SPALVFEDADIEQAIQATVPSIGWN-SGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHE 332
Cdd:cd07108   230 SPMIVFPDADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFA 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 333 TVKRYLALA-EKSGTKI------TEDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYG 405
Cdd:cd07108   310 KVCGYIDLGlSTSGATVlrggplPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYG 389

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 406 LYASVFTKDIDRAMRVSKQLEAGTVGVN-CSSPTKGndMPFGGWKGSGIGRE-SYIGGVESFMEDKAVLI 473
Cdd:cd07108   390 LAAYVWTRDLGRALRAAHALEAGWVQVNqGGGQQPG--QSYGGFKQSGLGREaSLEGMLEHFTQKKTVNI 457
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
 30-473 1.75e-118

NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.


Pssm-ID: 143409 [Multi-domain]  Cd Length: 457  Bit Score: 355.07  E-value: 1.75e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  30 PSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPV-TSFFDAGAA 108
Cdd:cd07090     4 PATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIeEARVDIDSS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 109 SDYFRYFSEAAYPMGTSSLNTPG--FVNMGvKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKA 186
Cdd:cd07090    84 ADCLEYYAGLAPTLSGEHVPLPGgsFAYTR-REPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 187 AELVAKAGFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADIEQ 266
Cdd:cd07090   163 AEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK-GIKHVTLELGGKSPLIIFDDADLEN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 267 AIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGF--KTKFMsaKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKS 344
Cdd:cd07090   242 AVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLveRTKKI--RIGDPLDEDTQMGALISEEHLEKVLGYIESAKQE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 345 GTKI-------TEDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDR 417
Cdd:cd07090   320 GAKVlcggervVPEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQR 399

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1069468527 418 AMRVSKQLEAGTVGVNC--SSPTkgnDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07090   400 AHRVIAQLQAGTCWINTynISPV---EVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
 28-473 9.70e-118

Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.


Pssm-ID: 143436 [Multi-domain]  Cd Length: 454  Bit Score: 353.18  E-value: 9.70e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  28 HSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPA--WSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVT-SFFD 104
Cdd:cd07118     2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISqARGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 105 AGAASDYFRYFSEAAYPMGTSSLNT--PGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLT 182
Cdd:cd07118    82 IEGAADLWRYAASLARTLHGDSYNNlgDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 183 CAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFED 261
Cdd:cd07118   162 TLMLAELLIEAGLPAGVVNIVTGYGAtVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFAD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 262 ADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALA 341
Cdd:cd07118   241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 342 EKSGTKIT---EDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRA 418
Cdd:cd07118   321 RAEGATLLlggERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1069468527 419 MRVSKQLEAGTVGVNC---SSPtkgnDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07118   401 LTVARRIRAGTVWVNTfldGSP----ELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
 1-478 2.55e-117

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 353.03  E-value: 2.55e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   1 MSASPiETRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLF 80
Cdd:PRK13252    1 MSRQP-LQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDIL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  81 AEHSAELAQLEAKSMGRPV--TSFFDAGAASDYFRYFSEAAyPM--GTS-SLNTPGFVnMGVKQPYGVCGIIIPWNAPLI 155
Cdd:PRK13252   80 RERNDELAALETLDTGKPIqeTSVVDIVTGADVLEYYAGLA-PAleGEQiPLRGGSFV-YTRREPLGVCAGIGAWNYPIQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 156 FFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRAIQ 235
Cdd:PRK13252  158 IACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 236 KAAADSnLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDP 315
Cdd:PRK13252  238 AAAAAS-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDP 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 316 TQAGTTQGPQADKVQHETVKRYLALAEKSG-------TKITED-LPNvsGLYISPTIFTDTPEDAQIMKEEIFGPVVHIN 387
Cdd:PRK13252  317 MDPATNFGPLVSFAHRDKVLGYIEKGKAEGarllcggERLTEGgFAN--GAFVAPTVFTDCTDDMTIVREEIFGPVMSVL 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 388 TFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNC--SSPTkgnDMPFGGWKGSGIGRESYIGGVESF 465
Cdd:PRK13252  395 TFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgESPA---EMPVGGYKQSGIGRENGIATLEHY 471

                         490
                  ....*....|...
gi 1069468527 466 MEDKAVLIKVAPL 478
Cdd:PRK13252  472 TQIKSVQVEMGPF 484
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
 25-473 7.02e-117

Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.


Pssm-ID: 143468 [Multi-domain]  Cd Length: 451  Bit Score: 350.86  E-value: 7.02e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  25 FDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPV-TSFF 103
Cdd:cd07150     1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYgKAWF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 104 DAGAASDYFRYFSEAAYPMGTSSL--NTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPL 181
Cdd:cd07150    81 ETTFTPELLRAAAGECRRVRGETLpsDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 182 TCAKAAELVAKAGFPPGVFNILSGHGAA-GAVMSSHMDIRIISFTGSTRTGRAIQKAAAdSNLKNCIFELGGKSPALVFE 260
Cdd:cd07150   161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEvGDELVDDPRVRMVTFTGSTAVGREIAEKAG-RHLKKITLELGGKNPLIVLA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 261 DADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLAL 340
Cdd:cd07150   240 DADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVED 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 341 AEKSGTKI----TEDlpnvsGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDID 416
Cdd:cd07150   320 AVAKGAKLltggKYD-----GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQ 394

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1069468527 417 RAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07150   395 RAFKLAERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
PLN02467 PLN02467
betaine aldehyde dehydrogenase
 3-471 1.04e-116

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 352.11  E-value: 1.04e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   3 ASPIETR-LFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPA-----WSALSPKERSVYLARL 76
Cdd:PLN02467    2 AIPVPRRqLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  77 GVLFAEHSAELAQLEAKSMGRPVTS----FFDAGAASDYFRYFSEA--AYPMGTSSLNTPGFVNMGVKQPYGVCGIIIPW 150
Cdd:PLN02467   82 AAKITERKSELAKLETLDCGKPLDEaawdMDDVAGCFEYYADLAEAldAKQKAPVSLPMETFKGYVLKEPLGVVGLITPW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 151 NAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTR 229
Cdd:PLN02467  162 NYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTeAGAPLASHPGVDKIAFTGSTA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 230 TGRAIQKAAAdSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMS 309
Cdd:PLN02467  242 TGRKIMTAAA-QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKN 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 310 AKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKI----TEDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVH 385
Cdd:PLN02467  321 IKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATIlcggKRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLC 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 386 INTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNdMPFGGWKGSGIGRESYIGGVESF 465
Cdd:PLN02467  401 VKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQ-APWGGIKRSGFGRELGEWGLENY 479


                  ....*.
gi 1069468527 466 MEDKAV 471
Cdd:PLN02467  480 LSVKQV 485
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
 10-473 1.09e-116

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.


Pssm-ID: 143471 [Multi-domain]  Cd Length: 480  Bit Score: 351.26  E-value: 1.09e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  10 LFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQ 89
Cdd:cd07559     3 NFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  90 LEAKSMGRPV--TSFFDAGAASDYFRYFSEAAYPM-GTSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALA 166
Cdd:cd07559    83 AETLDNGKPIreTLAADIPLAIDHFRYFAGVIRAQeGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 167 AGNTVVLKSSEKAPLTCAKAAELVAKAgFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKN 245
Cdd:cd07559   163 AGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSeAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE-NLIP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 246 CIFELGGKSPALVFEDA-----DIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGT 320
Cdd:cd07559   241 VTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPET 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 321 TQGPQADKVQHETVKRYLALAEKSGTKI--------TEDLPNvsGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGE 392
Cdd:cd07559   321 MMGAQVSKDQLEKILSYVDIGKEEGAEVltggerltLGGLDK--GYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 393 AEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNC--SSPTKGndmPFGGWKGSGIGRESYIGGVESFMEDKA 470
Cdd:cd07559   399 EEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCyhQYPAHA---PFGGYKKSGIGRETHKMMLDHYQQTKN 475


                  ...
gi 1069468527 471 VLI 473
Cdd:cd07559   476 ILV 478
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
 11-469 1.73e-115

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 347.57  E-value: 1.73e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  11 FINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQL 90
Cdd:TIGR01804   1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  91 EAKSMGRPV--TSFFDAGAASDYFRYFSEAAYPMGTSSLNTPG--FVNMgVKQPYGVCGIIIPWNAPLIFFSKKGAAALA 166
Cdd:TIGR01804  81 ETLDTGKTLqeTIVADMDSGADVFEFFAGLAPALNGEIIPLGGpsFAYT-IREPLGVCVGIGAWNYPLQIASWKIAPALA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 167 AGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAA-GAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKN 245
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEvGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAG-HLKH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 246 CIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQ 325
Cdd:TIGR01804 239 VTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 326 ADKVQHETVKRYLALAEKSGTKITE--DLPNVSGL----YISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKA 399
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATggGRPENVGLqngfFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 400 NDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGnDMPFGGWKGSGIGRESYIGGVESFMEDK 469
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPA-EAPFGGYKQSGIGRENGKAALAHYTEVK 467
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
 6-474 8.69e-113

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.


Pssm-ID: 143458 [Multi-domain]  Cd Length: 486  Bit Score: 341.40  E-value: 8.69e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   6 IETRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPA--WSALSPKERSVYLARLGVLFAEH 83
Cdd:cd07140     4 MPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  84 SAELAQLEAKSMGRPVTSFFDA--GAASDYFRYFSE-------AAYPMGTSSLNTPgfVNMGVKQPYGVCGIIIPWNAPL 154
Cdd:cd07140    84 QEELATIESLDSGAVYTLALKThvGMSIQTFRYFAGwcdkiqgKTIPINQARPNRN--LTLTKREPIGVCGIVIPWNYPL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 155 IFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRA 233
Cdd:cd07140   162 MMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSlVGQRLSDHPDVRKLGFTGSTPIGKH 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 234 IQKAAADSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLG 313
Cdd:cd07140   242 IMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 314 DPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKITEDLPNV--SGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTF-E 390
Cdd:cd07140   322 DPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVdrPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFdD 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 391 GEAEAIAK-ANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTkgnDM--PFGGWKGSGIGRESYIGGVESFME 467
Cdd:cd07140   402 GDVDGVLQrANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKT---DVaaPFGGFKQSGFGKDLGEEALNEYLK 478


                  ....*..
gi 1069468527 468 DKAVLIK 474
Cdd:cd07140   479 TKTVTIE 485
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
 3-473 1.42e-112

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 341.11  E-value: 1.42e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   3 ASPIETRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPA--WSALSPKERSVYLARLGVLF 80
Cdd:PRK09847   15 SLAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLM 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  81 AEHSAELAQLEAKSMGRPVTSFF--DAGAASDYFRYFSEAAYPM-GTSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFF 157
Cdd:PRK09847   95 EAHAEELALLETLDTGKPIRHSLrdDIPGAARAIRWYAEAIDKVyGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 158 SKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHG-AAGAVMSSHMDIRIISFTGSTRTGRAIQK 236
Cdd:PRK09847  175 CWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGhEAGQALSRHNDIDAIAFTGSTRTGKQLLK 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 237 AAADSNLKNCIFELGGKSPALVFEDA-DIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDP 315
Cdd:PRK09847  255 DAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHP 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 316 TQAGTTQGPQADKVQHETVKRYLALAEKSGTKITEDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEA 395
Cdd:PRK09847  335 LDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQA 414

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 396 IAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSptkGNDM--PFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:PRK09847  415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYN---DGDMtvPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
 58-473 3.98e-112

ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.


Pssm-ID: 143422 [Multi-domain]  Cd Length: 431  Bit Score: 337.97  E-value: 3.98e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  58 FPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVT-SFFDAGAASDYFRyfsEAA----YPMG-TSSLNTPG 131
Cdd:cd07104    13 QKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPkAAFEVGAAIAILR---EAAglprRPEGeILPSDVPG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 132 FVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCA-KAAELVAKAGFPPGVFNILSGHGA-A 209
Cdd:cd07104    90 KESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGlLIAEIFEEAGLPKGVLNVVPGGGSeI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 210 GAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRI 289
Cdd:cd07104   170 GDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRI 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 290 YVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKI----TEDlpnvsGLYISPTIF 365
Cdd:cd07104   249 LVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLltggTYE-----GLFYQPTVL 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 366 TDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPF 445
Cdd:cd07104   324 SDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDEPHVPF 403

                         410       420
                  ....*....|....*....|....*...
gi 1069468527 446 GGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07104   404 GGVKASGGGRFGGPASLEEFTEWQWITV 431
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
 9-467 7.88e-111

Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.


Pssm-ID: 143429 [Multi-domain]  Cd Length: 480  Bit Score: 336.29  E-value: 7.88e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   9 RLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELA 88
Cdd:cd07111    23 GHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  89 QLEAKSMGRPV--TSFFDAGAASDYFRYFSEAAYPMGTSslntpgfvnMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALA 166
Cdd:cd07111   103 VLESLDNGKPIreSRDCDIPLVARHFYHHAGWAQLLDTE---------LAGWKPVGVVGQIVPWNFPLLMLAWKICPALA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 167 AGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRAIQKAAADSNlKNC 246
Cdd:cd07111   174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTG-KKL 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 247 IFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQA 326
Cdd:cd07111   253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIV 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 327 DKVQHETVKRYLALAEKSGTKI--TEDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEY 404
Cdd:cd07111   333 DPAQLKRIRELVEEGRAEGADVfqPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPY 412

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1069468527 405 GLYASVFTKDIDRAMRVSKQLEAGTVGVNCSS---PTkgndMPFGGWKGSGIGREsyiGGVESFME 467
Cdd:cd07111   413 GLAASVWSENLSLALEVALSLKAGVVWINGHNlfdAA----AGFGGYRESGFGRE---GGKEGLYE 471
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
 2-471 1.07e-110

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 336.28  E-value: 1.07e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   2 SASPIETRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFA 81
Cdd:PLN02278   19 NAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLII 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  82 EHSAELAQLEAKSMGRPVTSFFD--AGAASdYFRYF-SEAAYPMG----TSSLNTPGFVnmgVKQPYGVCGIIIPWNAPL 154
Cdd:PLN02278   99 ANKEDLAQLMTLEQGKPLKEAIGevAYGAS-FLEYFaEEAKRVYGdiipSPFPDRRLLV---LKQPVGVVGAITPWNFPL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 155 IFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAA-GAVMSSHMDIRIISFTGSTRTGRA 233
Cdd:PLN02278  175 AMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEiGDALLASPKVRKITFTGSTAVGKK 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 234 IQKAAADSnLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLG 313
Cdd:PLN02278  255 LMAGAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVG 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 314 DPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKITEDLPNVS--GLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEG 391
Cdd:PLN02278  334 DGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSlgGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKT 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 392 EAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNcSSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAV 471
Cdd:PLN02278  414 EEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVN-EGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
 11-473 1.35e-108

Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.


Pssm-ID: 143449 [Multi-domain]  Cd Length: 478  Bit Score: 330.46  E-value: 1.35e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  11 FINGKFQAIDESQTFDLHSPSTG-EFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQ 89
Cdd:cd07131     2 YIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  90 LEAKSMGRPVT-SFFDAGAASDYFRY-FSEAAYPMG-TSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALA 166
Cdd:cd07131    82 LVTREMGKPLAeGRGDVQEAIDMAQYaAGEGRRLFGeTVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 167 AGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHG-AAGAVMSSHMDIRIISFTGSTRTGRAIQKAAADSNlKN 245
Cdd:cd07131   162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGeEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN-KR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 246 CIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQ 325
Cdd:cd07131   241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 326 ADKVQHETVKRYLALAEKSGTK-------ITEDLPNvSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAK 398
Cdd:cd07131   321 INEAQLEKVLNYNEIGKEEGATlllggerLTGGGYE-KGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1069468527 399 ANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNcsSPTKGND--MPFGGWKGSGIG-RESYIGGVESFMEDKAVLI 473
Cdd:cd07131   400 ANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN--APTIGAEvhLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
 10-474 4.73e-108

Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.


Pssm-ID: 143431  Cd Length: 477  Bit Score: 329.02  E-value: 4.73e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  10 LFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAF-PAWSALSPKERSVYLARLGVLFAEHSAELA 88
Cdd:cd07113     2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  89 QLEAKSMGRP--VTSFFDAGAASDYFRYFSEAAYPMGTSSLNtPGFVNMG--------VKQPYGVCGIIIPWNAPLIFFS 158
Cdd:cd07113    82 QLETLCSGKSihLSRAFEVGQSANFLRYFAGWATKINGETLA-PSIPSMQgerytaftRREPVGVVAGIVPWNFSVMIAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 159 KKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRAIQKAA 238
Cdd:cd07113   161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 239 AdSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQA 318
Cdd:cd07113   241 A-SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 319 GTTQGPQADKVQHETVKRYLALAEKSGTKITE--DLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAI 396
Cdd:cd07113   320 SVMFGPLANQPHFDKVCSYLDDARAEGDEIVRggEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELI 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1069468527 397 AKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNdMPFGGWKGSGIGRESYIGGVESFMEDKAVLIK 474
Cdd:cd07113   400 QLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPA-VPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
 25-473 1.22e-107

Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.


Pssm-ID: 143463 [Multi-domain]  Cd Length: 456  Bit Score: 327.00  E-value: 1.22e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  25 FDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPV-TSFF 103
Cdd:cd07145     1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIkQSRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 104 DAGAASDYFRYFSEAA-------YPMGTSSLNTPGFVnMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSS 176
Cdd:cd07145    81 EVERTIRLFKLAAEEAkvlrgetIPVDAYEYNERRIA-FTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 177 EKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAAdSNLKNCIFELGGKSP 255
Cdd:cd07145   160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSeVGDEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGGSDP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 256 ALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVK 335
Cdd:cd07145   239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 336 RYLALAEKSGTKITEDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDI 415
Cdd:cd07145   319 NLVNDAVEKGGKILYGGKRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDI 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1069468527 416 DRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07145   399 NRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
 10-473 4.68e-107

Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.


Pssm-ID: 143435  Cd Length: 475  Bit Score: 326.33  E-value: 4.68e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  10 LFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQ 89
Cdd:cd07117     3 LFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  90 LEAKSMGRPV--TSFFDAGAASDYFRYFSEAAYPM-GTSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALA 166
Cdd:cd07117    83 VETLDNGKPIreTRAVDIPLAADHFRYFAGVIRAEeGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 167 AGNTVVLKSSEKAPLTCAKAAELVAKAgFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKN 245
Cdd:cd07117   163 AGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSkSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK-KLIP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 246 CIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQ 325
Cdd:cd07117   241 ATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQ 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 326 ADKVQHETVKRYLALAEKSGTKI-------TEDlPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAK 398
Cdd:cd07117   321 VNKDQLDKILSYVDIAKEEGAKIltgghrlTEN-GLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDM 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1069468527 399 ANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNdMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07117   400 ANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAG-APFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
 10-471 2.92e-105

Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.


Pssm-ID: 143442  Cd Length: 512  Bit Score: 323.02  E-value: 2.92e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  10 LFINGKfqAIDESQTFDLHSPS-TGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELA 88
Cdd:cd07124    35 LVIGGK--EVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  89 QLEAKSMGRP-VTSFFDAGAASDYFRYFSEAAYPM-GTSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALA 166
Cdd:cd07124   113 AWMVLEVGKNwAEADADVAEAIDFLEYYAREMLRLrGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALV 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 167 AGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAA-GAVMSSHMDIRIISFTGSTRTGRAIQKAAA-----D 240
Cdd:cd07124   193 TGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEvGDYLVEHPDVRFIAFTGSREVGLRIYERAAkvqpgQ 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 241 SNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGT 320
Cdd:cd07124   273 KWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEV 352

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 321 TQGPQADKVQHETVKRYLALAEKSGTKITEDLP---NVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIA 397
Cdd:cd07124   353 YMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVlelAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALE 432

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 398 KANDTEYGLYASVFTKD---IDRAMRvskQLEAGTVGVN--CSSPTKGNDmPFGGWKGSGIGreSYIGG---VESFMEDK 469
Cdd:cd07124   433 IANDTEYGLTGGVFSRSpehLERARR---EFEVGNLYANrkITGALVGRQ-PFGGFKMSGTG--SKAGGpdyLLQFMQPK 506


                  ..
gi 1069468527 470 AV 471
Cdd:cd07124   507 TV 508
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
 11-471 3.09e-105

Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.


Pssm-ID: 143415 [Multi-domain]  Cd Length: 473  Bit Score: 321.51  E-value: 3.09e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  11 FINGKFQAIDEsqTFDLHSPS-TGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQ 89
Cdd:cd07097     4 YIDGEWVAGGD--GEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  90 LEAKSMGRPVT-SFFDAGAASDYFRYFSEAAYPMGTSSLNT--PGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALA 166
Cdd:cd07097    82 LLTREEGKTLPeARGEVTRAGQIFRYYAGEALRLSGETLPStrPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 167 AGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAA-GAVMSSHMDIRIISFTGSTRTGRAIQkAAADSNLKN 245
Cdd:cd07097   162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEvGQALVEHPDVDAVSFTGSTAVGRRIA-AAAAARGAR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 246 CIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQ 325
Cdd:cd07097   241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 326 ADKVQHETVKRYLALAEKSGTKITE-----DLPNvSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKAN 400
Cdd:cd07097   321 VSERQLEKDLRYIEIARSEGAKLVYggerlKRPD-EGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069468527 401 DTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCssPTKGND--MPFGGWKGSGIG-RESYIGGVESFMEDKAV 471
Cdd:cd07097   400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNL--PTAGVDyhVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
 58-473 4.47e-105

Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.


Pssm-ID: 143423 [Multi-domain]  Cd Length: 432  Bit Score: 319.91  E-value: 4.47e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  58 FPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPV-TSFFDAGAASDYFRYFSEAAYPMGTSSLNT--PGFVN 134
Cdd:cd07105    13 FPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAaWAGFNVDLAAGMLREAASLITQIIGGSIPSdkPGTLA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 135 MGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSgHGAAGA--- 211
Cdd:cd07105    93 MVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVT-HSPEDApev 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 212 --VMSSHMDIRIISFTGSTRTGRAIQKAAAdSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRI 289
Cdd:cd07105   172 veALIAHPAVRKVNFTGSTRVGRIIAETAA-KHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERI 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 290 YVHKSIAQTFIEGFKTKFMSAKLGDptqagTTQGPQADKVQHETVKRYLALAEKSGTKI---TEDLPNVSGLYISPTIFT 366
Cdd:cd07105   251 IVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLvvgGLADESPSGTSMPPTILD 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 367 DTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNcsSPTKGND--MP 444
Cdd:cd07105   326 NVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN--GMTVHDEptLP 403

                         410       420
                  ....*....|....*....|....*....
gi 1069468527 445 FGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07105   404 HGGVKSSGYGRFNGKWGIDEFTETKWITI 432
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
 28-467 4.38e-104

Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.


Pssm-ID: 143417 [Multi-domain]  Cd Length: 453  Bit Score: 318.01  E-value: 4.38e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  28 HSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVTsffDAGA 107
Cdd:cd07099     1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRA---DAGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 108 ----ASDYFRYFSEAA-----YPMGTSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEK 178
Cdd:cd07099    78 evllALEAIDWAARNAprvlaPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 179 APLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSSHMdIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALV 258
Cdd:cd07099   158 TPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPMIV 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 259 FEDADIEQAIQATVpsigW----NSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETV 334
Cdd:cd07099   236 LADADLERAAAAAV----WgamvNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 335 KRYLALAEKSGTKIT--EDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFT 412
Cdd:cd07099   312 RRHVDDAVAKGAKALtgGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1069468527 413 KDIDRAMRVSKQLEAGTVGVNCSSPTKGN-DMPFGGWKGSGIGResyIGGVESFME 467
Cdd:cd07099   392 RDLARAEAIARRLEAGAVSINDVLLTAGIpALPFGGVKDSGGGR---RHGAEGLRE 444
SSADH TIGR01780
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ...
 30-469 6.82e-103

succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]


Pssm-ID: 188167  Cd Length: 448  Bit Score: 314.75  E-value: 6.82e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  30 PSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVT-SFFDAGAA 108
Cdd:TIGR01780   4 PATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKeAKGEILYA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 109 SDYFRYFSEAAYPMGTSSLNTPGFVNMGV--KQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKA 186
Cdd:TIGR01780  84 ASFLEWFAEEAKRVYGDTIPSPQSDKRLIviKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSALAL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 187 AELVAKAGFPPGVFNILSGHGAA--GAVMSSHMDIRIISFTGSTRTGRAIQKAAADSnLKNCIFELGGKSPALVFEDADI 264
Cdd:TIGR01780 164 ARLAEQAGIPKGVLNVITGSRAKevGNVLTTSPLVRKISFTGSTNVGKILMKQSAST-VKKVSMELGGNAPFIVFDDADL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 265 EQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKS 344
Cdd:TIGR01780 243 DQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAVEK 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 345 GTKITE--DLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVS 422
Cdd:TIGR01780 323 GAKVVTggKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWRVA 402

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1069468527 423 KQLEAGTVGVNCSSPTKgNDMPFGGWKGSGIGRESYIGGVESFMEDK 469
Cdd:TIGR01780 403 EALEYGMVGINTGLISN-VVAPFGGVKQSGLGREGSKYGIEEYLETK 448
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
 29-471 1.30e-101

Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.


Pssm-ID: 143438 [Multi-domain]  Cd Length: 455  Bit Score: 311.59  E-value: 1.30e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  29 SPSTGEFIAKVPEATAKDVDAAVAAAKAAF--PAWSAlSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVT-SFFDA 105
Cdd:cd07120     3 DPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGeARFEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 106 GAASDYFRYFSEAAYPM-GTSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCA 184
Cdd:cd07120    82 SGAISELRYYAGLARTEaGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 185 KAAELVAKA-GFPPGVFNILSGHGAAGA-VMSSHMDIRIISFTGSTRTGRAIQKAAAdSNLKNCIFELGGKSPALVFEDA 262
Cdd:cd07120   162 AIIRILAEIpSLPAGVVNLFTESGSEGAaHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCIVFDDA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 263 DIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYL--AL 340
Cdd:cd07120   241 DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVerAI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 341 AEKS-----GTKITEDLPNvsGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDI 415
Cdd:cd07120   321 AAGAevvlrGGPVTEGLAK--GAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1069468527 416 DRAMRVSKQLEAGTVGVNcSSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAV 471
Cdd:cd07120   399 ARAMRVARAIRAGTVWIN-DWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
 25-468 3.04e-101

Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143467 [Multi-domain]  Cd Length: 453  Bit Score: 310.68  E-value: 3.04e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  25 FDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVTsffD 104
Cdd:cd07149     1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIK---D 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 105 AGA----ASDYFRYFSEAA-------YPMGTS--SLNTPGFVnmgVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTV 171
Cdd:cd07149    78 ARKevdrAIETLRLSAEEAkrlagetIPFDASpgGEGRIGFT---IREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 172 VLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAA-GAVMSSHMDIRIISFTGSTRTGRAIQKAAAdsnLKNCIFEL 250
Cdd:cd07149   155 VLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETvGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLEL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 251 GGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQ 330
Cdd:cd07149   232 GSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 331 HETVKRYLALAEKSGTKITEDlPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASV 410
Cdd:cd07149   312 AERIEEWVEEAVEGGARLLTG-GKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1069468527 411 FTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIGREsyigGVESFMED 468
Cdd:cd07149   391 FTNDLQKALKAARELEVGGVMINDSSTFRVDHMPYGGVKESGTGRE----GPRYAIEE 444
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
 58-471 5.45e-101

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.


Pssm-ID: 143418 [Multi-domain]  Cd Length: 429  Bit Score: 309.01  E-value: 5.45e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  58 FPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVTsffDAGA----ASDYFRYFSE--AAYpMGTSSLNTPG 131
Cdd:cd07100    12 FLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIA---EARAevekCAWICRYYAEnaEAF-LADEPIETDA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 132 FVNMGVKQPYGVCGIIIPWNAPL--IF-FSkkgAAALAAGNTVVLKSSEKAPLtCAKA-AELVAKAGFPPGVF-NILSGH 206
Cdd:cd07100    88 GKAYVRYEPLGVVLGIMPWNFPFwqVFrFA---APNLMAGNTVLLKHASNVPG-CALAiEELFREAGFPEGVFqNLLIDS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 207 GAAGAVMSSHMdIRIISFTGSTRTGRAIQKAAAdSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFAN 286
Cdd:cd07100   164 DQVEAIIADPR-VRGVTLTGSERAGRAVAAEAG-KNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 287 SRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKITE--DLPNVSGLYISPTI 364
Cdd:cd07100   242 KRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLggKRPDGPGAFYPPTV 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 365 FTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNcsSPTKGN-DM 443
Cdd:cd07100   322 LTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN--GMVKSDpRL 399

                         410       420
                  ....*....|....*....|....*...
gi 1069468527 444 PFGGWKGSGIGRESYIGGVESFMEDKAV 471
Cdd:cd07100   400 PFGGVKRSGYGRELGRFGIREFVNIKTV 427
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
 11-473 9.52e-101

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).


Pssm-ID: 143405 [Multi-domain]  Cd Length: 478  Bit Score: 310.26  E-value: 9.52e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  11 FINGKFQAiDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQL 90
Cdd:cd07086     2 VIGGEWVG-SGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  91 EAKSMGRP-------VTSFFDAgaaSDYFryFSEAAYPMGT---SSLntPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKK 160
Cdd:cd07086    81 VSLEMGKIlpeglgeVQEMIDI---CDYA--VGLSRMLYGLtipSER--PGHRLMEQWNPLGVVGVITAFNFPVAVPGWN 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 161 GAAALAAGNTVVLKSSEKAPLTCAKAAELVAKA----GFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRAIQK 236
Cdd:cd07086   154 AAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 237 AAADSNlKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPT 316
Cdd:cd07086   234 TVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPL 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 317 QAGTTQGPQADKVQHETVKRYLALAEKSGTKI-------TEDLPnvsGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTF 389
Cdd:cd07086   313 DEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVltggkriDGGEP---GNYVEPTIVTGVTDDARIVQEETFAPILYVIKF 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 390 EGEAEAIAKANDTEYGLYASVFTKDIDRAMRV--SKQLEAGTVGVNcsSPTKGND--MPFGGWKGSGIGRESYIGGVESF 465
Cdd:cd07086   390 DSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVN--IPTSGAEigGAFGGEKETGGGRESGSDAWKQY 467


                  ....*...
gi 1069468527 466 MEDKAVLI 473
Cdd:cd07086   468 MRRSTCTI 475
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
 28-454 2.26e-97

Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.


Pssm-ID: 143420 [Multi-domain]  Cd Length: 452  Bit Score: 300.70  E-value: 2.26e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  28 HSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVT-SFFDAG 106
Cdd:cd07102     1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAqAGGEIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 107 AASDYFRYF-SEAAYPMGTSSL-NTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCA 184
Cdd:cd07102    81 GMLERARYMiSIAEEALADIRVpEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 185 KAAELVAKAGFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADI 264
Cdd:cd07102   161 RFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYVRPDADL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 265 EQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKS 344
Cdd:cd07102   240 DAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 345 GTKI-----TEDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAM 419
Cdd:cd07102   320 GARAlidgaLFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAE 399

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1069468527 420 RVSKQLEAGTVGVNCS---SPtkgnDMPFGGWKGSGIG 454
Cdd:cd07102   400 ALGEQLETGTVFMNRCdylDP----ALAWTGVKDSGRG 433
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
 26-473 1.92e-96

ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.


Pssm-ID: 143413 [Multi-domain]  Cd Length: 453  Bit Score: 298.19  E-value: 1.92e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  26 DLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVT-SFFD 104
Cdd:cd07094     2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKdARVE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 105 AGAASDYFRYFSEAA-------YPMGTSSLNTP--GFVnmgVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKS 175
Cdd:cd07094    82 VDRAIDTLRLAAEEAerirgeeIPLDATQGSDNrlAWT---IREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 176 SEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAAdsnLKNCIFELGGKS 254
Cdd:cd07094   159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREvLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 255 PALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETV 334
Cdd:cd07094   236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 335 KRYLALA-EKSGTKITEDLPnvSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTK 413
Cdd:cd07094   316 ERWVEEAvEAGARLLCGGER--DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR 393

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 414 DIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07094   394 DLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
 14-474 5.45e-93

NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.


Pssm-ID: 143469 [Multi-domain]  Cd Length: 465  Bit Score: 289.59  E-value: 5.45e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  14 GKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAK 93
Cdd:cd07151     1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  94 SMGRPVT-SFFDAGAASDYFRyfsEAA-YP--MGTSSL--NTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAA 167
Cdd:cd07151    81 ESGSTRIkANIEWGAAMAITR---EAAtFPlrMEGRILpsDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 168 GNTVVLKSSEKAPLT----CAKAAElvaKAGFPPGVFNILSGHGAA-GAVMSSHMDIRIISFTGSTRTGRAIQKAAADsN 242
Cdd:cd07151   158 GNAVVLKPASDTPITggllLAKIFE---EAGLPKGVLNVVVGAGSEiGDAFVEHPVPRLISFTGSTPVGRHIGELAGR-H 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 243 LKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQ 322
Cdd:cd07151   234 LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVV 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 323 GPQADKVQHETVKRYLALAEKSG-TKITEDlpNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKAND 401
Cdd:cd07151   314 GPLINESQVDGLLDKIEQAVEEGaTLLVGG--EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1069468527 402 TEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIGResyIGG---VESFMEDKAVLIK 474
Cdd:cd07151   392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGR---FNGewaLEEFTTDKWISVQ 464
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
11-475 8.13e-93

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 289.88  E-value: 8.13e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  11 FINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQL 90
Cdd:PRK11241   14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  91 EAKSMGRPVT-SFFDAGAASDYFRYFSEAAYPMGTSSL--NTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAA 167
Cdd:PRK11241   94 MTLEQGKPLAeAKGEISYAASFIEWFAEEGKRIYGDTIpgHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 168 GNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGH-GAAGAVMSSHMDIRIISFTGSTRTGRAIQKAAAdSNLKNC 246
Cdd:PRK11241  174 GCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSaGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCA-KDIKKV 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 247 IFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQA 326
Cdd:PRK11241  253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLI 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 327 DKVQHETVKRYLALAEKSGTKITE--DLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEY 404
Cdd:PRK11241  333 DEKAVAKVEEHIADALEKGARVVCggKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEF 412

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1069468527 405 GLYASVFTKDIDRAMRVSKQLEAGTVGVNcSSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLIKV 475
Cdd:PRK11241  413 GLAAYFYARDLSRVFRVGEALEYGIVGIN-TGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
 11-473 2.54e-88

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.


Pssm-ID: 143434 [Multi-domain]  Cd Length: 479  Bit Score: 278.18  E-value: 2.54e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  11 FINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQL 90
Cdd:cd07116     4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  91 EAKSMGRPV--TSFFDAGAASDYFRYFSEA--AYPMGTSSL--NTpgfVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAA 164
Cdd:cd07116    84 ETWDNGKPVreTLAADIPLAIDHFRYFAGCirAQEGSISEIdeNT---VAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 165 LAAGNTVVLKSSEKAPLTCAKAAELVAKAgFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsNL 243
Cdd:cd07116   161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLeAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 244 KNCIFELGGKSPALVFE------DADIEQAIQATVpSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQ 317
Cdd:cd07116   239 IPVTLELGGKSPNIFFAdvmdadDAFFDKALEGFV-MFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLD 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 318 AGTTQGPQADKVQHETVKRYLALAEKSGTKI--------TEDLPNvsGLYISPTIFTDTpEDAQIMKEEIFGPVVHINTF 389
Cdd:cd07116   318 TETMIGAQASLEQLEKILSYIDIGKEEGAEVltggerneLGGLLG--GGYYVPTTFKGG-NKMRIFQEEIFGPVLAVTTF 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 390 EGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNC--SSPTKGndmPFGGWKGSGIGRESYIGGVESFME 467
Cdd:cd07116   395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCyhLYPAHA---AFGGYKQSGIGRENHKMMLDHYQQ 471


                  ....*.
gi 1069468527 468 DKAVLI 473
Cdd:cd07116   472 TKNLLV 477
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
 24-455 3.25e-87

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 276.76  E-value: 3.25e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  24 TFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELA---QLEA-KSMGRPV 99
Cdd:PRK09407   33 TREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLdlvQLETgKARRHAF 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 100 TSFFDAGAASDYF-----RYFSE----AAYPMGTSSLNtpgfvnmgVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNT 170
Cdd:PRK09407  113 EEVLDVALTARYYarrapKLLAPrrraGALPVLTKTTE--------LRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNA 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 171 VVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAA-GAVMSSHMDIriISFTGSTRTGRAIQKAAAdSNLKNCIFE 249
Cdd:PRK09407  185 VVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVvGTALVDNADY--LMFTGSTATGRVLAEQAG-RRLIGFSLE 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 250 LGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKV 329
Cdd:PRK09407  262 LGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEA 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 330 QHETVKRYLALAEKSGTKItedL------PNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTE 403
Cdd:PRK09407  342 QLETVSAHVDDAVAKGATV---LaggkarPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTP 418

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1069468527 404 YGLYASVFTKDIDRAMRVSKQLEAGTVGVNCS-SPTKGN-DMPFGGWKGSGIGR 455
Cdd:PRK09407  419 YGLNASVWTGDTARGRAIAARIRAGTVNVNEGyAAAWGSvDAPMGGMKDSGLGR 472
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
 28-471 2.47e-86

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).


Pssm-ID: 143419 [Multi-domain]  Cd Length: 454  Bit Score: 272.26  E-value: 2.47e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  28 HSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELA---QLEA-KSMGRPVTSFF 103
Cdd:cd07101     1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLdliQLETgKARRHAFEEVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 104 DAGAASDYFRYFSEA---------AYPMGTSSLNTpgfvnmgvKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLK 174
Cdd:cd07101    81 DVAIVARYYARRAERllkprrrrgAIPVLTRTTVN--------RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 175 SSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA--AGAVMSsHMDIriISFTGSTRTGRAIQKAAAdSNLKNCIFELGG 252
Cdd:cd07101   153 PDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSevGGAIVD-NADY--VMFTGSTATGRVVAERAG-RRLIGCSLELGG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 253 KSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHE 332
Cdd:cd07101   229 KNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLD 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 333 TVKRYLALAEKSGTKIT---EDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYAS 409
Cdd:cd07101   309 RVTAHVDDAVAKGATVLaggRARPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNAS 388

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069468527 410 VFTKDIDRAMRVSKQLEAGTVGVNCS-SPTKGN-DMPFGGWKGSGIGRESYIGGVESFMEDKAV 471
Cdd:cd07101   389 VWTRDGARGRRIAARLRAGTVNVNEGyAAAWASiDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
 8-454 6.14e-86

Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.


Pssm-ID: 143404 [Multi-domain]  Cd Length: 478  Bit Score: 272.08  E-value: 6.14e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   8 TRLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAEL 87
Cdd:cd07085     1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  88 AQLEAKSMGRPVtsffdAGAASDYFRYFS--EAA-----YPMGTSSLN-TPGFVNMGVKQPYGVCGIIIPWN----APLI 155
Cdd:cd07085    81 ARLITLEHGKTL-----ADARGDVLRGLEvvEFAcsiphLLKGEYLENvARGIDTYSYRQPLGVVAGITPFNfpamIPLW 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 156 FFSkkgaAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRAIQ 235
Cdd:cd07085   156 MFP----MAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIY 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 236 KAAAdSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDP 315
Cdd:cd07085   232 ERAA-ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAG 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 316 TQAGTTQGPQADKVQHETVKRYLALAEKSGTKITEDLPNVS------GLYISPTIFTDTPEDAQIMKEEIFGPV---VHI 386
Cdd:cd07085   311 DDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKvpgyenGNFVGPTILDNVTPDMKIYKEEIFGPVlsiVRV 390

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1069468527 387 NTFEgeaEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIG 454
Cdd:cd07085   391 DTLD---EAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFG 455
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
 11-474 2.00e-84

NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.


Pssm-ID: 143401 [Multi-domain]  Cd Length: 473  Bit Score: 267.90  E-value: 2.00e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  11 FINGKFQaIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSP-KERSVYLARLGVLFAEHSAELAQ 89
Cdd:cd07082     5 LINGEWK-ESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEEVAN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  90 LEAKSMGRPVTSF---FDAGAasDYFRYFSEAA------YPMGTSSLNTPGFVNMGVKQPYGVCGIIIPWNAPL-IFFSK 159
Cdd:cd07082    84 LLMWEIGKTLKDAlkeVDRTI--DYIRDTIEELkrldgdSLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLnLTVSK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 160 KgAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAA 238
Cdd:cd07082   162 L-IPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGReIGDPLVTHGRIDVISFTGSTEVGNRLKKQH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 239 AdsnLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQA 318
Cdd:cd07082   241 P---MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDN 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 319 GTTQGPQADKVQHETVKRYLALAEKSGTKITEDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAK 398
Cdd:cd07082   318 GVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1069468527 399 ANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCsSPTKGND-MPFGGWKGSGIGRESYIGGVESFMEDKAVLIK 474
Cdd:cd07082   398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINS-KCQRGPDhFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
 59-467 2.34e-84

NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.


Pssm-ID: 143470 [Multi-domain]  Cd Length: 443  Bit Score: 266.85  E-value: 2.34e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  59 PAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMG--RPVTSFFDAGAASDYFRYFSEAAYPMGTSSLNTPGFVNMG 136
Cdd:cd07152    27 RAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGsiRPKAGFEVGAAIGELHEAAGLPTQPQGEILPSAPGRLSLA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 137 VKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKA-AELVAKAGFPPGVFNILSGHGAAGAVMSS 215
Cdd:cd07152   107 RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVViARLFEEAGLPAGVLHVLPGGADAGEALVE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 216 HMDIRIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSI 295
Cdd:cd07152   187 DPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESV 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 296 AQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKI----TEDlpnvsGLYISPTIFTDTPED 371
Cdd:cd07152   266 ADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLeaggTYD-----GLFYRPTVLSGVKPG 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 372 AQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGS 451
Cdd:cd07152   341 MPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDEPHNPFGGMGAS 420

                         410
                  ....*....|....*....
gi 1069468527 452 GIGreSYIGG---VESFME 467
Cdd:cd07152   421 GNG--SRFGGpanWEEFTQ 437
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
 25-468 1.69e-83

Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.


Pssm-ID: 143465 [Multi-domain]  Cd Length: 452  Bit Score: 264.88  E-value: 1.69e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  25 FDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVT-SFF 103
Cdd:cd07147     1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKdARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 104 DAGAASDYFRYFSEAA-------YPMGTSSlNTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSS 176
Cdd:cd07147    81 EVARAIDTFRIAAEEAtriygevLPLDISA-RGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 177 EKAPLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRAIQKAAADsnlKNCIFELGGKSPA 256
Cdd:cd07147   160 SRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGNAAV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 257 LVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKR 336
Cdd:cd07147   237 IVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEG 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 337 YLALAEKSGTKITEDLpNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDID 416
Cdd:cd07147   317 WVNEAVDAGAKLLTGG-KRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLE 395

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1069468527 417 RAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIGREsyigGVESFMED 468
Cdd:cd07147   396 KALRAWDELEVGGVVINDVPTFRVDHMPYGGVKDSGIGRE----GVRYAIEE 443
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
 82-474 2.09e-80

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 255.43  E-value: 2.09e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  82 EHSAELAQLEAKSMGRP-----VTSFFDAgaasDYFRYFSEAA--YPMGTSSLNTPGFVNMGVKQPYGVCGIIIPWNAPL 154
Cdd:PRK10090   10 ERASEISALIVEEGGKIqqlaeVEVAFTA----DYIDYMAEWArrYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 155 IFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRA 233
Cdd:PRK10090   86 FLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGEtVGQELAGNPKVAMVSMTGSVSAGEK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 234 IQKAAADSNLKNCIfELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLG 313
Cdd:PRK10090  166 IMAAAAKNITKVCL-ELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 314 DPTQAGTTQ-GPQADKVQHETVKRYLALAEKSGTKITE--DLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFE 390
Cdd:PRK10090  245 NPAERNDIAmGPLINAAALERVEQKVARAVEEGARVALggKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFD 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 391 GEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSS--PTKGndmpF-GGWKGSGIGRESYIGGVESFME 467
Cdd:PRK10090  325 TLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENfeAMQG----FhAGWRKSGIGGADGKHGLHEYLQ 400


                  ....*..
gi 1069468527 468 DKAVLIK 474
Cdd:PRK10090  401 TQVVYLQ 407
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
 10-471 7.79e-77

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 249.47  E-value: 7.79e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  10 LFINGKfqAIDESQTFDLHSPS-TGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELA 88
Cdd:PRK03137   39 LIIGGE--RITTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  89 QLEAKSMGRP-VTSFFDAGAASDYFRYFSEAA--YPMGTSSLNTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAAL 165
Cdd:PRK03137  117 AWLVKEAGKPwAEADADTAEAIDFLEYYARQMlkLADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAI 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 166 AAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAA-GAVMSSHMDIRIISFTGSTRTGRAIQKAAADSN-- 242
Cdd:PRK03137  197 VAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEvGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQpg 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 243 ---LKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAg 319
Cdd:PRK03137  277 qiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN- 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 320 TTQGPQADKVQHETVKRYLALAEKSGTKIT--EDLPNvSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIA 397
Cdd:PRK03137  356 AYMGPVINQASFDKIMSYIEIGKEEGRLVLggEGDDS-KGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALE 434

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1069468527 398 KANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVN--CSSPTKGNDmPFGGWKGSGIgrESYIGGVE---SFMEDKAV 471
Cdd:PRK03137  435 IANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYH-PFGGFNMSGT--DSKAGGPDyllLFLQAKTV 510
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
 27-473 4.43e-75

Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.


Pssm-ID: 143464 [Multi-domain]  Cd Length: 451  Bit Score: 243.03  E-value: 4.43e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  27 LHSPSTGEFIAKVPeATAKDVDAAVAAAKAAFPawSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVT-SFFDA 105
Cdd:cd07146     3 VRNPYTGEVVGTVP-AGTEEALREALALAASYR--STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKdTRYEV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 106 GAASDYFRYFSEAAYPMGTSSLNTPGFVNMG------VKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKA 179
Cdd:cd07146    80 GRAADVLRFAAAEALRDDGESFSCDLTANGKarkiftLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 180 PLTCAKAAELVAKAGFPPGVFNILSGH-GAAGAVMSSHMDIRIISFTGSTRTGRAIqkaAADSNLKNCIFELGGKSPALV 258
Cdd:cd07146   160 PLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELGGNDPLIV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 259 FEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYL 338
Cdd:cd07146   237 MDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRV 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 339 ALAEKSGTKITedLPNV-SGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDR 417
Cdd:cd07146   317 EEAIAQGARVL--LGNQrQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDT 394

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1069468527 418 AMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIG-RESYIGGVESFMEDKAVLI 473
Cdd:cd07146   395 IKRLVERLDVGTVNVNEVPGFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
 28-463 1.17e-65

Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.


Pssm-ID: 143416 [Multi-domain]  Cd Length: 465  Bit Score: 218.71  E-value: 1.17e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  28 HSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVtsfFDAG- 106
Cdd:cd07098     1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTM---VDASl 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 107 ----AASDYFRYFSEAaypmGTSSLNT---PGFVNMGVK------QPYGVCGIIIPWNAPL----------IFfskkgaa 163
Cdd:cd07098    78 geilVTCEKIRWTLKH----GEKALRPesrPGGLLMFYKrarveyEPLGVVGAIVSWNYPFhnllgpiiaaLF------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 164 alaAGNTVVLKSSEKAPLTCAKAAELVAKA----GFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRAIQKAAA 239
Cdd:cd07098   147 ---AGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAA 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 240 DSnLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQA- 318
Cdd:cd07098   224 ES-LTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGd 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 319 ----GTTQGPQADKVQHETVKRYLALAE-KSGTKITEDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEA 393
Cdd:cd07098   303 vdvgAMISPARFDRLEELVADAVEKGARlLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDE 382

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1069468527 394 EAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGN-DMPFGGWKGSGIGResyIGGVE 463
Cdd:cd07098   383 EAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVqQLPFGGVKGSGFGR---FAGEE 450
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
 137-473 4.51e-63

ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.


Pssm-ID: 143406 [Multi-domain]  Cd Length: 426  Bit Score: 210.85  E-value: 4.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 137 VKQPYGVCGIIIPWN-------APLIffskkgaAALAAGNTVVLKSSEKAPLTCAKAAELVAKAgFPPGVFNILSGHGA- 208
Cdd:cd07087    97 IPEPLGVVLIIGPWNyplqlalAPLI-------GAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEv 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 209 AGAVMSSHMDIriISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADIEQAIQatvpSIGW----NSGQTCF 284
Cdd:cd07087   169 ATALLAEPFDH--IFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAAR----RIAWgkflNAGQTCI 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 285 ANSRIYVHKSIAQTFIEGFKtKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLalaeKSGTKITEDLPNVSGLYISPTI 364
Cdd:cd07087   242 APDYVLVHESIKDELIEELK-KAIKEFYGEDPKESPDYGRIINERHFDRLASLL----DDGKVVIGGQVDKEERYIAPTI 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 365 FTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVN-----CSSPTk 439
Cdd:cd07087   317 LDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvllhAAIPN- 395

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1069468527 440 gndMPFGGWKGSGIGResYIG--GVESFMEDKAVLI 473
Cdd:cd07087   396 ---LPFGGVGNSGMGA--YHGkaGFDTFSHLKSVLK 426
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
 58-457 1.37e-62

N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.


Pssm-ID: 143414 [Multi-domain]  Cd Length: 431  Bit Score: 209.44  E-value: 1.37e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  58 FPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRP-------VTSFfdAGAASdyfryFSEAAYPMGTSSLNTP 130
Cdd:cd07095    13 FPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPlweaqteVAAM--AGKID-----ISIKAYHERTGERATP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 131 -GFVNMGVKQ-PYGVCGIIIPWNAP-----------LIffskkgaaalaAGNTVVLKSSEKAPLTCAKAAELVAKAGFPP 197
Cdd:cd07095    86 mAQGRAVLRHrPHGVMAVFGPFNFPghlpnghivpaLL-----------AGNTVVFKPSELTPAVAELMVELWEEAGLPP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 198 GVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRAIQKAAADSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGW 277
Cdd:cd07095   155 GVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 278 NSGQTCFANSRIYVH-KSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQadkVQHETVKRYLALAEK----SGTKITE-D 351
Cdd:cd07095   235 TAGQRCTCARRLIVPdGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPL---IIAAAAARYLLAQQDllalGGEPLLAmE 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 352 LPNVSGLYISPTIFtDTPEDAQIMKEEIFGPVVHI---NTFEgeaEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAG 428
Cdd:cd07095   312 RLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVyryDDFD---EAIALANATRFGLSAGLLSDDEALFERFLARIRAG 387

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1069468527 429 TvgVNCSSPTKG--NDMPFGGWKGSGIGRES 457
Cdd:cd07095   388 I--VNWNRPTTGasSTAPFGGVGLSGNHRPS 416
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
 13-457 6.94e-62

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.


Pssm-ID: 143448  Cd Length: 474  Bit Score: 208.99  E-value: 6.94e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  13 NGKFQAidESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEA 92
Cdd:cd07130     4 DGEWGG--GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  93 KSMGRP-------VTSFFDAgaasdyfryfseAAYPMGTS-SLN-------TPGFVNMGVKQPYGVCGIIIPWNAPLIFF 157
Cdd:cd07130    82 LEMGKIlpeglgeVQEMIDI------------CDFAVGLSrQLYgltipseRPGHRMMEQWNPLGVVGVITAFNFPVAVW 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 158 SKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKA----GFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRA 233
Cdd:cd07130   150 GWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 234 IQKAAADsNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLG 313
Cdd:cd07130   230 VGQAVAA-RFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIG 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 314 DPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKIT---EDLPNvSGLYISPTIFTdTPEDAQIMKEEIFGPVVHINTFE 390
Cdd:cd07130   309 DPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLfggKVIDG-PGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFD 386

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1069468527 391 GEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDM--PFGGWKGSGIGRES 457
Cdd:cd07130   387 TLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIggAFGGEKETGGGRES 455
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
 29-460 2.24e-60

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 204.71  E-value: 2.24e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  29 SPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVTSFFDAGAA 108
Cdd:PRK13968   13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 109 SDYF-RYFSEaaypMGTSSLNT-PGFV--NMGV--KQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKsseKAP-- 180
Cdd:PRK13968   93 SANLcDWYAE----HGPAMLKAePTLVenQQAVieYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLK---HAPnv 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 181 LTCAK-AAELVAKAGFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRAIqKAAADSNLKNCIFELGGKSPALVF 259
Cdd:PRK13968  166 MGCAQlIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAI-GAQAGAALKKCVLELGGSDPFIVL 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 260 EDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQA-----DKVqHETV 334
Cdd:PRK13968  245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMArfdlrDEL-HHQV 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 335 KRYLALAEK---SGTKITEdlpnvSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVF 411
Cdd:PRK13968  324 EATLAEGARlllGGEKIAG-----AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1069468527 412 TKDIDRAMRVSKQLEAGTVGVN--CSSPTKgndMPFGGWKGSGIGRE-SYIG 460
Cdd:PRK13968  399 TTDETQARQMAARLECGGVFINgyCASDAR---VAFGGVKKSGFGRElSHFG 447
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
 29-454 2.71e-60

ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.


Pssm-ID: 143402 [Multi-domain]  Cd Length: 500  Bit Score: 205.51  E-value: 2.71e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  29 SPS-TGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVTSFFDAGA 107
Cdd:cd07083    38 SPFaPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 108 -ASDYFRYFSEAAYP-MGTSSL--NTPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTC 183
Cdd:cd07083   118 eAIDFIRYYARAALRlRYPAVEvvPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVG 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 184 AKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAAAD-----SNLKNCIFELGGKSPAL 257
Cdd:cd07083   198 YKVFEIFHEAGFPPGVVQFLPGVGEeVGAYLTEHERIRGINFTGSLETGKKIYEAAARlapgqTWFKRLYVETGGKNAII 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 258 VFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRY 337
Cdd:cd07083   278 VDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSY 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 338 LALAEKSGTKITE-DLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGE--AEAIAKANDTEYGLYASVFTKD 414
Cdd:cd07083   358 IEHGKNEGQLVLGgKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDdfAEALEVANSTPYGLTGGVYSRK 437

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1069468527 415 IDRAMRVSKQLEAGTVGVN-CSSPTKGNDMPFGGWKGSGIG 454
Cdd:cd07083   438 REHLEEARREFHVGNLYINrKITGALVGVQPFGGFKLSGTN 478
gabD1 PRK09406
succinic semialdehyde dehydrogenase; Reviewed
 30-473 2.45e-59

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181826 [Multi-domain]  Cd Length: 457  Bit Score: 201.89  E-value: 2.45e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  30 PSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVTSF-FDAGAA 108
Cdd:PRK09406    8 PATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAkAEALKC 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 109 SDYFRYFSEAAYPMGTSSLNTPGFVN----MGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCA 184
Cdd:PRK09406   88 AKGFRYYAEHAEALLADEPADAAAVGasraYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTAL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 185 KAAELVAKAGFPPGVF-NILSGHGAAGAVMSshmDIRII--SFTGSTRTGRAIQKAAADSnLKNCIFELGGKSPALVFED 261
Cdd:PRK09406  168 YLADLFRRAGFPDGCFqTLLVGSGAVEAILR---DPRVAaaTLTGSEPAGRAVAAIAGDE-IKKTVLELGGSDPFIVMPS 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 262 ADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALA 341
Cdd:PRK09406  244 ADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDA 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 342 EKSGTKIT--EDLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAM 419
Cdd:PRK09406  324 VAAGATILcgGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQE 403

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1069468527 420 RVSKQLEAGTVGVN---CSSPtkgnDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:PRK09406  404 RFIDDLEAGQVFINgmtVSYP----ELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
 7-454 3.46e-59

Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.


Pssm-ID: 143443 [Multi-domain]  Cd Length: 518  Bit Score: 202.81  E-value: 3.46e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   7 ETRLFINGKFQAIDESQtfDLHSPSTGE-FIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSA 85
Cdd:cd07125    32 EAIPIINGEETETGEGA--PVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  86 EL---AQLEAksmGRPVTsffDAGA----ASDYFRYFSEAA-YPMGTSSLNTP-GFVNMGVKQPYGVCGIIIPWNAPLIF 156
Cdd:cd07125   110 ELialAAAEA---GKTLA---DADAevreAIDFCRYYAAQArELFSDPELPGPtGELNGLELHGRGVFVCISPWNFPLAI 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 157 FSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQ 235
Cdd:cd07125   184 FTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEeIGEALVAHPRIDGVIFTGSTETAKLIN 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 236 K--AAADSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLG 313
Cdd:cd07125   264 RalAERDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVG 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 314 DPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKI-TEDLPNVSGLYISPTIFtdtpEDAQI--MKEEIFGPVVHINTFE 390
Cdd:cd07125   344 DPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIaPAPLDDGNGYFVAPGII----EIVGIfdLTTEVFGPILHVIRFK 419

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1069468527 391 GE--AEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNcsSPTKG---NDMPFGGWKGSGIG 454
Cdd:cd07125   420 AEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN--RNITGaivGRQPFGGWGLSGTG 486
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
 139-473 1.30e-54

Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.


Pssm-ID: 143452 [Multi-domain]  Cd Length: 433  Bit Score: 188.59  E-value: 1.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 139 QPYGVCGIIIPWN-------APLIffskkgaAALAAGNTVVLKSSEKAPLTCAKAAELVAKAgFPPGVFNILSGhgaaGA 211
Cdd:cd07134    99 EPKGVCLIISPWNypfnlafGPLV-------SAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG----DA 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 212 VMSSH-MDIRI--ISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADIEQAIQAtvpsIGW----NSGQTCF 284
Cdd:cd07134   167 EVAQAlLELPFdhIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKK----IAWgkflNAGQTCI 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 285 ANSRIYVHKSIAQTFIEGFKT---KFMSAklGDPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKITED-LPNVSGLYI 360
Cdd:cd07134   242 APDYVFVHESVKDAFVEHLKAeieKFYGK--DAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGgQFDAAQRYI 319

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 361 SPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVN-CSSPTK 439
Cdd:cd07134   320 APTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNdVVLHFL 399

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1069468527 440 GNDMPFGGWKGSGIGRESYIGGVESFMEDKAVLI 473
Cdd:cd07134   400 NPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVLR 433
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
 139-472 2.39e-53

Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.


Pssm-ID: 143451 [Multi-domain]  Cd Length: 434  Bit Score: 185.38  E-value: 2.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 139 QPYGVCGIIIPWN-------APLIffskkgaAALAAGNTVVLKSSEKAPLTCAKAAELVAKAgFPPGVFNILSGHGAAGA 211
Cdd:cd07133   100 QPLGVVGIIVPWNyplylalGPLI-------AALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTGGADVAA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 212 VMSS----HMdiriiSFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANS 287
Cdd:cd07133   172 AFSSlpfdHL-----LFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPD 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 288 RIYVHKSIAQTFIEGFKTKFmsAKLGdPTQAGttqGPQ----ADKVQHETVKRYLALAEKSGTKITEDLPN----VSGLY 359
Cdd:cd07133   246 YVLVPEDKLEEFVAAAKAAV--AKMY-PTLAD---NPDytsiINERHYARLQGLLEDARAKGARVIELNPAgedfAATRK 319

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 360 ISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIA--KANDTEYGLYasVFTKDIDRAMRVSKQLEAGTVGVN-CSS 436
Cdd:cd07133   320 LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDyiNARPRPLALY--YFGEDKAEQDRVLRRTHSGGVTINdTLL 397

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1069468527 437 PTKGNDMPFGGWKGSGIGResYIG--GVESFMEDKAVL 472
Cdd:cd07133   398 HVAQDDLPFGGVGASGMGA--YHGkeGFLTFSHAKPVF 433
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
 64-468 5.86e-53

Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143466 [Multi-domain]  Cd Length: 455  Bit Score: 184.93  E-value: 5.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  64 LSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRP-VTSFFDAGAASDYFRYFSEA-------AYPMGTSSLNTpGFVNM 135
Cdd:cd07148    41 LPAHERIAILERLADLMEERADELALLIAREGGKPlVDAKVEVTRAIDGVELAADElgqlggrEIPMGLTPASA-GRIAF 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 136 GVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSS 215
Cdd:cd07148   120 TTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVT 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 216 HMDIRIISFTGSTRTG-RAIQKAAADSNlknCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKS 294
Cdd:cd07148   200 DPRVAFFSFIGSARVGwMLRSKLAPGTR---CALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAE 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 295 IAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKITEDLPNVSGLYISPTIFTDTPEDAQI 374
Cdd:cd07148   277 IADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTYAPTVLLDPPRDAKV 356

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 375 MKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIG 454
Cdd:cd07148   357 STQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436

                         410
                  ....*....|....
gi 1069468527 455 resyIGGVESFMED 468
Cdd:cd07148   437 ----TGGIPYTMHD 446
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
 138-474 1.82e-50

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 179.07  E-value: 1.82e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 138 KQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAgFPPGVFN-ILSGHGAAGAVMSSH 216
Cdd:PTZ00381  107 PEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRvIEGGVEVTTELLKEP 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 217 MDIriISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIA 296
Cdd:PTZ00381  186 FDH--IFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIK 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 297 QTFIEGFKTkFMSAKLGDPTQagtTQGPQADKVQHETVKRYLALAEKSGTKIT---EdlPNVSGLYISPTIFTDTPEDAQ 373
Cdd:PTZ00381  263 DKFIEALKE-AIKEFFGEDPK---KSEDYSRIVNEFHTKRLAELIKDHGGKVVyggE--VDIENKYVAPTIIVNPDLDSP 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 374 IMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGND-MPFGGWKGSG 452
Cdd:PTZ00381  337 LMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPnLPFGGVGNSG 416

                         330       340
                  ....*....|....*....|..
gi 1069468527 453 IGRESYIGGVESFMEDKAVLIK 474
Cdd:PTZ00381  417 MGAYHGKYGFDTFSHPKPVLNK 438
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
 137-474 2.53e-50

Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.


Pssm-ID: 143454 [Multi-domain]  Cd Length: 449  Bit Score: 177.70  E-value: 2.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 137 VKQPYGVCGIIIPWN-------APLIffskkgaAALAAGNTVVLKSSEKAPLTCAKAAELVAKAgFPPG-VFNILSGHGA 208
Cdd:cd07136    97 YYEPYGVVLIIAPWNypfqlalAPLI-------GAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEyVAVVEGGVEE 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 209 AGAVMSSHMDIriISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADIEQAIQatvpSIGW----NSGQTCF 284
Cdd:cd07136   169 NQELLDQKFDY--IFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAK----RIVWgkflNAGQTCV 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 285 ANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPtqagtTQGPQADKVQHEtvKRYLALAE--KSGTKITEDLPNVSGLYISP 362
Cdd:cd07136   242 APDYVLVHESVKEKFIKELKEEIKKFYGEDP-----LESPDYGRIINE--KHFDRLAGllDNGKIVFGGNTDRETLYIEP 314

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 363 TIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVN-----CSSP 437
Cdd:cd07136   315 TILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtimhLANP 394

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1069468527 438 tkgnDMPFGGWKGSGIGreSYIG--GVESFMEDKAVLIK 474
Cdd:cd07136   395 ----YLPFGGVGNSGMG--SYHGkySFDTFSHKKSILKK 427
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
 3-454 4.40e-45

delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273518 [Multi-domain]  Cd Length: 500  Bit Score: 164.70  E-value: 4.40e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   3 ASPIetrlfINGKFQAIDESQTfdLHSPST-GEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFA 81
Cdd:TIGR01238  38 AAPI-----IGHSYKADGEAQP--VTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  82 EHSAELAQLEAKSMGRPVT-SFFDAGAASDYFRYFS-EAAYPMGTSSLNTPGFVnmgvkqpygVCgiIIPWNAPLIFFSK 159
Cdd:TIGR01238 111 LHMPELMALCVREAGKTIHnAIAEVREAVDFCRYYAkQVRDVLGEFSVESRGVF---------VC--ISPWNFPLAIFTG 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 160 KGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGA-AGAVMSSHMDIRIISFTGSTRTGRAIQKAA 238
Cdd:TIGR01238 180 QISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGAdVGAALTSDPRIAGVAFTGSTEVAQLINQTL 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 239 A--DSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPT 316
Cdd:TIGR01238 260 AqrEDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPH 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 317 QAGTTQGPQADKVQHETVKRYLALAEKSGTKITE-----DLPNVSGLYISPTIFTDTPEDAqiMKEEIFGPVVHINTFEG 391
Cdd:TIGR01238 340 LLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQltlddSRACQHGTFVAPTLFELDDIAE--LSEEVFGPVLHVVRYKA 417

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1069468527 392 E--AEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNcssptkgNDM--------PFGGWKGSGIG 454
Cdd:TIGR01238 418 RelDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN-------RNQvgavvgvqPFGGQGLSGTG 483
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
 10-457 2.68e-43

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 159.35  E-value: 2.68e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  10 LFINGKFQAiDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQ 89
Cdd:PRK09457    3 LWINGDWIA-GQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  90 LEAKSMGRP-------VTSFFDAGAasdyfryFSEAAYP--MGTSSLNTPGFVNMGVKQPYGVCGIIIPWNAP------- 153
Cdd:PRK09457   82 VIARETGKPlweaateVTAMINKIA-------ISIQAYHerTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPghlpngh 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 154 ----LIffskkgaaalaAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTR 229
Cdd:PRK09457  155 ivpaLL-----------AGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSAN 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 230 TGRAIQKAAADSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSI-AQTFIEGFKTKFM 308
Cdd:PRK09457  224 TGYLLHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAK 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 309 SAKLGDPTQA-----GTTQGPQADKVQHETVKRYLALAEKS---GTKITEDLPNVSGLYISPTIFTDTPEdaqimkEEIF 380
Cdd:PRK09457  304 RLTVGRWDAEpqpfmGAVISEQAAQGLVAAQAQLLALGGKSlleMTQLQAGTGLLTPGIIDVTGVAELPD------EEYF 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 381 GP---VVHINTFEgeaEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTvgVNCSSPTKG--NDMPFGGWKGSGIGR 455
Cdd:PRK09457  378 GPllqVVRYDDFD---EAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGI--VNWNKPLTGasSAAPFGGVGASGNHR 452


                  ..
gi 1069468527 456 ES 457
Cdd:PRK09457  453 PS 454
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
 11-471 6.19e-43

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 160.30  E-value: 6.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  11 FINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQL 90
Cdd:PLN02419  117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMN 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  91 EAKSMGRPVTSffdagAASDYFRYFSEAAYPMGTSSLN--------TPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGA 162
Cdd:PLN02419  197 ITTEQGKTLKD-----SHGDIFRGLEVVEHACGMATLQmgeylpnvSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFP 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 163 AALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGSTRTGRAIQKAAADSN 242
Cdd:PLN02419  272 VAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 243 lKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIyVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQ 322
Cdd:PLN02419  352 -KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTV-VFVGDAKSWEDKLVERAKALKVTCGSEPDADL 429

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 323 GPQADKVQHETVKRYLALAEKSGTKITEDLPNV------SGLYISPTIFTDTPEDAQIMKEEIFGPVV---HINTFEgea 393
Cdd:PLN02419  430 GPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgyeKGNFIGPTILSGVTPDMECYKEEIFGPVLvcmQANSFD--- 506

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 394 EAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDMPFGGWKGSGIGRESYIG--GVESFMEDKAV 471
Cdd:PLN02419  507 EAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGkaGVDFFTQIKLV 586
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
 54-472 6.38e-43

Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.


Pssm-ID: 143453 [Multi-domain]  Cd Length: 436  Bit Score: 157.38  E-value: 6.38e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  54 AKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPV--TSFFDAGAASDYFRY-------FSEAAYPMGT 124
Cdd:cd07135    14 LRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPfeTLLTEVSGVKNDILHmlknlkkWAKDEKVKDG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 125 SslntPGFVNMGV---KQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAgFPPGVFN 201
Cdd:cd07135    94 P----LAFMFGKPrirKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQ 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 202 ILSGHGA-AGAVMSSHMDirIISFTGSTRTGRAIQKAAADsNLKNCIFELGGKSPALVFEDADIEQAIQatvpSIGW--- 277
Cdd:cd07135   169 VVQGGVPeTTALLEQKFD--KIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELAAK----RILWgkf 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 278 -NSGQTCFANSRIYVHKSIAQTFIEGFKT---KFMSAKLGDPTQAGTTQGPQAdkvqhetVKRYLALAEKSGTKI-TEDL 352
Cdd:cd07135   242 gNAGQICVAPDYVLVDPSVYDEFVEELKKvldEFYPGGANASPDYTRIVNPRH-------FNRLKSLLDTTKGKVvIGGE 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 353 PNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGV 432
Cdd:cd07135   315 MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVI 394

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1069468527 433 N-CSSPTKGNDMPFGGWKGSGIGRESYIGGVESFMEDKAVL 472
Cdd:cd07135   395 NdTLIHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
 9-473 1.23e-42

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 157.61  E-value: 1.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   9 RLFINGKFQAIDESQTFDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELA 88
Cdd:PLN00412   17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  89 QLEAKSMGRP----VTSFFDAGAASDY-----FRYFSEAAYPMGTSslnTPGfvN------MGVKQPYGVCGIIIPWNAP 153
Cdd:PLN00412   97 ECLVKEIAKPakdaVTEVVRSGDLISYtaeegVRILGEGKFLVSDS---FPG--NernkycLTSKIPLGVVLAIPPFNYP 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 154 LIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAA-GAVMSSHMDIRIISFTGSTrTGR 232
Cdd:PLN00412  172 VNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEiGDFLTMHPGVNCISFTGGD-TGI 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 233 AIQKAAADSNLKnciFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKL 312
Cdd:PLN00412  251 AISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTV 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 313 GDPtQAGTTQGPQADKVQHETVKRYLALAEKSGTKITEDLPNVSGLyISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGE 392
Cdd:PLN00412  328 GPP-EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGNL-IWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSV 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 393 AEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNcSSPTKGND-MPFGGWKGSGIGRESYIGGVESFMEDKAV 471
Cdd:PLN00412  406 EEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN-SAPARGPDhFPFQGLKDSGIGSQGITNSINMMTKVKST 484


                  ..
gi 1069468527 472 LI 473
Cdd:PLN00412  485 VI 486
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
 130-457 9.17e-41

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 152.68  E-value: 9.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 130 PGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVA----KAGFPPGVFNILSG 205
Cdd:PLN02315  144 PNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAevleKNNLPGAIFTSFCG 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 206 HGAAGAVMSSHMDIRIISFTGSTRTGRAIQKAAaDSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFA 285
Cdd:PLN02315  224 GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV-NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTT 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 286 NSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKITEDLPNVS--GLYISPT 363
Cdd:PLN02315  303 CRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIEseGNFVQPT 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 364 IFTDTPeDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGNDM 443
Cdd:PLN02315  383 IVEISP-DADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEI 461

                         330
                  ....*....|....*.
gi 1069468527 444 --PFGGWKGSGIGRES 457
Cdd:PLN02315  462 ggAFGGEKATGGGREA 477
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
 21-454 1.21e-40

bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 156.18  E-value: 1.21e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   21 ESQTFDLHSPS-TGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRpv 99
Cdd:PRK11905   565 DGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGK-- 642

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  100 tSFFDAGA----ASDYFRYFSEAAypmgtsslntPGFVNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKS 175
Cdd:PRK11905   643 -TLANAIAevreAVDFLRYYAAQA----------RRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKP 711

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  176 SEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAA-GAVMSShmDIRI--ISFTGSTRTGRAIQKAAADSNLKNC--IFEL 250
Cdd:PRK11905   712 AEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTvGAALVA--DPRIagVMFTGSTEVARLIQRTLAKRSGPPVplIAET 789

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  251 GGKSPALVFEDADIEQAIQATVPSiGWNS-GQTCFANSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKV 329
Cdd:PRK11905   790 GGQNAMIVDSSALPEQVVADVIAS-AFDSaGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAE 868

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  330 QHETVKRYLALAEKSGTKITE-DLPNV--SGLYISPTIF-TDTPEDaqiMKEEIFGPVVHINTFEGE--AEAIAKANDTE 403
Cdd:PRK11905   869 AQANIEAHIEAMRAAGRLVHQlPLPAEteKGTFVAPTLIeIDSISD---LEREVFGPVLHVVRFKADelDRVIDDINATG 945

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1069468527  404 YGLYASVFTKDIDRAMRVSKQLEAGT-----------VGVNcssptkgndmPFGGWKGSGIG 454
Cdd:PRK11905   946 YGLTFGLHSRIDETIAHVTSRIRAGNiyvnrniigavVGVQ----------PFGGEGLSGTG 997
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
 137-472 1.33e-40

Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.


Pssm-ID: 143455 [Multi-domain]  Cd Length: 432  Bit Score: 151.02  E-value: 1.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 137 VKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSSH 216
Cdd:cd07137    98 VSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEGGVPETTALLEQK 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 217 MDirIISFTGSTRTGRAIQKAAAdSNLKNCIFELGGKSPALVFEDADIEQAIQATVP-SIGWNSGQTCFANSRIYVHKSI 295
Cdd:cd07137   178 WD--KIFFTGSPRVGRIIMAAAA-KHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGgKWGCNNGQACIAPDYVLVEESF 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 296 AQTFIEGFKTKFMSAKLGDPTQAGTTqgpqADKVQHETVKRYLALAEKS--------GTKITEDlpnvsGLYISPTIFTD 367
Cdd:cd07137   255 APTLIDALKNTLEKFFGENPKESKDL----SRIVNSHHFQRLSRLLDDPsvadkivhGGERDEK-----NLYIEPTILLD 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 368 TPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKGND-MPFG 446
Cdd:cd07137   326 PPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDtLPFG 405

                         330       340
                  ....*....|....*....|....*...
gi 1069468527 447 GWKGSGIGResYIG--GVESFMEDKAVL 472
Cdd:cd07137   406 GVGESGFGA--YHGkfSFDAFSHKKAVL 431
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
2-454 1.77e-39

bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 152.66  E-value: 1.77e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527    2 SASPIetrlfINGKFQAIDesqtfdLHSPS-TGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLF 80
Cdd:PRK11904   552 QAGPI-----INGEGEARP------VVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLL 620

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   81 AEHSAE---LAQLEA-KSMGrpvtsffDAGA----ASDYFRYFSEAAYPMGTSSLNTPGFV---NMGVKQPYGVCGIIIP 149
Cdd:PRK11904   621 EANRAEliaLCVREAgKTLQ-------DAIAevreAVDFCRYYAAQARRLFGAPEKLPGPTgesNELRLHGRGVFVCISP 693

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  150 WNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAA-GAVMSSHMDIRIISFTGST 228
Cdd:PRK11904   694 WNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATvGAALTADPRIAGVAFTGST 773

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  229 RTGRAIQK--AAADSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTK 306
Cdd:PRK11904   774 ETARIINRtlAARDGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGA 853

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  307 FMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKITE-DLPNVS--GLYISPTIF-TDTPEDaqiMKEEIFGP 382
Cdd:PRK11904   854 MAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQlPLPAGTenGHFVAPTAFeIDSISQ---LEREVFGP 930

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  383 VVHINTFEGE--AEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNcssptkgNDM--------PFGGWKGSG 452
Cdd:PRK11904   931 ILHVIRYKASdlDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN-------RNQigavvgvqPFGGQGLSG 1003


                   ..
gi 1069468527  453 IG 454
Cdd:PRK11904  1004 TG 1005
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
58-447 2.10e-39

Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 443374 [Multi-domain]  Cd Length: 1156  Bit Score: 152.40  E-value: 2.10e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   58 FPAWSALSPKERSVYLARLGVLFAEHSAE---LAQLEAksmGRpvtSFFDAGA----ASDYFRYfseaaYPMGTSSLntp 130
Cdd:COG4230    606 FPAWSATPVEERAAILERAADLLEAHRAElmaLLVREA---GK---TLPDAIAevreAVDFCRY-----YAAQARRL--- 671

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  131 gFVNMGVKQPYGVCGIIIPWNAPL-IFfskkgaaalaaGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAA 209
Cdd:COG4230    672 -FAAPTVLRGRGVFVCISPWNFPLaIFtgqva-aalaaGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGET 749

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  210 -GAVMSSHMDIRIISFTGSTRTGRAIQKAAADSN-----LkncIFELGGK------SPALvfedadIEQAIQATVPSiGW 277
Cdd:COG4230    750 vGAALVADPRIAGVAFTGSTETARLINRTLAARDgpivpL---IAETGGQnamivdSSAL------PEQVVDDVLAS-AF 819

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  278 NS-GQTCFAnSRI-YVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKITE-DLPN 354
Cdd:COG4230    820 DSaGQRCSA-LRVlCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQlPLPE 898

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  355 --VSGLYISPTIFT-DTPEDaqiMKEEIFGPVVHINTFEGE--AEAIAKANDTEYGLYASVFTKdID-RAMRVSKQLEAG 428
Cdd:COG4230    899 ecANGTFVAPTLIEiDSISD---LEREVFGPVLHVVRYKADelDKVIDAINATGYGLTLGVHSR-IDeTIDRVAARARVG 974

                          410       420       430
                   ....*....|....*....|....*....|
gi 1069468527  429 -----------TVGVNcssptkgndmPFGG 447
Cdd:COG4230    975 nvyvnrniigaVVGVQ----------PFGG 994
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
 138-474 5.58e-35

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.


Pssm-ID: 143450 [Multi-domain]  Cd Length: 443  Bit Score: 135.43  E-value: 5.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 138 KQPYGVCGIIIPWNAP--LIFFSKKGAAALaaGNTVVLKSSEKAPLTCAKAAELVAKAgFPPGVFNILSGhGA--AGAVM 213
Cdd:cd07132    98 KEPLGVVLIIGAWNYPlqLTLVPLVGAIAA--GNCVVIKPSEVSPATAKLLAELIPKY-LDKECYPVVLG-GVeeTTELL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 214 SSHMDIriISFTGSTRTGRAIQKAAAdSNLKNCIFELGGKSPALVFEDADIeqaiQATVPSIGW----NSGQTCFANSRI 289
Cdd:cd07132   174 KQRFDY--IFYTGSTSVGKIVMQAAA-KHLTPVTLELGGKSPCYVDKSCDI----DVAARRIAWgkfiNAGQTCIAPDYV 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 290 YVHKSIAQTFIEGFKT---KFMsaklGDPTQAGTTQGPQADKVQHETVKRYLalaekSGTKITedlpnVSG------LYI 360
Cdd:cd07132   247 LCTPEVQEKFVEALKKtlkEFY----GEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVA-----IGGqtdekeRYI 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 361 SPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVN----CSS 436
Cdd:cd07132   313 APTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdtimHYT 392

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1069468527 437 PTkgnDMPFGGWKGSGIGResYIG--GVESFMEDKAVLIK 474
Cdd:cd07132   393 LD---SLPFGGVGNSGMGA--YHGkySFDTFSHKRSCLVK 427
ALDH_F4-17_P5CDH cd07123
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ...
 1-452 5.67e-35

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.


Pssm-ID: 143441 [Multi-domain]  Cd Length: 522  Bit Score: 136.95  E-value: 5.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   1 MSASPIETRLFINGKfqAIDESQTFDLHSPST-GEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKER-SVYLarlgv 78
Cdd:cd07123    26 LKSLTVEIPLVIGGK--EVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRaAIFL----- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  79 lfaeHSAEL------AQLEAKSM-GRPVTSF---FDAGAAS-DYFR---YFSEAAYPMGTSSlNTPGFVNMGVKQPY-GV 143
Cdd:cd07123    99 ----KAADLlsgkyrYELNAATMlGQGKNVWqaeIDAACELiDFLRfnvKYAEELYAQQPLS-SPAGVWNRLEYRPLeGF 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 144 CGIIIPWN----------APLIFfskkgaaalaaGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAA-GAV 212
Cdd:cd07123   174 VYAVSPFNftaiggnlagAPALM-----------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVvGDT 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 213 MSSHMDIRIISFTGSTRTGRAIQKAAADsNLKN------CIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFAN 286
Cdd:cd07123   243 VLASPHLAGLHFTGSTPTFKSLWKQIGE-NLDRyrtyprIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAA 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 287 SRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKSgtkitedlPNVS---------- 356
Cdd:cd07123   322 SRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSD--------PEAEiiaggkcdds 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 357 -GLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEGE--AEAIAKANDT-EYGLYASVFTKD---IDRAMRVSKQlEAGT 429
Cdd:cd07123   394 vGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSdfEETLELVDTTsPYALTGAIFAQDrkaIREATDALRN-AAGN 472

                         490       500
                  ....*....|....*....|....*
gi 1069468527 430 VGVNCsSPTKG--NDMPFGGWKGSG 452
Cdd:cd07123   473 FYIND-KPTGAvvGQQPFGGARASG 496
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
 59-464 2.83e-31

ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.


Pssm-ID: 143403 [Multi-domain]  Cd Length: 442  Bit Score: 125.04  E-value: 2.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  59 PAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRPVTSFFDAGAASDYFRYFSEAAYPMG--TSSLNTPG----F 132
Cdd:cd07084    13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRipHEPGNHLGqglkQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 133 VNMGVKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAG-FPPGVFNILSGHGAAGA 211
Cdd:cd07084    93 QSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKTMQ 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 212 VMSSHMDIRIISFTGSTRTGRAIQKAAADSNLKnciFELGGKSPALVFEDADIEQA-IQATVPSIGWNSGQTCFANSRIY 290
Cdd:cd07084   173 ALLLHPNPKMVLFTGSSRVAEKLALDAKQARIY---LELAGFNWKVLGPDAQAVDYvAWQCVQDMTACSGQKCTAQSMLF 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 291 VHKSIA-QTFIEGFKTKFMSAKLGD----PTQAGTTQGPQADKVQHETVKRYLALAEKSGTKITEdlpNVSGLYISPTIF 365
Cdd:cd07084   250 VPENWSkTPLVEKLKALLARRKLEDlllgPVQTFTTLAMIAHMENLLGSVLLFSGKELKNHSIPS---IYGACVASALFV 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 366 TDTPEDAQ--IMKEEIFGPVVHINTFEGEAEAIA-KANDTEYG-LYASVFTKDIDRAMRVSKQLE-AGTVGVNCSSPTKG 440
Cdd:cd07084   327 PIDEILKTyeLVTEEIFGPFAIVVEYKKDQLALVlELLERMHGsLTAAIYSNDPIFLQELIGNLWvAGRTYAILRGRTGV 406

                         410       420
                  ....*....|....*....|....
gi 1069468527 441 NDMPFGGWKGSGIGRESYIGGVES 464
Cdd:cd07084   407 APNQNHGGGPAADPRGAGIGGPEA 430
PLN02203 PLN02203
aldehyde dehydrogenase
 137-472 3.49e-31

aldehyde dehydrogenase


Pssm-ID: 165847 [Multi-domain]  Cd Length: 484  Bit Score: 125.61  E-value: 3.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 137 VKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSSH 216
Cdd:PLN02203  105 VPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEGGPAVGEQLLQHK 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 217 MDirIISFTGSTRTGRAIQKAAAdSNLKNCIFELGGKSPAlVFEDADIEQAIQATVPSI---GWNS--GQTCFANSRIYV 291
Cdd:PLN02203  185 WD--KIFFTGSPRVGRIIMTAAA-KHLTPVALELGGKCPC-IVDSLSSSRDTKVAVNRIvggKWGScaGQACIAIDYVLV 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 292 HKSIAQTFIEGFKT---KFMSAKLGDPtqagttqGPQADKVQHETVKRYLALAEKS--------GTKITEDlpnvsGLYI 360
Cdd:PLN02203  261 EERFAPILIELLKStikKFFGENPRES-------KSMARILNKKHFQRLSNLLKDPrvaasivhGGSIDEK-----KLFI 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 361 SPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSPTKG 440
Cdd:PLN02203  329 EPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYA 408

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1069468527 441 ND-MPFGGWKGSGIGResYIG--GVESFMEDKAVL 472
Cdd:PLN02203  409 CDsLPFGGVGESGFGR--YHGkySFDTFSHEKAVL 441
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
 59-454 1.71e-28

trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 119.69  E-value: 1.71e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527   59 PAWSALSPKERSVYLARLGVLFAEHSAELAQLEAKSMGRpvtSFFDAGA----ASDYFRYFSEAAypmgtsslnTPGFVN 134
Cdd:PRK11809   696 PIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGK---TFSNAIAevreAVDFLRYYAGQV---------RDDFDN 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  135 mGVKQPYG--VCgiIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHG-AAGA 211
Cdd:PRK11809   764 -DTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGeTVGA 840

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  212 VMSSHMDIRIISFTGSTRTGRAIQKAAADsNLKN------CIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFA 285
Cdd:PRK11809   841 ALVADARVRGVMFTGSTEVARLLQRNLAG-RLDPqgrpipLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSA 919

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  286 NSRIYVHKSIAQTFIEGFKTKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKITE-DLPNV----SGLYI 360
Cdd:PRK11809   920 LRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQaARENSedwqSGTFV 999

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  361 SPT-IFTDTPEDaqiMKEEIFGPVVHINTFEGEA--EAIAKANDTEYGLYASVFTKdIDRAM-RVSKQLEAGTVGVNcss 436
Cdd:PRK11809  1000 PPTlIELDSFDE---LKREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTR-IDETIaQVTGSAHVGNLYVN--- 1072

                          410       420
                   ....*....|....*....|....*.
gi 1069468527  437 ptkgNDM--------PFGGWKGSGIG 454
Cdd:PRK11809  1073 ----RNMvgavvgvqPFGGEGLSGTG 1094
PLN02174 PLN02174
aldehyde dehydrogenase family 3 member H1
 137-474 2.03e-27

aldehyde dehydrogenase family 3 member H1


Pssm-ID: 177831  Cd Length: 484  Bit Score: 114.76  E-value: 2.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 137 VKQPYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSSH 216
Cdd:PLN02174  109 VSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTETTALLEQK 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 217 MDIriISFTGSTRTGRAIQKAAAdSNLKNCIFELGGKSPALVFEDADIEQAIQATVP-SIGWNSGQTCFANSRIYVHKSI 295
Cdd:PLN02174  189 WDK--IFYTGSSKIGRVIMAAAA-KHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAgKWGCNNGQACISPDYILTTKEY 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 296 AQTFIEGFKTKFMSAKLGDPTQAgTTQGPQADKVQHETVKRYLALAEKSGTKITEDLPNVSGLYISPTIFTDTPEDAQIM 375
Cdd:PLN02174  266 APKVIDAMKKELETFYGKNPMES-KDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTILLDVPLDSLIM 344

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 376 KEEIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVN-CSSPTKGNDMPFGGWKGSGIG 454
Cdd:PLN02174  345 SEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFGGVGESGMG 424

                         330       340
                  ....*....|....*....|
gi 1069468527 455 RESYIGGVESFMEDKAVLIK 474
Cdd:PLN02174  425 AYHGKFSFDAFSHKKAVLYR 444
PRK11903 PRK11903
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
11-462 1.83e-16

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;


Pssm-ID: 237016 [Multi-domain]  Cd Length: 521  Bit Score: 81.67  E-value: 1.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  11 FINGKFQAIDESQTfDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARL-GVLFAEHSAELAQ 89
Cdd:PRK11903    8 YVAGRWQAGSGAGT-PLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIvKVLQANRDAYYDI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  90 LEAKSMGRPVTSFFDAGAASDYFRYFSEAAYPMGTSSL----------NTPGFVNMGVKQP-YGVCGIIIPWNAPLIFFS 158
Cdd:PRK11903   87 ATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDARLlrdgeavqlgKDPAFQGQHVLVPtRGVALFINAFNFPAWGLW 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 159 KKGAAALAAGNTVVLK-SSEKAPLTCAKAAELVAKAGFPPGVFNILSGhgAAGAVMSSHMDIRIISFTGSTRTGRAIQK- 236
Cdd:PRK11903  167 EKAAPALLAGVPVIVKpATATAWLTQRMVKDVVAAGILPAGALSVVCG--SSAGLLDHLQPFDVVSFTGSAETAAVLRSh 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 237 -AAADSNLKNCIfELGGKSPALVFEDAD-----IEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKFMSA 310
Cdd:PRK11903  245 pAVVQRSVRVNV-EADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKT 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 311 KLGDPTQAGTTQGPQADKVQHETVKRYLA-LAEKS------GTKITEDLPNVSGLYISPTIF-TDTPEDAQIMKE-EIFG 381
Cdd:PRK11903  324 TVGNPRNDGVRMGPLVSRAQLAAVRAGLAaLRAQAevlfdgGGFALVDADPAVAACVGPTLLgASDPDAATAVHDvEVFG 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 382 PVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRVSKQL-------EAGTVGVNCSSPTKGNDMP---FGGWKGS 451
Cdd:PRK11903  404 PVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELadshgrvHVISPDVAALHTGHGNVMPqslHGGPGRA 483

                         490
                  ....*....|.
gi 1069468527 452 GIGREsyIGGV 462
Cdd:PRK11903  484 GGGEE--LGGL 492
ALDH_KGSADH cd07129
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...
 168-433 7.44e-15

Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.


Pssm-ID: 143447 [Multi-domain]  Cd Length: 454  Bit Score: 76.43  E-value: 7.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 168 GNTVVLKSSEKAPLTCAKAAELVAKA----GFPPGVFNILSGHG-AAGAVMSSHMDIRIISFTGSTRTGRAIQKAAADSN 242
Cdd:cd07129   135 GCPVVVKAHPAHPGTSELVARAIRAAlratGLPAGVFSLLQGGGrEVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARP 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 243 LKNCIF-ELGGKSPALVFEDADIEQA---IQATVPSIGWNSGQTCFANSRIYVHKSIA-QTFIEGFKTKFMSAKLGDPTQ 317
Cdd:cd07129   215 EPIPFYaELGSVNPVFILPGALAERGeaiAQGFVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQTMLT 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 318 AGTTQGPQADKVQHETVKRYLALAEKSGTkitedlpnVSGLYISPTIFTDTPEDA---QIMKEEIFGPVVHINTFEGEAE 394
Cdd:cd07129   295 PGIAEAYRQGVEALAAAPGVRVLAGGAAA--------EGGNQAAPTLFKVDAAAFladPALQEEVFGPASLVVRYDDAAE 366

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1069468527 395 AIAKANDTEYGLYASVF--TKDIDRAMRVSKQLE--AGTVGVN 433
Cdd:cd07129   367 LLAVAEALEGQLTATIHgeEDDLALARELLPVLErkAGRLLFN 409
ALDH_MaoC-N cd07128
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ...
 11-421 8.38e-15

N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.


Pssm-ID: 143446 [Multi-domain]  Cd Length: 513  Bit Score: 76.54  E-value: 8.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  11 FINGKFQAIDESQTfDLHSPSTGEFIAKVPEATAKDVDAAVAAAKAAFPAWSALSPKERSVYLARLGVLFAEHSAELAQL 90
Cdd:cd07128     4 YVAGQWHAGTGDGR-TLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLYAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  91 EAKSMGRPVTSFFDA-GAASDYFRYFSEAAYPMGTSSLNTPG----------FVNMGVKQP-YGVCGIIIPWNAPLIFFS 158
Cdd:cd07128    83 SAATGATRRDSWIDIdGGIGTLFAYASLGRRELPNAHFLVEGdveplskdgtFVGQHILTPrRGVAVHINAFNFPVWGML 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 159 KKGAAALAAGNTVVLK-SSEKAPLTCAKAAELVAKAGFPPGVFNILSGhgAAGAVMSsHMDIR-IISFTGSTRTGRAIQK 236
Cdd:cd07128   163 EKFAPALLAGVPVIVKpATATAYLTEAVVKDIVESGLLPEGALQLICG--SVGDLLD-HLGEQdVVAFTGSAATAAKLRA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 237 ------------AAADSnLKNCIfeLGgksPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFK 304
Cdd:cd07128   240 hpnivarsirfnAEADS-LNAAI--LG---PDATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALK 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 305 TKFMSAKLGDPTQAGTTQGPQADKVQHETVKRYLALAEKSGTKITEDLPNVS--------GLYISPTIFT-DTPEDAQIM 375
Cdd:cd07128   314 ARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEvvgadaekGAFFPPTLLLcDDPDAATAV 393

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1069468527 376 KE-EIFGPVVHINTFEGEAEAIAKANDTEYGLYASVFTKDIDRAMRV 421
Cdd:cd07128   394 HDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFAREL 440
ALDH_PAD-PaaZ cd07127
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ...
 59-435 4.52e-10

Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.


Pssm-ID: 143445  Cd Length: 549  Bit Score: 61.73  E-value: 4.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  59 PAWSALSPKERSVY----LARLgvlfAEHSAELAQLEAKSMGRPVTSFFDAGAASDYFRYFSEAAYPM-------GTSSL 127
Cdd:cd07127    98 PGWRDAGARARAGVcleiLQRL----NARSFEMAHAVMHTTGQAFMMAFQAGGPHAQDRGLEAVAYAWremsripPTAEW 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 128 NTPGFVNMGVKQ-------PYGV-----CGIIIPWNA-PLIFFSkkgaaaLAAGNTVVLKSSEKAPLTCA----KAAELV 190
Cdd:cd07127   174 EKPQGKHDPLAMektftvvPRGValvigCSTFPTWNGyPGLFAS------LATGNPVIVKPHPAAILPLAitvqVAREVL 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 191 AKAGFPPGVFNILS---GHGAAGAvMSSHMDIRIISFTGSTRTGRAIQKAAADSNLKNcifELGGKSPALVFEDADIEQA 267
Cdd:cd07127   248 AEAGFDPNLVTLAAdtpEEPIAQT-LATRPEVRIIDFTGSNAFGDWLEANARQAQVYT---EKAGVNTVVVDSTDDLKAM 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 268 IQATVPSIGWNSGQTCFANSRIYV----------HKS---IAQTFIEGfktkfMSAKLGDPTQAGTTQGpqadKVQHETV 334
Cdd:cd07127   324 LRNLAFSLSLYSGQMCTTPQNIYVprdgiqtddgRKSfdeVAADLAAA-----IDGLLADPARAAALLG----AIQSPDT 394

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 335 KRYLALAEKSGTKITEDL----PNVSGLYI-SPTIFTDTPEDAQIMKEEIFGPVVHINTFEGEAEAIAKANDT--EYG-L 406
Cdd:cd07127   395 LARIAEARQLGEVLLASEavahPEFPDARVrTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESvrEHGaM 474

                         410       420
                  ....*....|....*....|....*....
gi 1069468527 407 YASVFTKDIDRAMRVskQLEAGTVGVNCS 435
Cdd:cd07127   475 TVGVYSTDPEVVERV--QEAALDAGVALS 501
ALDH_F12_P5CDH cd07126
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ...
 72-454 2.37e-09

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.


Pssm-ID: 143444  Cd Length: 489  Bit Score: 59.43  E-value: 2.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  72 YLARLGVLFAEHSAELAQLEAKsmgrpVTSFFDAGAASDYFRYFseaaypmgTSSLNTPGFV----NMGVKQPYGVCGII 147
Cdd:cd07126    83 FFARLIQRVAPKSDAQALGEVV-----VTRKFLENFAGDQVRFL--------ARSFNVPGDHqgqqSSGYRWPYGPVAII 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 148 IPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSSHMDIRIISFTGS 227
Cdd:cd07126   150 TPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGS 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 228 TRTGRAIQKaaadsnlkncifELGGKspaLVFEDADIEQAIQA----TVPSIGWN--------SGQTCFANSRIYVHKSI 295
Cdd:cd07126   230 SKVAERLAL------------ELHGK---VKLEDAGFDWKILGpdvsDVDYVAWQcdqdayacSGQKCSAQSILFAHENW 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 296 AQTFIEGfKTKFMSA--KLGD----PTQAGTTQGPQadkvqhETVKRYLAL----AEKSGTKITE-DLPNVSGLYISPTI 364
Cdd:cd07126   295 VQAGILD-KLKALAEqrKLEDltigPVLTWTTERIL------DHVDKLLAIpgakVLFGGKPLTNhSIPSIYGAYEPTAV 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 365 F-----TDTPEDAQIMKEEIFGPVVHINTFEGEAE--AIAKANDTEYGLYASVFTKDIDRAMRVSKQLEAGTVGVNCSSP 437
Cdd:cd07126   368 FvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTYAGIRAR 447

                         410       420
                  ....*....|....*....|..
gi 1069468527 438 TKGNDM-----PFGGWKGSGIG 454
Cdd:cd07126   448 TTGAPQnhwfgPAGDPRGAGIG 469
ALDH-like cd07077
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ...
 140-388 3.50e-09

NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143396 [Multi-domain]  Cd Length: 397  Bit Score: 58.39  E-value: 3.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 140 PYGVCGIIIPWNAPLIFFSKkGAAALAAGNTVVLKSSEKAPLTcAKAAELVAKAGFPPGVFNILSGHGAAGAV-----MS 214
Cdd:cd07077   100 PIGVTMHILPSTNPLSGITS-ALRGIATRNQCIFRPHPSAPFT-NRALALLFQAADAAHGPKILVLYVPHPSDelaeeLL 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 215 SHMDIRIISFTGSTRTGRAIQKAaadSNLKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNsGQTCFANSRIYVHKS 294
Cdd:cd07077   178 SHPKIDLIVATGGRDAVDAAVKH---SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYVVDD 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 295 IAQTFIEGFKTKFMSAKLGDPTQ---AGTTQGPQADKVQHETVKRYLALAE----KSGTKITEDLPNVSGLYISPTIFTD 367
Cdd:cd07077   254 VLDPLYEEFKLKLVVEGLKVPQEtkpLSKETTPSFDDEALESMTPLECQFRvldvISAVENAWMIIESGGGPHTRCVYTH 333

                         250       260
                  ....*....|....*....|.
gi 1069468527 368 TPEDAQIMKEEIFGPVVHINT 388
Cdd:cd07077   334 KINKVDDFVQYIDTASFYPNE 354
ALDH_F20_ACDH_EutE-like cd07081
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ...
 85-460 1.38e-06

Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.


Pssm-ID: 143400 [Multi-domain]  Cd Length: 439  Bit Score: 50.34  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527  85 AELAQLEAkSMGRPVTSFFDAGAASDYFRYFSEAAYPMGTSSLNTPGFVnMGVKQPYGVCGIIIPWNAPLIFFSKKGAAA 164
Cdd:cd07081    42 AKLAVSET-GMGRVEDKVIKNHFAAEYIYNVYKDEKTCGVLTGDENGGT-LIIAEPIGVVASITPSTNPTSTVIFKSLIS 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 165 LAAGNTVVLKSSEKAPLTCAKAAELVAKAGFPPGVFNILSGHGAAGAVMSS-----HMDIRIISFTGstrtGRAIQKAAA 239
Cdd:cd07081   120 LKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAqrlmkFPGIGLLLATG----GPAVVKAAY 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 240 DSNlKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKSIAQTFIEGFKTKfmsaklgdptQAG 319
Cdd:cd07081   196 SSG-KPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQ----------GAY 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 320 TTQGPQADKVQHETVKR---YLALAEKSGTKITE----DLPNVSGLYISPTIFTDTPEDAQIMKEEIFGPVVHINTFEgE 392
Cdd:cd07081   265 KLTAEELQQVQPVILKNgdvNRDIVGQDAYKIAAaaglKVPQETRILIGEVTSLAEHEPFAHEKLSPVLAMYRAANFA-D 343

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1069468527 393 AEAIAKANDTEYGLY--ASVFT---KDIDRAMRVSKQLEAGTVGVN--CSSPTKGNDMPFGGWKGSGIGRESYIG 460
Cdd:cd07081   344 ADAKALALKLEGGCGhtSAMYSdniKAIENMNQFANAMKTSRFVKNgpCSQGGLGDLYNFRGWPSMTLGCGTWGG 418
PRK15398 PRK15398
aldehyde dehydrogenase;
140-417 3.08e-04

aldehyde dehydrogenase;


Pssm-ID: 237956  Cd Length: 465  Bit Score: 42.97  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 140 PYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAEL----VAKAGfppGVFNILS-----GHGAAG 210
Cdd:PRK15398  129 PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELlneaIVAAG---GPENLVVtvaepTIETAQ 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 211 AVMsSHMDIRIISFTGstrtGRAIQKAAADSNlKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIY 290
Cdd:PRK15398  206 RLM-KHPGIALLVVTG----GPAVVKAAMKSG-KKAIGAGAGNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVI 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 291 VHKSIAQTFIEGFK-------TKFMSAKLgdpTQAGTTQGPQADKvqhETV-KRYLALAEKSGTKITEDLpnvsglyisP 362
Cdd:PRK15398  280 VVDSVADELMRLMEkngavllTAEQAEKL---QKVVLKNGGTVNK---KWVgKDAAKILEAAGINVPKDT---------R 344

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 363 TIFTDTPEDAQIMKEEI---FGPVVHINTFEgeaEAIAKANDTEYGLY--ASVFTKDIDR 417
Cdd:PRK15398  345 LLIVETDANHPFVVTELmmpVLPVVRVKDVD---EAIALAVKLEHGNRhtAIMHSRNVDN 401
ALDH_EutE cd07121
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ...
 140-417 1.87e-03

Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.


Pssm-ID: 143439 [Multi-domain]  Cd Length: 429  Bit Score: 40.68  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 140 PYGVCGIIIPWNAPLIFFSKKGAAALAAGNTVVLKSSEKAPLTCAKAAEL----VAKAGFPPGVFNILSGHG-AAGAVMS 214
Cdd:cd07121    97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELinkaIAEAGGPDNLVVTVEEPTiETTNELM 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 215 SHMDIRIISFTGstrtGRAIQKAAADSNlKNCIFELGGKSPALVFEDADIEQAIQATVPSIGWNSGQTCFANSRIYVHKS 294
Cdd:cd07121   177 AHPDINLLVVTG----GPAVVKAALSSG-KKAIGAGAGNPPVVVDETADIEKAARDIVQGASFDNNLPCIAEKEVIAVDS 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069468527 295 IAQTFIEGFK--------TKFMSAKLGDPTQAGTTQGPQADKVQHETVKrylaLAEKSGTKITEDLpnvsglyisPTIFT 366
Cdd:cd07121   252 VADYLIAAMQrngayvlnDEQAEQLLEVVLLTNKGATPNKKWVGKDASK----ILKAAGIEVPADI---------RLIIV 318

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1069468527 367 DTPEDAQIMKEEI---FGPVVHINTFEgeaEAIAKANDTEYGLY--ASVFTKDIDR 417
Cdd:cd07121   319 ETDKDHPFVVEEQmmpILPVVRVKNFD---EAIELAVELEHGNRhtAIIHSKNVEN 371
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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