|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
19-472 |
0e+00 |
|
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: 771.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 19 PLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGE 98
Cdd:cd07149 2 EVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 99 VDRTVQTYKFAAEEAKRIYGETLPLDAAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQ 178
Cdd:cd07149 82 VDRAIETLRLSAEEAKRLAGETIPFDASPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 179 TPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAGLKRVTLELGSNAAVIIDE 258
Cdd:cd07149 162 TPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLKKVTLELGSNAAVIVDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 259 DVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQ 338
Cdd:cd07149 242 DADL-EKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 339 EAIKEGATVLCGGkKRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAM 418
Cdd:cd07149 321 EAVEGGARLLTGG-KRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKAL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 446639112 419 RAIDELEVGGVMINDIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07149 400 KAARELEVGGVMINDSSTFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
19-472 |
0e+00 |
|
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: 599.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 19 PLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGE 98
Cdd:cd07147 2 EVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 99 VDRTVQTYKFAAEEAKRIYGETLPLDAAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQ 178
Cdd:cd07147 82 VARAIDTFRIAAEEATRIYGEVLPLDISARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 179 TPLSSYALVELFEEAGLPNGALNIIsgPGSTVG-EAIVKNDYVASITFTGSPKVGIGIKQKAGLKRVTLELGSNAAVIID 257
Cdd:cd07147 162 TPLSALILGEVLAETGLPKGAFSVL--PCSRDDaDLLVTDERIKLLSFTGSPAVGWDLKARAGKKKVVLELGGNAAVIVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 258 EDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWV 337
Cdd:cd07147 240 SDADL-DFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 338 QEAIKEGATVLCGGkKRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKA 417
Cdd:cd07147 319 NEAVDAGAKLLTGG-KRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446639112 418 MRAIDELEVGGVMINDIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07147 398 LRAWDELEVGGVVINDVPTFRVDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
2-473 |
0e+00 |
|
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: 588.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 2 KKHLYINGDWKSVNT--YKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREE 79
Cdd:COG1012 5 EYPLFIGGEWVAAASgeTFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 80 FAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPLDAapgaDGRIAYTIRKPIGVIGAITPFNFPLNLVAH 159
Cdd:COG1012 85 LAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDA----PGTRAYVRREPLGVVGAITPWNFPLALAAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 160 KVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKA 239
Cdd:COG1012 161 KLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 240 G--LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLE 317
Cdd:COG1012 241 AenLKRVTLELGGKNPAIVLDDADL-DAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 318 ETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDA---RIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEA 394
Cdd:COG1012 320 GTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeggYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446639112 395 IEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCIK 473
Cdd:COG1012 400 IALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
19-470 |
0e+00 |
|
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: 576.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 19 PLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGE 98
Cdd:pfam00171 10 EVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 99 VDRTVQTYKFAAEEAKRIYGETLPLDAapgadGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQ 178
Cdd:pfam00171 90 VDRAIDVLRYYAGLARRLDGETLPSDP-----GRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 179 TPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVII 256
Cdd:pfam00171 165 TPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAqnLKRVTLELGGKNPLIV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 257 DEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHEtKMH-EFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDM 335
Cdd:pfam00171 245 LEDADL-DAAVEAAVFGAFGNAGQVCTATSRLLVHE-SIYdEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 336 WVQEAIKEGATVLCGGK--KRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNN 413
Cdd:pfam00171 323 YVEDAKEEGAKLLTGGEagLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSD 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446639112 414 LFKAMRAIDELEVGGVMINDIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLV 470
Cdd:pfam00171 403 LERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| lactal_redase_Meth |
NF040648 |
lactaldehyde dehydrogenase; |
5-472 |
0e+00 |
|
lactaldehyde dehydrogenase;
Pssm-ID: 468615 [Multi-domain] Cd Length: 463 Bit Score: 526.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDWKSVNTYkPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEII 84
Cdd:NF040648 1 MFINGKWIDREDI-DVINPYNLEVIDKIPSLSREEVKEAIEIANEAKEVMKNLSPRKRYNILMDIAEELKKNKEELAKLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 85 AKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPLDAapgadgRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPA 164
Cdd:NF040648 80 TIDAGKPIKQSIIEVDRSIETFKLAAFYAKEIRGETIPSDA------GLIFTKKEPLGVVGAITPFNYPLNLAAHKIAPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 165 IAAGNTVVLKPADQTPLSSYALVELFEEA----GLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG 240
Cdd:NF040648 154 IATGNSVVLHPSSKAPLAAIELAKIIEKVlkkmNIPLGVFNLVTGYGEVVGDEIVKNEKVNKISFTGSVEVGESISKKAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 241 LKRVTLELGSNAAVIIDEDVELTDEIIERVKwGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETD 320
Cdd:NF040648 234 MKKITLELGGNNPLIVLKDADIEKAVESAVK-GSFLNSGQVCISVGRVIVEEEIADEFIKKLVEETKKLKVGNPLDEKTD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 321 VSALISKRDVERIDMWVQEAIKEGATVLCGGkKRDARIFEPTVLkNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNN 400
Cdd:NF040648 313 IGPLITEEAAIRVENLVNEAIEEGAKLLCGG-NREGSLFYPTVL-DVDEDNILVKVETFGPVLPIIRVKDIDEAIEIANN 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446639112 401 SRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:NF040648 391 TKYGLQAGVFTNDINKALKFADELEYGGVIINKSSTFRTDNMPFGGFKKSGLGKEGIKYAVEEMTEIKTIVI 462
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
23-472 |
0e+00 |
|
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: 525.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRT 102
Cdd:cd07094 6 PYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 103 VQTYKFAAEEAKRIYGETLPLDAAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLS 182
Cdd:cd07094 86 IDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 183 SYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAGLKRVTLELGSNAAVIIDEDVEL 262
Cdd:cd07094 166 ALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVIVDRDADL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 263 tDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEAIK 342
Cdd:cd07094 246 -DAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 343 EGATVLCGGkKRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAID 422
Cdd:cd07094 325 AGARLLCGG-ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAE 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446639112 423 ELEVGGVMINDIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07094 404 KLEVGGVMVNDSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
42-472 |
5.65e-179 |
|
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: 507.90 E-value: 5.65e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 42 EAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETL 121
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 122 PldaaPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALN 201
Cdd:cd07078 82 P----SPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 202 IISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNG 279
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAenLKRVTLELGGKSPLIVFDDADL-DAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 280 QVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDARI- 358
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKg 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 359 --FEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPT 436
Cdd:cd07078 317 yfVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 446639112 437 FRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07078 397 GAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
19-472 |
6.96e-178 |
|
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: 506.12 E-value: 6.96e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 19 PLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGE 98
Cdd:cd07145 2 EVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 99 VDRTVQTYKFAAEEAKRIYGETLPLDAAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQ 178
Cdd:cd07145 82 VERTIRLFKLAAEEAKVLRGETIPVDAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 179 TPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVII 256
Cdd:cd07145 162 TPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGgtGKKVALELGGSDPMIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 257 --DEDVELTDEIIERvkwGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERID 334
Cdd:cd07145 242 lkDADLERAVSIAVR---GRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 335 MWVQEAIKEGATVLCGGKKRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNL 414
Cdd:cd07145 319 NLVNDAVEKGGKILYGGKRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDI 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446639112 415 FKAMRAIDELEVGGVMINDIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07145 399 NRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
23-472 |
2.06e-164 |
|
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: 471.53 E-value: 2.06e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRT 102
Cdd:cd07103 4 PATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 103 VQTYKFAAEEAKRIYGETLPldaAPGADGRIaYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLS 182
Cdd:cd07103 84 ASFLEWFAEEARRIYGRTIP---SPAPGKRI-LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 183 SYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVG-IGIKQKA-GLKRVTLELGSNAAVIIDEDV 260
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGkLLMAQAAdTVKRVSLELGGNAPFIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 261 ELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEA 340
Cdd:cd07103 240 DL-DKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 341 IKEGATVLCGGKKRDAR--IFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAM 418
Cdd:cd07103 319 VAKGAKVLTGGKRLGLGgyFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 446639112 419 RAIDELEVGGVMINDiPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07103 399 RVAEALEAGMVGINT-GLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
23-472 |
3.15e-157 |
|
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: 453.35 E-value: 3.15e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNamtKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRT 102
Cdd:cd07146 6 PYTGEVVGTVPAGTEEALREALALAAS---YRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 103 VQTYKFAAEEAKRIYGETLPLDAAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLS 182
Cdd:cd07146 83 ADVLRFAAAEALRDDGESFSCDLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 183 SYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAGLKRVTLELGSNAAVIIDEDVEL 262
Cdd:cd07146 163 AIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLIVMDDADL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 263 tDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEAIK 342
Cdd:cd07146 243 -ERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 343 EGATVLCGGKKRDArIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAID 422
Cdd:cd07146 322 QGARVLLGNQRQGA-LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446639112 423 ELEVGGVMINDIPTFRVDHMPYGGVKESGTG-REGIKYAIEEMTEMKLVCI 472
Cdd:cd07146 401 RLDVGTVNVNEVPGFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
21-472 |
7.39e-148 |
|
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: 429.68 E-value: 7.39e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 21 YAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAAR-GEV 99
Cdd:cd07093 2 FNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 100 DRTVQTYKFAAEEAKRIYGETLPLDaapgaDGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQT 179
Cdd:cd07093 82 PRAAANFRFFADYILQLDGESYPQD-----GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 180 PLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKA--GLKRVTLELGSNAAVIID 257
Cdd:cd07093 157 PLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAapNLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 258 EDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWV 337
Cdd:cd07093 237 ADADL-DRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 338 QEAIKEGATVLCGGKKRDARIF------EPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFT 411
Cdd:cd07093 316 ELARAEGATILTGGGRPELPDLeggyfvEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446639112 412 NNLFKAMRAIDELEVGGVMINdipTFRVDH--MPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07093 396 RDLGRAHRVARRLEAGTVWVN---CWLVRDlrTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
5-470 |
3.06e-146 |
|
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: 426.24 E-value: 3.06e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDW---KSVNTYkPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAM--TKMNTLSAYDRATILEKVAQKMDERREE 79
Cdd:cd07091 6 LFINNEFvdsVSGKTF-PTINPATEEVICQVAEADEEDVDAAVKAARAAFetGWWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 80 FAEIIAKEAAKPIR-AARGEVDRTVQTYKFAAEEAKRIYGETLPLDaapgaDGRIAYTIRKPIGVIGAITPFNFPLNLVA 158
Cdd:cd07091 85 LAALESLDNGKPLEeSAKGDVALSIKCLRYYAGWADKIQGKTIPID-----GNFLAYTRREPIGVCGQIIPWNFPLLMLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 159 HKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQK 238
Cdd:cd07091 160 WKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 239 AG---LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPL 315
Cdd:cd07091 240 AAksnLKKVTLELGGKSPNIVFDDADL-DKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 316 LEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDAR--IFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDE 393
Cdd:cd07091 319 DPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKgyFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446639112 394 AIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINdipTFRVDH--MPYGGVKESGTGREGIKYAIEEMTEMKLV 470
Cdd:cd07091 399 VIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN---TYNVFDaaVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
39-472 |
5.28e-143 |
|
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: 416.55 E-value: 5.28e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 39 DVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYG 118
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 119 ETLPLDAApgadGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSS-YALVELFEEAGLPN 197
Cdd:cd07104 81 EILPSDVP----GKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 198 GALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVII--DEDVELTDEIIervKWG 273
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGrhLKKVALELGGNNPLIVldDADLDLAVSAA---AFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 274 AFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKk 353
Cdd:cd07104 234 AFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 354 RDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIND 433
Cdd:cd07104 313 YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 446639112 434 IPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07104 393 QTVNDEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
6-470 |
1.45e-141 |
|
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: 414.36 E-value: 1.45e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 6 YINGDW--KSVNTYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEI 83
Cdd:cd07088 1 YINGEFvpSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 84 IAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPLDAApgadGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGP 163
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRP----NENIFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 164 AIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--L 241
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAenI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 242 KRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDV 321
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADL-DLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 322 SALISKRDVERIDMWVQEAIKEGATVLCGGKKRDAR---IFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQV 398
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEkgyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446639112 399 NNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDiPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLV 470
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINR-ENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
6-473 |
3.77e-141 |
|
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: 413.51 E-value: 3.77e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 6 YINGDWK-SVNTYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTK-MNTLSAYDRATILEKVAQKMDERREEFAEI 83
Cdd:cd07082 5 LINGEWKeSSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGwWPTMPLEERIDCLHKFADLLKENKEEVANL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 84 IAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPLDAAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGP 163
Cdd:cd07082 85 LMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 164 AIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAGLKR 243
Cdd:cd07082 165 ALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMKR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 244 VTLELGSNAAVII--DEDVELT-DEIIErvkwGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETD 320
Cdd:cd07082 245 LVLELGGKDPAIVlpDADLELAaKEIVK----GALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 321 VSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNN 400
Cdd:cd07082 321 ITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANK 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446639112 401 SRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCIK 473
Cdd:cd07082 401 SNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
23-472 |
2.69e-139 |
|
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: 407.96 E-value: 2.69e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAV-TAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDR 101
Cdd:cd07148 6 PFDLKPIGEVPTVDWAAIDKALdTAHALFLDRNNWLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 102 TVQTYKFAAEEAKRIYGETLPLDAAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPL 181
Cdd:cd07148 86 AIDGVELAADELGQLGGREIPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 182 SSYALVELFEEAGLPNGALNIISgPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQK-AGLKRVTLELGSNAAVIIDEDV 260
Cdd:cd07148 166 SCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKlAPGTRCALEHGGAAPVIVDRSA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 261 ELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEA 340
Cdd:cd07148 245 DL-DAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 341 IKEGATVLCGGKKRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRA 420
Cdd:cd07148 324 VAAGARLLCGGKRLSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKA 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 446639112 421 IDELEVGGVMINDIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07148 404 VRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
23-472 |
2.71e-139 |
|
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: 407.87 E-value: 2.71e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRT 102
Cdd:cd07150 6 PADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 103 VQTYKFAAEEAKRIYGETLPLDAApgadGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLS 182
Cdd:cd07150 86 PELLRAAAGECRRVRGETLPSDSP----GTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 183 SYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDV 260
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGrhLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 261 ELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEA 340
Cdd:cd07150 242 DL-DYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 341 IKEGATVLCGGkKRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRA 420
Cdd:cd07150 321 VAKGAKLLTGG-KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 446639112 421 IDELEVGGVMINDIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07150 400 AERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
45-472 |
1.14e-136 |
|
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: 398.14 E-value: 1.14e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 45 TAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPld 124
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 125 aaPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIIS 204
Cdd:cd06534 79 --SPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 205 GPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVC 282
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAenLKPVTLELGGKSPVIVDEDADL-DAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 283 ISVQRVFVHETKMHEFLSKLKkamesvvvgdplleetdvsaliskrdveridmwvqeaikegatvlcggkkrdarifepT 362
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------T 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 363 VLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFRVDHM 442
Cdd:cd06534 258 VLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEA 337
|
410 420 430
....*....|....*....|....*....|
gi 446639112 443 PYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd06534 338 PFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
6-470 |
1.53e-136 |
|
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: 401.63 E-value: 1.53e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 6 YINGDWKSVNTYKPLYAPYS-EETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEII 84
Cdd:cd07097 4 YIDGEWVAGGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 85 AKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPldaaPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPA 164
Cdd:cd07097 84 TREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLP----STRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 165 IAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LK 242
Cdd:cd07097 160 LAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAarGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 243 RVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVS 322
Cdd:cd07097 240 RVQLEMGGKNPLVVLDDADL-DLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 323 ALISKRDVERIDMWVQEAIKEGATVLCGGK--KRDAR--IFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQV 398
Cdd:cd07097 319 PVVSERQLEKDLRYIEIARSEGAKLVYGGErlKRPDEgyYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446639112 399 NNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINdIPTFRVD-HMPYGGVKESGTG-REGIKYAIEEMTEMKLV 470
Cdd:cd07097 399 NDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVN-LPTAGVDyHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
23-472 |
6.48e-136 |
|
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: 399.12 E-value: 6.48e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARG-EVDR 101
Cdd:cd07115 4 PATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 102 TVQTYKFAAEEAKRIYGETLPLDAapgadGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPL 181
Cdd:cd07115 84 AADTFRYYAGWADKIEGEVIPVRG-----PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 182 SSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDED 259
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAgnLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 260 VELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQE 339
Cdd:cd07115 239 ADL-DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 340 AIKEGATVLCGGKKRDARIF--EPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKA 417
Cdd:cd07115 318 GREEGARLLTGGKRPGARGFfvEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446639112 418 MRAIDELEVGGVMINDIPTFRVDhMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07115 398 HRVAAALKAGTVWINTYNRFDPG-SPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
7-472 |
1.79e-134 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 397.14 E-value: 1.79e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 7 INGDWKSVNTYK--PLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEII 84
Cdd:PLN02278 29 IGGKWTDAYDGKtfPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 85 AKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPldaAPGADGRIaYTIRKPIGVIGAITPFNFPLNLVAHKVGPA 164
Cdd:PLN02278 109 TLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIP---SPFPDRRL-LVLKQPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 165 IAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LK 242
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAatVK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 243 RVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVS 322
Cdd:PLN02278 265 RVSLELGGNAPFIVFDDADL-DVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 323 ALISKRDVERIDMWVQEAIKEGATVLCGGK--KRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNN 400
Cdd:PLN02278 344 PLINEAAVQKVESHVQDAVSKGAKVLLGGKrhSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAND 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446639112 401 SRYGLQAGVFTNNLFKAMRAIDELEVGGVMIND--IPTfrvDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:PLN02278 424 TEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEglIST---EVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
6-470 |
4.04e-133 |
|
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: 392.87 E-value: 4.04e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 6 YINGDW---KSVNTYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAE 82
Cdd:cd07131 2 YIGGEWvdsASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 83 IIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPLDAaPGADgriAYTIRKPIGVIGAITPFNFPLNLVAHKVG 162
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSEL-PNKD---AMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 163 PAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG-- 240
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCArp 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 241 LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETD 320
Cdd:cd07131 238 NKRVALEMGGKNPIIVMDDADL-DLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 321 VSALISKRDVERIDMWVQEAIKEGATVLCGGKK------RDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEA 394
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERltgggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446639112 395 IEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINdIPTFRVD-HMPYGGVKESGTG-REGIKYAIEEMTEMKLV 470
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN-APTIGAEvHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
5-470 |
6.37e-133 |
|
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: 391.87 E-value: 6.37e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDWKSVNT--YKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAE 82
Cdd:cd07138 1 FYIDGAWVAPAGteTIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 83 IIAKEAAKPIRAARG-EVDRTVQTYKFAAEEAKriygeTLPLDAAPGaDGRIaytIRKPIGVIGAITPFNFPLNLVAHKV 161
Cdd:cd07138 81 AITLEMGAPITLARAaQVGLGIGHLRAAADALK-----DFEFEERRG-NSLV---VREPIGVCGLITPWNWPLNQIVLKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 162 GPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG- 240
Cdd:cd07138 152 APALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAAd 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 241 -LKRVTLELGSNAAVIIDEDVELTdeiiERVKWG---AFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLL 316
Cdd:cd07138 232 tVKRVALELGGKSANIILDDADLE----KAVPRGvaaCFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 317 EETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDARI-----FEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEF 391
Cdd:cd07138 308 PATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEGLergyfVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446639112 392 DEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPtFRVdHMPYGGVKESGTGREGIKYAIEEMTEMKLV 470
Cdd:cd07138 388 DEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAA-FNP-GAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
23-474 |
1.12e-130 |
|
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: 386.27 E-value: 1.12e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRT 102
Cdd:cd07151 17 PYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 103 VQTYKFAAEEAKRIYGETLPLDAaPGADGRIaytIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLS 182
Cdd:cd07151 97 MAITREAATFPLRMEGRILPSDV-PGKENRV---YREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPIT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 183 SYALV-ELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDED 259
Cdd:cd07151 173 GGLLLaKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGrhLKKVALELGGNNPFVVLED 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 260 VELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQE 339
Cdd:cd07151 253 ADI-DAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 340 AIKEGATVLCGGKkRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMR 419
Cdd:cd07151 332 AVEEGATLLVGGE-AEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQ 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446639112 420 AIDELEVGGVMINDIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCIKK 474
Cdd:cd07151 411 FARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQH 465
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
23-472 |
5.81e-130 |
|
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: 384.21 E-value: 5.81e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMN--TLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVD 100
Cdd:cd07114 4 PATGEPWARVPEASAADVDRAVAAARAAFEGGAwrKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 101 RTVQTYKFAAEEAKRIYGETLPLDAAPgadgRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTP 180
Cdd:cd07114 84 YLAEWYRYYAGLADKIEGAVIPVDKGD----YLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 181 LSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDE 258
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAenLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 259 DVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQ 338
Cdd:cd07114 240 DADL-DAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 339 EAIKEGATVLCGGKKRDARI------FEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTN 412
Cdd:cd07114 319 RAREEGARVLTGGERPSGADlgagyfFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTR 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446639112 413 NLFKAMRAIDELEVGGVMINdipTFRVDH--MPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07114 399 DLARAHRVARAIEAGTVWVN---TYRALSpsSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
23-472 |
1.24e-127 |
|
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: 378.22 E-value: 1.24e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMN--TLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVD 100
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPwpRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 101 RTVQTYKFAAEEAKRIYGETLpldAAPGaDGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTP 180
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSY---NNLG-DDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 181 LSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDE 258
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAArnLKKVSLELGGKNPQIVFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 259 DVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQ 338
Cdd:cd07118 240 DADL-DAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 339 EAIKEGATVLCGGKK---RDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLF 415
Cdd:cd07118 319 AGRAEGATLLLGGERlasAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDID 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446639112 416 KAMRAIDELEVGGVMINDIPTFRVDhMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07118 399 TALTVARRIRAGTVWVNTFLDGSPE-LPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
23-472 |
2.80e-127 |
|
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: 377.33 E-value: 2.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTK--MNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIR-AARGEV 99
Cdd:cd07112 9 PATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISdALAVDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 100 DRTVQTYKFAAEEAKRIYGETlpldaAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQT 179
Cdd:cd07112 89 PSAANTFRWYAEAIDKVYGEV-----APTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 180 PLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG---LKRVTLELGSNAAVII 256
Cdd:cd07112 164 PLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqsnLKRVWLECGGKSPNIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 257 DEDVELTDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMW 336
Cdd:cd07112 244 FADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 337 VQEAIKEGATVLCGGKKRDAR----IFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTN 412
Cdd:cd07112 324 IESGKAEGARLVAGGKRVLTEtggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTS 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446639112 413 NLFKAMRAIDELEVGGVMIN-----DIPTfrvdhmPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07112 404 DLSRAHRVARRLRAGTVWVNcfdegDITT------PFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
6-472 |
3.83e-127 |
|
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: 377.81 E-value: 3.83e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 6 YINGDWKSVNT--YKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTK--MNTLSAYDRATILEKVAQKMDERREEFA 81
Cdd:cd07119 1 YIDGEWVEAASgkTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 82 EIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPldaapGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKV 161
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYD-----VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 162 GPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG- 240
Cdd:cd07119 156 APALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAg 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 241 -LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEET 319
Cdd:cd07119 236 nVKKVALELGGKNPNIVFADADF-ETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 320 DVSALISKRDVERIDMWVQEAIKEGATVLCGGKK------RDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDE 393
Cdd:cd07119 315 EMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRptgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 394 AIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDI-PTFrvDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07119 395 AIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYhPYF--AEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
5-473 |
4.09e-122 |
|
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: 365.13 E-value: 4.09e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDW-KSVNTYK-PLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAM---TKMNTLSAYDRATILEKVAQKMDERREE 79
Cdd:cd07141 9 IFINNEWhDSVSGKTfPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 80 FAEIIAKEAAKPIR-AARGEVDRTVQTYKFAAEEAKRIYGETLPldaapgADGRI-AYTIRKPIGVIGAITPFNFPLNLV 157
Cdd:cd07141 89 LASLETLDNGKPFSkSYLVDLPGAIKVLRYYAGWADKIHGKTIP------MDGDFfTYTRHEPVGVCGQIIPWNFPLLMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 158 AHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQ 237
Cdd:cd07141 163 AWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 238 KAG---LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDP 314
Cdd:cd07141 243 AAGksnLKRVTLELGGKSPNIVFADADL-DYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 315 LLEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDARIF--EPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFD 392
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYfiQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 393 EAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFRVdHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSP-QAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
gi 446639112 473 K 473
Cdd:cd07141 481 K 481
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
23-470 |
1.29e-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: 362.62 E-value: 1.29e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRT 102
Cdd:cd07106 4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 103 VQTYKFAAEEAkriygetLPLDAAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLS 182
Cdd:cd07106 84 VAWLRYTASLD-------LPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 183 SYALVELFEEAgLPNGALNIISGPGStVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDV 260
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAktLKRVTLELGGNDAAIVLPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 261 ELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEA 340
Cdd:cd07106 235 DI-DAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 341 IKEGATVLCGGKKRDAR--IFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAM 418
Cdd:cd07106 314 KAKGAKVLAGGEPLDGPgyFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 446639112 419 RAIDELEVGGVMINDIPTFRVdHMPYGGVKESGTGREGIKYAIEEMTEMKLV 470
Cdd:cd07106 394 AVARRLEAGTVWINTHGALDP-DAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
23-455 |
1.58e-121 |
|
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: 362.44 E-value: 1.58e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRT 102
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 103 VQTYKFAAEEAKRI---YGETLPLDAapgaDGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQT 179
Cdd:cd07110 84 AGCFEYYADLAEQLdakAERAVPLPS----EDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 180 PLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKA--GLKRVTLELGSNAAVIID 257
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAaqDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 258 EDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWV 337
Cdd:cd07110 240 DDADL-EKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 338 QEAIKEGATVLCGGKKRDAR----IFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNN 413
Cdd:cd07110 319 ARGKEEGARLLCGGRRPAHLekgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446639112 414 LFKAMRAIDELEVGGVMIN-DIPTFrvDHMPYGGVKESGTGRE 455
Cdd:cd07110 399 AERCDRVAEALEAGIVWINcSQPCF--PQAPWGGYKRSGIGRE 439
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
40-472 |
2.36e-121 |
|
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: 361.01 E-value: 2.36e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 40 VKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRiYGE 119
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEA-FLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 120 TLPLDAapgaDGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGA 199
Cdd:cd07100 80 DEPIET----DAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 200 LNIISGPGSTVgEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVII--DEDVELTdeiierVKWGA- 274
Cdd:cd07100 156 FQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGknLKKSVLELGGSDPFIVldDADLDKA------VKTAVk 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 275 --FVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGK 352
Cdd:cd07100 229 grLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 353 KRDAR--IFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVM 430
Cdd:cd07100 309 RPDGPgaFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVF 388
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446639112 431 INDIptFRVD-HMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07100 389 INGM--VKSDpRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
5-470 |
4.50e-120 |
|
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: 359.50 E-value: 4.50e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDW---KSVNTYkPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMT-----KMntlSAYDRATILEKVAQKMDER 76
Cdd:cd07142 6 LFINGQFvdaASGKTF-PTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegpwpRM---TGYERSRILLRFADLLEKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 77 REEFAEIIAKEAAKPIRAAR-GEVDRTVQTYKFAAEEAKRIYGETLPLDAApgadgRIAYTIRKPIGVIGAITPFNFPLN 155
Cdd:cd07142 82 ADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGP-----HHVYTLHEPIGVVGQIIPWNFPLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 156 LVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGI 235
Cdd:cd07142 157 MFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKII 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 236 KQKAG---LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVG 312
Cdd:cd07142 237 MQLAAksnLKPVTLELGGKSPFIVCEDADV-DKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 313 DPLLEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDARIF--EPTVLKNVPNHVSVQCQEVFGPLMTVNTFKE 390
Cdd:cd07142 316 DPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYyiQPTIFSDVKDDMKIARDEIFGPVQSILKFKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 391 FDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFRVDhMPYGGVKESGTGREGIKYAIEEMTEMKLV 470
Cdd:cd07142 396 VDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDAS-IPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
20-472 |
5.63e-120 |
|
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: 358.47 E-value: 5.63e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 20 LYAPYSEETLAEIAQGTEEDVKEAVTAAKNAM-TKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGE 98
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFeSGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 99 VDRTVQTYKFAAEEAKRIYGETLPLdaapgADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQ 178
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPL-----GPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 179 TPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVII 256
Cdd:cd07109 156 APLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAenVVPVTLELGGKSPQIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 257 DEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGdPLLEETDVSALISKRDVERIDMW 336
Cdd:cd07109 236 FADADL-EAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 337 VQEAIKEGATVLCGG-----KKRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFT 411
Cdd:cd07109 314 VARARARGARIVAGGriaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWT 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446639112 412 NNLFKAMRAIDELEVGGVMINDIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07109 394 RDGDRALRVARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
21-472 |
2.36e-119 |
|
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: 357.00 E-value: 2.36e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 21 YAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVD 100
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 101 RTVQTYKFAAEEAKRIYGETLPLDAapgadGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTP 180
Cdd:cd07090 82 SSADCLEYYAGLAPTLSGEHVPLPG-----GSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 181 LSSYALVELFEEAGLPNGALNIISGPGSTvGEAIVKNDYVASITFTGSPKVGIGIKQKA--GLKRVTLELGSNAAVIIDE 258
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAakGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 259 DVEltdeiIERVKWGA----FVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERID 334
Cdd:cd07090 236 DAD-----LENAVNGAmmanFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 335 MWVQEAIKEGATVLCGG-------KKRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQA 407
Cdd:cd07090 311 GYIESAKQEGAKVLCGGervvpedGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446639112 408 GVFTNNLFKAMRAIDELEVGGVMINDIPTFRVDhMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07090 391 GVFTRDLQRAHRVIAQLQAGTCWINTYNISPVE-VPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
6-455 |
2.49e-118 |
|
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: 355.33 E-value: 2.49e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 6 YINGDW-----KSVNTYKPLYApyseETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEF 80
Cdd:cd07086 2 VIGGEWvgsggETFTSRNPANG----EPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 81 AEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPLDAApgadGRIAYTIRKPIGVIGAITPFNFPLNLVAHK 160
Cdd:cd07086 78 GRLVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERP----GHRLMEQWNPLGVVGVITAFNFPVAVPGWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 161 VGPAIAAGNTVVLKPADQTPLSSYALVELFEEA----GLPNGALNIISGPGsTVGEAIVKNDYVASITFTGSPKVGIGIK 236
Cdd:cd07086 154 AAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRVG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 237 QKAG--LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDP 314
Cdd:cd07086 233 ETVArrFGRVLLELGGNNAIIVMDDADL-DLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 315 LLEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDARI----FEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKE 390
Cdd:cd07086 312 LDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEpgnyVEPTIVTGVTDDARIVQEETFAPILYVIKFDS 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446639112 391 FDEAIEQVNNSRYGLQAGVFTNNLFKAMRAID--ELEVGGVMINdIPTFRVD-HMPYGGVKESGTGRE 455
Cdd:cd07086 392 LEEAIAINNDVPQGLSSSIFTEDLREAFRWLGpkGSDCGIVNVN-IPTSGAEiGGAFGGEKETGGGRE 458
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
23-470 |
8.23e-118 |
|
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: 352.78 E-value: 8.23e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAAR-GEVDR 101
Cdd:cd07092 4 PATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 102 TVQTYKFAAEEAK----RIYGETLPldaapgadGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPAD 177
Cdd:cd07092 84 AVDNFRFFAGAARtlegPAAGEYLP--------GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 178 QTPLSSYALVELFEEaGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKA--GLKRVTLELGSNAAVI 255
Cdd:cd07092 156 TTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAadTLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 256 IDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDM 335
Cdd:cd07092 235 VFDDADL-DAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 336 WVQEAiKEGATVLCGGKKRDAR--IFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNN 413
Cdd:cd07092 314 FVERA-PAHARVLTGGRRAEGPgyFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446639112 414 LFKAMRAIDELEVGGVMINDIPTFrVDHMPYGGVKESGTGREGIKYAIEEMTEMKLV 470
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPL-AAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
5-472 |
2.18e-117 |
|
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: 352.87 E-value: 2.18e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDW-KSVNTYK-PLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAM-TKMNTLSAYDRATILEKVAQKMDERREEFA 81
Cdd:cd07144 10 LFINNEFvKSSDGETiKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFeSWWSKVTGEERGELLDKLADLVEKNRDLLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 82 EIIAKEAAKPIRA-ARGEVDRTVQTYKFAAEEAKRIYGETLPLDAApgadgRIAYTIRKPIGVIGAITPFNFPLNLVAHK 160
Cdd:cd07144 90 AIEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKTIPTSPN-----KLAYTLHEPYGVCGQIIPWNYPLAMAAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 161 VGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG 240
Cdd:cd07144 165 LAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 241 --LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAM-ESVVVGDPLLE 317
Cdd:cd07144 245 qnLKAVTLECGGKSPALVFEDADL-DQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 318 ETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDARI-----FEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFD 392
Cdd:cd07144 324 DTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLgkgyfIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 393 EAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIN-----DIptfrvdHMPYGGVKESGTGREGIKYAIEEMTEM 467
Cdd:cd07144 404 EAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINssndsDV------GVPFGGFKMSGIGRELGEYGLETYTQT 477
|
....*
gi 446639112 468 KLVCI 472
Cdd:cd07144 478 KAVHI 482
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
5-473 |
3.77e-117 |
|
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: 352.22 E-value: 3.77e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDW-KSV-NTYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAM--TKMNTLSAYDRATILEKVAQKMDERREEF 80
Cdd:cd07143 9 LFINGEFvDSVhGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFetDWGLKVSGSKRGRCLSKLADLMERNLDYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 81 AEIIAKEAAKPIR-AARGEVDRTVQTYKFAAEEAKRIYGETLPLDAApgadgRIAYTIRKPIGVIGAITPFNFPLNLVAH 159
Cdd:cd07143 89 ASIEALDNGKTFGtAKRVDVQASADTFRYYGGWADKIHGQVIETDIK-----KLTYTRHEPIGVCGQIIPWNFPLLMCAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 160 KVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQ-- 237
Cdd:cd07143 164 KIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEaa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 238 -KAGLKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLL 316
Cdd:cd07143 244 aKSNLKKVTLELGGKSPNIVFDDADL-ESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 317 EETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKK--RDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEA 394
Cdd:cd07143 323 EDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRhgNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 395 IEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTfrVDH-MPYGGVKESGTGREGIKYAIEEMTEMKLVCIK 473
Cdd:cd07143 403 IKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNL--LHHqVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
5-470 |
9.35e-117 |
|
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: 350.72 E-value: 9.35e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDWKSVNTYKPL--YAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTK--MNTLSAYDRATILEKVAQKMDERREEF 80
Cdd:cd07139 1 LFIGGRWVAPSGSETIdvVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 81 AEIIAKEAAKPIRAAR-GEVDRTVQTYKFAAEEAkriygETLPL-DAAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVA 158
Cdd:cd07139 81 ARLWTAENGMPISWSRrAQGPGPAALLRYYAALA-----RDFPFeERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 159 HKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGpGSTVGEAIVKNDYVASITFTGSPKVGIGIKQK 238
Cdd:cd07139 156 LKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 239 AG--LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLL 316
Cdd:cd07139 235 CGerLARVTLELGGKSAAIVLDDADL-DAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 317 EETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDAR----IFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFD 392
Cdd:cd07139 314 PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLdrgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446639112 393 EAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINdipTFRVD-HMPYGGVKESGTGREGIKYAIEEMTEMKLV 470
Cdd:cd07139 394 DAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN---GFRLDfGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
5-468 |
1.66e-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: 350.49 E-value: 1.66e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDWK--SVNTYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAE 82
Cdd:cd07559 3 NFINGEWVapSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 83 IIAKEAAKPIRAARG-EVDRTVQTYK-FA----AEE--AKRIYGETlpldaapgadgrIAYTIRKPIGVIGAITPFNFPL 154
Cdd:cd07559 83 AETLDNGKPIRETLAaDIPLAIDHFRyFAgvirAQEgsLSEIDEDT------------LSYHFHEPLGVVGQIIPWNFPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 155 NLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAgLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIG 234
Cdd:cd07559 151 LMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 235 IKQKAG--LKRVTLELGSNAAVIIDEDVELTDEIIERVKWGAFV----NNGQVCISVQRVFVHETKMHEFLSKLKKAMES 308
Cdd:cd07559 230 IMQYAAenLIPVTLELGGKSPNIFFDDAMDADDDFDDKAEEGQLgfafNQGEVCTCPSRALVQESIYDEFIERAVERFEA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 309 VVVGDPLLEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKR------DARIFEPTVLKNVPNHVSVQCQEVFGPL 382
Cdd:cd07559 310 IKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggldKGYFYEPTLIKGGNNDMRIFQEEIFGPV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 383 MTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIN---DIPTfrvdHMPYGGVKESGTGREGIKY 459
Cdd:cd07559 390 LAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcyhQYPA----HAPFGGYKKSGIGRETHKM 465
|
....*....
gi 446639112 460 AIEEMTEMK 468
Cdd:cd07559 466 MLDHYQQTK 474
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
23-472 |
5.10e-116 |
|
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: 348.58 E-value: 5.10e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIR-AARGEVDR 101
Cdd:cd07108 4 PATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPEAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 102 TVQTYKFAAEEAKRIYGETLPLdaapgADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPL 181
Cdd:cd07108 84 LADLFRYFGGLAGELKGETLPF-----GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 182 SSYALVELFEEAgLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDED 259
Cdd:cd07108 159 AVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAdrLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 260 VELtDEIIERVKWGA-FVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQ 338
Cdd:cd07108 238 ADL-DDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 339 EAIKE-GATVLCGGK-KRDARI-----FEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFT 411
Cdd:cd07108 317 LGLSTsGATVLRGGPlPGEGPLadgffVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446639112 412 NNLFKAMRAIDELEVGGVMINDIPTFRVDhMPYGGVKESGTGREgikYAIEEM----TEMKLVCI 472
Cdd:cd07108 397 RDLGRALRAAHALEAGWVQVNQGGGQQPG-QSYGGFKQSGLGRE---ASLEGMlehfTQKKTVNI 457
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
1-473 |
1.44e-115 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 348.05 E-value: 1.44e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 1 MKKHLYINGDWKSVNTYK-PLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREE 79
Cdd:PRK13473 1 MQTKLLINGELVAGEGEKqPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 80 FAEIIAKEAAKPIRAARG-EVDRTVQTYKFAAEEAKRIYGetlpLDAAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVA 158
Cdd:PRK13473 81 FARLESLNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEG----KAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 159 HKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAgLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQK 238
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 239 AG--LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLL 316
Cdd:PRK13473 236 AAdsVKRTHLELGGKAPVIVFDDADL-DAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 317 EETDVSALISKRDVERIDMWVQEAIKEG-ATVLCGGKKRDAR--IFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDE 393
Cdd:PRK13473 315 EDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKgyYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 394 AIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIND-IPTfrVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:PRK13473 395 AVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNThFML--VSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMV 472
|
.
gi 446639112 473 K 473
Cdd:PRK13473 473 K 473
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
27-466 |
4.39e-114 |
|
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: 343.12 E-value: 4.39e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 27 ETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRTVQTY 106
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 107 KFAAEEAKRIYGETLPldaapGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSS-YA 185
Cdd:cd07152 82 HEAAGLPTQPQGEILP-----SAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 186 LVELFEEAGLPNGALNIISGpGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDVELt 263
Cdd:cd07152 157 IARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGrhLKKVSLELGGKNALIVLDDADL- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 264 DEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEAIKE 343
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 344 GATVLCGGKkRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDE 423
Cdd:cd07152 315 GARLEAGGT-YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADR 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 446639112 424 LEVGGVMINDIPTFRVDHMPYGGVKESGTG-REGIKYAIEEMTE 466
Cdd:cd07152 394 LRTGMLHINDQTVNDEPHNPFGGMGASGNGsRFGGPANWEEFTQ 437
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
23-470 |
1.51e-112 |
|
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: 339.60 E-value: 1.51e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAM-TKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARG-EVD 100
Cdd:cd07089 4 PATEEVIGTAPDAGAADVDAAIAAARRAFdTGDWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAmQVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 101 RTVQTYKFAAEEAKRIYGETlPLDAAPGADGRIAYTIRK-PIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQT 179
Cdd:cd07089 84 GPIGHLRYFADLADSFPWEF-DLPVPALRGGPGRRVVRRePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 180 PLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIID 257
Cdd:cd07089 163 PLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAatLKRVLLELGGKSANIVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 258 EDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWV 337
Cdd:cd07089 243 DDADL-AAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 338 QEAIKEGATVLCGGkKRDARI-----FEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTN 412
Cdd:cd07089 322 ARGRDEGARLVTGG-GRPAGLdkgfyVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446639112 413 NLFKAMRAIDELEVGGVMINDIPTFRVDhMPYGGVKESGTGREGIKYAIEEMTEMKLV 470
Cdd:cd07089 401 DVDRAYRVARRIRTGSVGINGGGGYGPD-APFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
5-472 |
5.04e-109 |
|
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: 331.34 E-value: 5.04e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDWK--SVNTYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAE 82
Cdd:cd07117 3 LFINGEWVkgSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 83 IIAKEAAKPIRAARG-EVDRTVQTYKFAAEEAKRIYGETLPLDaapgaDGRIAYTIRKPIGVIGAITPFNFPLNLVAHKV 161
Cdd:cd07117 83 VETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMID-----EDTLSIVLREPIGVVGQIIPWNFPFLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 162 GPAIAAGNTVVLKPADQTPLSSYALVELFEEAgLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVG--IGIKQKA 239
Cdd:cd07117 158 APALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGrdVAIAAAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 240 GLKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEET 319
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANW-DKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 320 DVSALISKRDVERIDMWVQEAIKEGATVLCGGKK-----RDARIF-EPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDE 393
Cdd:cd07117 316 QMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRltengLDKGFFiEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 394 AIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIN---DIPTfrvdHMPYGGVKESGTGREGIKYAIEEMTEMKLV 470
Cdd:cd07117 396 VIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNtynQIPA----GAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
..
gi 446639112 471 CI 472
Cdd:cd07117 472 YI 473
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
5-455 |
1.24e-108 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 331.31 E-value: 1.24e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDWK--SVNTYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMN------TLSAYdRATILEKVAQKMDER 76
Cdd:PLN02467 10 LFIGGEWRepVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRNKgkdwarTTGAV-RAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 77 REEFAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGE-----TLPLDAAPGadgriaYTIRKPIGVIGAITPFN 151
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKqkapvSLPMETFKG------YVLKEPLGVVGLITPWN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 152 FPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKV 231
Cdd:PLN02467 163 YPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 232 GIGIKQKAG--LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESV 309
Cdd:PLN02467 243 GRKIMTAAAqmVKPVSLELGGKSPIIVFDDVDL-DKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 310 VVGDPLLEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRD--ARIF--EPTVLKNVPNHVSVQCQEVFGPLMTV 385
Cdd:PLN02467 322 KISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFfiEPTIITDVTTSMQIWREEVFGPVLCV 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446639112 386 NTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIN-DIPTFrvDHMPYGGVKESGTGRE 455
Cdd:PLN02467 402 KTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINcSQPCF--CQAPWGGIKRSGFGRE 470
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
2-472 |
1.42e-108 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 330.33 E-value: 1.42e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 2 KKHLYINGDWKSVNTYK--PLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREE 79
Cdd:PRK11241 10 RQQALINGEWLDANNGEviDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 80 FAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPldaAPGADGRIaYTIRKPIGVIGAITPFNFPLNLVAH 159
Cdd:PRK11241 90 LARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIP---GHQADKRL-IVIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 160 KVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKA 239
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 240 G--LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLE 317
Cdd:PRK11241 246 AkdIKKVSLELGGNAPFIVFDDADL-DKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 318 ETDVSALISKRDVERIDMWVQEAIKEGATVLCGGK--KRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAI 395
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKahELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446639112 396 EQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINdIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:PRK11241 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGIN-TGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
5-453 |
2.84e-108 |
|
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: 330.34 E-value: 2.84e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDW-------KSVNTYKPlyapysEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERR 77
Cdd:cd07124 35 LVIGGKEvrteekiESRNPADP------SEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 78 EEFAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGEtlPLDAAPGADGRIAYtirKPIGVIGAITPFNFPLNLV 157
Cdd:cd07124 109 FELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGF--PVEMVPGEDNRYVY---RPLGVGAVISPWNFPLAIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 158 AHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQ 237
Cdd:cd07124 184 AGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 238 KAG--------LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESV 309
Cdd:cd07124 264 RAAkvqpgqkwLKRVIAEMGGKNAIIVDEDADL-DEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKAL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 310 VVGDPLLEETDVSALISKRDVERIDMWVQEAIKEGaTVLCGGKKRDARI----FEPTVLKNVPNHVSVQCQEVFGPLMTV 385
Cdd:cd07124 343 KVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAAegyfVQPTIFADVPPDHRLAQEEIFGPVLAV 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446639112 386 NTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIN-DIPTFRVDHMPYGGVKESGTG 453
Cdd:cd07124 422 IKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrKITGALVGRQPFGGFKMSGTG 490
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
5-470 |
9.84e-108 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 329.85 E-value: 9.84e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYING---DWKSVNTYkPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMT-----KMntlSAYDRATILEKVAQKMDER 76
Cdd:PLN02466 60 LLINGqfvDAASGKTF-PTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegpwpKM---TAYERSRILLRFADLLEKH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 77 REEFAEIIAKEAAKPI-RAARGEVDRTVQTYKFAAEEAKRIYGETLPldaapgADG-RIAYTIRKPIGVIGAITPFNFPL 154
Cdd:PLN02466 136 NDELAALETWDNGKPYeQSAKAELPMFARLFRYYAGWADKIHGLTVP------ADGpHHVQTLHEPIGVAGQIIPWNFPL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 155 NLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVG-- 232
Cdd:PLN02466 210 LMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGki 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 233 -IGIKQKAGLKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVV 311
Cdd:PLN02466 290 vLELAAKSNLKPVTLELGGKSPFIVCEDADV-DKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 312 GDPLLEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDARIF--EPTVLKNVPNHVSVQCQEVFGPLMTVNTFK 389
Cdd:PLN02466 369 GDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYyiQPTVFSNVQDDMLIAQDEIFGPVQSILKFK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 390 EFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFRVDhMPYGGVKESGTGREGIKYAIEEMTEMKL 469
Cdd:PLN02466 449 DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAA-IPFGGYKMSGIGREKGIYSLNNYLQVKA 527
|
.
gi 446639112 470 V 470
Cdd:PLN02466 528 V 528
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
39-472 |
2.15e-106 |
|
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: 322.99 E-value: 2.15e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 39 DVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYG 118
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 119 ETLPLDAapgaDGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNG 198
Cdd:cd07105 81 GSIPSDK----PGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 199 ALNIIS-----GPgsTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDVELtDEIIERVK 271
Cdd:cd07105 157 VLNVVThspedAP--EVVEALIAHPAVRKVNFTGSTRVGRIIAETAAkhLKPVLLELGGKAPAIVLEDADL-DAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 272 WGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDplleeTDVSALISKRDVERIDMWVQEAIKEGATVLCGG 351
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 352 KKR---DARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGG 428
Cdd:cd07105 309 LADespSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446639112 429 VMINDiPTFRVD-HMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07105 389 VHING-MTVHDEpTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
5-473 |
2.67e-106 |
|
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: 324.39 E-value: 2.67e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDWKSVN--TYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAM-TKMNTLSAYDRATILEKVAQKMDERREEFA 81
Cdd:cd07113 2 HFIDGRPVAGQseKRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 82 EIIAKEAAKPIRAARG-EVDRTVQTYKFAAEEAKRIYGETL-PLDAAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAH 159
Cdd:cd07113 82 QLETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETLaPSIPSMQGERYTAFTRREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 160 KVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGStVGEAIVKNDYVASITFTGSPKVGIGIKQKA 239
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 240 --GLKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLE 317
Cdd:cd07113 241 asDLTRVTLELGGKNAAAFLKDADI-DWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 318 ETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKK--RDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAI 395
Cdd:cd07113 320 SVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEAlaGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446639112 396 EQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINdIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCIK 473
Cdd:cd07113 400 QLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN-MHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
21-470 |
4.06e-106 |
|
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: 323.02 E-value: 4.06e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 21 YAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVD 100
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 101 RTVQTYKFAAEEAKRIYG-ETLPLDAA-PGADGRIAYtirKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQ 178
Cdd:cd07099 81 LALEAIDWAARNAPRVLApRKVPTGLLmPNKKATVEY---RPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 179 TPLSSYALVELFEEAGLPNGALNIISGPGSTvGEAIVKN--DYVAsitFTGSPKVGIGIKQKAG--LKRVTLELGSNAAV 254
Cdd:cd07099 158 TPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAgvDKVA---FTGSVATGRKVMAAAAerLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 255 IIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERID 334
Cdd:cd07099 234 IVLADADL-ERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 335 MWVQEAIKEGATVLCGGKKR--DARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTN 412
Cdd:cd07099 313 RHVDDAVAKGAKALTGGARSngGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 446639112 413 NLFKAMRAIDELEVGGVMIND-IPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLV 470
Cdd:cd07099 393 DLARAEAIARRLEAGAVSINDvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
22-472 |
7.09e-106 |
|
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: 322.40 E-value: 7.09e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 22 APYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDR 101
Cdd:cd07107 3 NPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 102 TVQTYKFAAEEAKRIYGETLPLDAapgadGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPL 181
Cdd:cd07107 83 AAALLDYFAGLVTELKGETIPVGG-----RNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 182 SSYALVELFEEAgLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKA--GLKRVTLELGSNAAVIIDED 259
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAaeGIKHVTLELGGKNALIVFPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 260 VELTDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQE 339
Cdd:cd07107 237 ADPEAAADAAVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 340 AIKEGATVLCGGKKRDARIF------EPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNN 413
Cdd:cd07107 317 AKREGARLVTGGGRPEGPALeggfyvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446639112 414 LFKAMRAIDELEVGGVMINDIPTfrvdH---MPYGGVKESGTGREgikYAIEEM---TEMKLVCI 472
Cdd:cd07107 397 ISQAHRTARRVEAGYVWINGSSR----HflgAPFGGVKNSGIGRE---ECLEELlsyTQEKNVNV 454
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
5-463 |
1.01e-104 |
|
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: 320.50 E-value: 1.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDWKSV--NTYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAE 82
Cdd:cd07111 24 HFINGKWVKPenRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 83 IIAKEAAKPIRAAR-GEVDRTVQTYKFAAEEAKRIygETlpldAAPGadgriaytiRKPIGVIGAITPFNFPLNLVAHKV 161
Cdd:cd07111 104 LESLDNGKPIRESRdCDIPLVARHFYHHAGWAQLL--DT----ELAG---------WKPVGVVGQIVPWNFPLLMLAWKI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 162 GPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTvGEAIVKNDYVASITFTGSPKVGIGI-KQKAG 240
Cdd:cd07111 169 CPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALrRATAG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 241 L-KRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEET 319
Cdd:cd07111 248 TgKKLSLELGGKSPFIVFDDADL-DSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 320 DVSALISKRDVERIDMWVQEAIKEGATVL--CGGKKRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQ 397
Cdd:cd07111 327 DMGAIVDPAQLKRIRELVEEGRAEGADVFqpGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVAL 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446639112 398 VNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFRVDhMPYGGVKESGTGREGIKYAIEE 463
Cdd:cd07111 407 ANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAA-AGFGGYRESGFGREGGKEGLYE 471
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
21-471 |
2.28e-103 |
|
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: 316.21 E-value: 2.28e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 21 YAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTkmNTLSAYD---RATILEKVAQKMDERREEFAEIIAKEAAKPIRAARG 97
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFD--ETDWAHDprlRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 98 EVDRTVQTYKFAAEEAKRIYGETLplDAAPGADGRIaytIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPAD 177
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMI--EPEPGSFSLV---LREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 178 QTPLSSYALVELFEEA-GLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAV 254
Cdd:cd07120 155 QTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAptLKRLGLELGGKTPC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 255 IIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERID 334
Cdd:cd07120 235 IVFDDADL-DAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 335 MWVQEAIKEGATVLCGGKKRDARI-----FEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGV 409
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEGLakgafLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446639112 410 FTNNLFKAMRAIDELEVGGVMINDIPTFRvDHMPYGGVKESGTGR-EGIKyAIEEMTEMKLVC 471
Cdd:cd07120 394 WTRDLARAMRVARAIRAGTVWINDWNKLF-AEAEEGGYRQSGLGRlHGVA-ALEDFIEYKHIY 454
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
19-459 |
7.17e-103 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 316.82 E-value: 7.17e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 19 PLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGE 98
Cdd:PRK09407 35 EVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 99 VDRTVQTYKFAAEEAKRIYGETLPLDAAPGAdGRiAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQ 178
Cdd:PRK09407 115 VLDVALTARYYARRAPKLLAPRRRAGALPVL-TK-TTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 179 TPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKN-DYVAsitFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVI 255
Cdd:PRK09407 193 TPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNaDYLM---FTGSTATGRVLAEQAGrrLIGFSLELGGKNPMI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 256 IDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDM 335
Cdd:PRK09407 270 VLDDADL-DKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 336 WVQEAIKEGATVLCGGKKR-D--ARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTN 412
Cdd:PRK09407 349 HVDDAVAKGATVLAGGKARpDlgPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTG 428
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 446639112 413 NLFKAMRAIDELEVGGVMINDI--PTFRVDHMPYGGVKESGTGR----EGI-KY 459
Cdd:PRK09407 429 DTARGRAIAARIRAGTVNVNEGyaAAWGSVDAPMGGMKDSGLGRrhgaEGLlKY 482
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
5-470 |
8.08e-102 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 312.97 E-value: 8.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDWKSVNTYKPL--YAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAE 82
Cdd:PRK13252 9 LYIDGAYVEATSGETFevINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 83 IIAKEAAKPIRAARgEVDrtVQT----YKFAAEEAKRIYGETLPLdaapgADGRIAYTIRKPIGVIGAITPFNFPLNLVA 158
Cdd:PRK13252 89 LETLDTGKPIQETS-VVD--IVTgadvLEYYAGLAPALEGEQIPL-----RGGSFVYTRREPLGVCAGIGAWNYPIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 159 HKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGStVGEAIVKNDYVASITFTGSpkVGIGIKQK 238
Cdd:PRK13252 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGG--VPTGKKVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 239 A----GLKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDP 314
Cdd:PRK13252 238 AaaaaSLKEVTMELGGKSPLIVFDDADL-DRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 315 LLEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDARIF------EPTVLKNVPNHVSVQCQEVFGPLMTVNTF 388
Cdd:PRK13252 317 MDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFangafvAPTVFTDCTDDMTIVREEIFGPVMSVLTF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 389 KEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIN---DIPTfrvdHMPYGGVKESGTGREGIKYAIEEMT 465
Cdd:PRK13252 397 DDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINtwgESPA----EMPVGGYKQSGIGRENGIATLEHYT 472
|
....*
gi 446639112 466 EMKLV 470
Cdd:PRK13252 473 QIKSV 477
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
22-460 |
8.92e-100 |
|
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: 306.93 E-value: 8.92e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 22 APYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDR 101
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 102 TVQTYKFAAEEAKRIYGETLPLDAAPGADGRIAYtiRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPL 181
Cdd:cd07101 82 VAIVARYYARRAERLLKPRRRRGAIPVLTRTTVN--RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 182 SSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKN-DYVAsitFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDE 258
Cdd:cd07101 160 TALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNaDYVM---FTGSTATGRVVAERAGrrLIGCSLELGGKNPMIVLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 259 DVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQ 338
Cdd:cd07101 237 DADL-DKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 339 EAIKEGATVLCGGKKR---DARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLF 415
Cdd:cd07101 316 DAVAKGATVLAGGRARpdlGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 446639112 416 KAMRAIDELEVGGVMIND--IPTFRVDHMPYGGVKESGTGR----EGI-KYA 460
Cdd:cd07101 396 RGRRIAARLRAGTVNVNEgyAAAWASIDAPMGGMKDSGLGRrhgaEGLlKYT 447
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
5-470 |
1.34e-99 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 307.90 E-value: 1.34e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYING---DWKSVNTYKPLyAPYSEETLAEIAQGTEEDVKEAVTAAKNAMT--KMNTLSAYDRATILEKVAQKMDERREE 79
Cdd:PLN02766 23 LFINGefvDAASGKTFETR-DPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 80 FAEIIAKEAAKPIRAARG-EVDRTVQTYKFAAEEAKRIYGETLPLDAApgadgRIAYTIRKPIGVIGAITPFNFPLNLVA 158
Cdd:PLN02766 102 LAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQ-----LQGYTLKEPIGVVGHIIPWNFPSTMFF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 159 HKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQK 238
Cdd:PLN02766 177 MKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 239 AG---LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPL 315
Cdd:PLN02766 257 AAtsnLKQVSLELGGKSPLLIFDDADV-DMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 316 LEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKK--RDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDE 393
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPcgDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446639112 394 AIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFRVDhMPYGGVKESGTGREGIKYAIEEMTEMKLV 470
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPD-CPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
5-472 |
7.27e-99 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 305.67 E-value: 7.27e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDWKSV--NTYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTK--MNTLSAYDRATILEKVAQKMDERREEF 80
Cdd:PRK09847 22 LFINGEYTAAaeNETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 81 AEIIAKEAAKPIR-AARGEVDRTVQTYKFAAEEAKRIYGETlpldaAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAH 159
Cdd:PRK09847 102 ALLETLDTGKPIRhSLRDDIPGAARAIRWYAEAIDKVYGEV-----ATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 160 KVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKA 239
Cdd:PRK09847 177 KLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 240 G---LKRVTLELGSNAAVIIDEDVELTDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLL 316
Cdd:PRK09847 257 GdsnMKRVWLEAGGKSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 317 EETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIE 396
Cdd:PRK09847 337 PATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446639112 397 QVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDiptFRVDHM--PYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNN---YNDGDMtvPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
4-470 |
5.33e-97 |
|
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: 300.20 E-value: 5.33e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 4 HLYINGDWKSVNT--YKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFA 81
Cdd:cd07085 2 KLFINGEWVESKTteWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 82 EIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPlDAAPGADgriAYTIRKPIGVIGAITPFNFPLNLVAHKV 161
Cdd:cd07085 82 RLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLE-NVARGID---TYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 162 GPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVgEAIVKNDYVASITFTGSPKVGIGIKQKAG- 240
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYERAAa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 241 -LKRVTLELGS-NAAVII-DEDVELTdeiIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLE 317
Cdd:cd07085 237 nGKRVQALGGAkNHAVVMpDADLEQT---ANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 318 ETDVSALISKRDVERIDMWVQEAIKEGATVLCGGkkRDARI--------FEPTVLKNVPNHVSVQCQEVFGPLMTVNTFK 389
Cdd:cd07085 314 GADMGPVISPAAKERIEGLIESGVEEGAKLVLDG--RGVKVpgyengnfVGPTILDNVTPDMKIYKEEIFGPVLSIVRVD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 390 EFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIN-DIPTfRVDHMPYGGVKES------GTGREGIKYaie 462
Cdd:cd07085 392 TLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINvPIPV-PLAFFSFGGWKGSffgdlhFYGKDGVRF--- 467
|
....*...
gi 446639112 463 eMTEMKLV 470
Cdd:cd07085 468 -YTQTKTV 474
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
66-470 |
5.68e-97 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 298.19 E-value: 5.68e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 66 LEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPLDAApgadGRIAYTIRKPIGVIG 145
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRP----GENILLFKRALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 146 AITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITF 225
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 226 TGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLK 303
Cdd:PRK10090 157 TGSVSAGEKIMAAAAknITKVCLELGGKAPAIVMDDADL-DLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 304 KAMESVVVGDPLLEET-DVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDAR--IFEPTVLKNVPNHVSVQCQEVFG 380
Cdd:PRK10090 236 EAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKgyYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 381 PLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDiPTFRVDHMPYGGVKESGTGREGIKYA 460
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR-ENFEAMQGFHAGWRKSGIGGADGKHG 394
|
410
....*....|
gi 446639112 461 IEEMTEMKLV 470
Cdd:PRK10090 395 LHEYLQTQVV 404
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
1-473 |
2.36e-95 |
|
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: 296.33 E-value: 2.36e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 1 MKKHLYING---DWKSVNTYKPLyAPYSEETLAEIAQGTEEDVKEAVTAAKNAM-----TKMNtlsAYDRATILEKVAQK 72
Cdd:cd07140 4 MPHQLFINGefvDAEGGKTYNTI-NPTDGSVICKVSLATVEDVDRAVAAAKEAFengewGKMN---ARDRGRLMYRLADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 73 MDERREEFAEIIAKEA-AKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPLDAAPgADGRIAYTIRKPIGVIGAITPFN 151
Cdd:cd07140 80 MEEHQEELATIESLDSgAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQAR-PNRNLTLTKREPIGVCGIVIPWN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 152 FPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKV 231
Cdd:cd07140 159 YPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 232 GIGIKQKAG---LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMES 308
Cdd:cd07140 239 GKHIMKSCAvsnLKKVSLELGGKSPLIIFADCDM-DKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 309 VVVGDPLLEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKK--RDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVN 386
Cdd:cd07140 318 MKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQvdRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIIS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 387 TFK--EFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFRVdHMPYGGVKESGTGREGIKYAIEEM 464
Cdd:cd07140 398 KFDdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDV-AAPFGGFKQSGFGKDLGEEALNEY 476
|
....*....
gi 446639112 465 TEMKLVCIK 473
Cdd:cd07140 477 LKTKTVTIE 485
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
6-472 |
6.56e-88 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 277.41 E-value: 6.56e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 6 YINGDWKSVNTYK--PLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEI 83
Cdd:PLN00412 19 YADGEWRTSSSGKsvAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 84 IAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGET--LPLDAAPGaDGRIAY--TIRKPIGVIGAITPFNFPLNLVAH 159
Cdd:PLN00412 99 LVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEGkfLVSDSFPG-NERNKYclTSKIPLGVVLAIPPFNYPVNLAVS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 160 KVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSpKVGIGIKQKA 239
Cdd:PLN00412 178 KIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISKKA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 240 GLKRVTLELGSNAAVIIDEDVELTDEIIERVKwGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLlEET 319
Cdd:PLN00412 257 GMVPLQMELGGKDACIVLEDADLDLAAANIIK-GGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPE-DDC 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 320 DVSALISKRDVERIDMWVQEAIKEGATvLCGGKKRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVN 399
Cdd:PLN00412 335 DITPVVSESSANFIEGLVMDAKEKGAT-FCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCN 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446639112 400 NSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:PLN00412 414 ASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGITNSINMMTKVKSTVI 486
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
5-452 |
1.55e-85 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 271.81 E-value: 1.55e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDW-------KSVNTYKPlyapysEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERR 77
Cdd:PRK03137 39 LIIGGERittedkiVSINPANK------SEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 78 EEFAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRiYGETLPLDAAPGADGRIAYTirkPIGVIGAITPFNFPLNLV 157
Cdd:PRK03137 113 HEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLK-LADGKPVESRPGEHNRYFYI---PLGVGVVISPWNFPFAIM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 158 AHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQ 237
Cdd:PRK03137 189 AGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 238 KAG--------LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESV 309
Cdd:PRK03137 269 RAAkvqpgqiwLKRVIAEMGGKDAIVVDEDADL-DLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKEL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 310 VVGDPlLEETDVSALISKRDVERIDMWVQEAIKEGaTVLCGGKKRDARIF--EPTVLKNVPNHVSVQCQEVFGPLMTVNT 387
Cdd:PRK03137 348 TVGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYfiQPTIFADVDPKARIMQEEIFGPVVAFIK 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446639112 388 FKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIN-DIPTFRVDHMPYGGVKESGT 452
Cdd:PRK03137 426 AKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrGCTGAIVGYHPFGGFNMSGT 491
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
23-472 |
2.80e-84 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 266.99 E-value: 2.80e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRT 102
Cdd:PRK09406 8 PATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 103 VQTYKFAAEEAKRIYGETlPLDAAPGADGRiAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLS 182
Cdd:PRK09406 88 AKGFRYYAEHAEALLADE-PADAAAVGASR-AYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 183 SYALVELFEEAGLPNGALNIISGPGSTVgEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVII---- 256
Cdd:PRK09406 166 ALYLADLFRRAGFPDGCFQTLLVGSGAV-EAILRDPRVAAATLTGSEPAGRAVAAIAGdeIKKTVLELGGSDPFIVmpsa 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 257 DEDVELTDEIIERVKwgafvNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMW 336
Cdd:PRK09406 245 DLDRAAETAVTARVQ-----NNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 337 VQEAIKEGATVLCGGKK--RDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNL 414
Cdd:PRK09406 320 VDDAVAAGATILCGGKRpdGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446639112 415 FKAMRAIDELEVGGVMINDIpTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:PRK09406 400 AEQERFIDDLEAGQVFINGM-TVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
21-453 |
6.58e-83 |
|
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: 262.95 E-value: 6.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 21 YAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVD 100
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 101 RTVQTYKFAAEEAKRiYGETLPLDAAPGADGRIAytiRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTP 180
Cdd:cd07102 81 GMLERARYMISIAEE-ALADIRVPEKDGFERYIR---REPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 181 LSSYALVELFEEAGLPNGALNIISGpGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDE 258
Cdd:cd07102 157 LCGERFAAAFAEAGLPEGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAgrFIKVGLELGGKDPAYVRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 259 DVELTDEIIERVKwGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQ 338
Cdd:cd07102 236 DADLDAAAESLVD-GAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 339 EAIKEGATVLCGGK-----KRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNN 413
Cdd:cd07102 315 DAIAKGARALIDGAlfpedKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKD 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 446639112 414 LFKAMRAIDELEVGGVMINdiptfRVDH----MPYGGVKESGTG 453
Cdd:cd07102 395 IARAEALGEQLETGTVFMN-----RCDYldpaLAWTGVKDSGRG 433
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
6-468 |
1.45e-81 |
|
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: 260.46 E-value: 1.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 6 YINGDWksVNTYKPLY----APYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFA 81
Cdd:cd07116 4 FIGGEW--VAPVKGEYfdniTPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 82 EIIAKEAAKPIRAARG-EVDRTVQTYKFAAEEAKRIYGETLPLDaapgaDGRIAYTIRKPIGVIGAITPFNFPLNLVAHK 160
Cdd:cd07116 82 VAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSISEID-----ENTVAYHFHEPLGVVGQIIPWNFPLLMATWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 161 VGPAIAAGNTVVLKPADQTPLSSYALVELFEEAgLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKA- 239
Cdd:cd07116 157 LAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAs 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 240 -GLKRVTLELGSNA-----AVIIDEDVELTDEIIERVKWGAFvNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGD 313
Cdd:cd07116 236 eNIIPVTLELGGKSpniffADVMDADDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 314 PLLEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKR-------DARIFEPTVLKNvpNHVSVQCQEVFGPLMTVN 386
Cdd:cd07116 315 PLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNelggllgGGYYVPTTFKGG--NKMRIFQEEIFGPVLAVT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 387 TFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFRVdHMPYGGVKESGTGREGIKYAIEEMTE 466
Cdd:cd07116 393 TFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPA-HAAFGGYKQSGIGRENHKMMLDHYQQ 471
|
..
gi 446639112 467 MK 468
Cdd:cd07116 472 TK 473
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
39-461 |
1.65e-80 |
|
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: 256.43 E-value: 1.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 39 DVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRTVQTYKFAAeeakRIYG 118
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISI----KAYH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 119 ETLPLDAAPGADGRiAYTIRKPIGVIGAITPFNFPLNLV-AHKVgPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPN 197
Cdd:cd07095 77 ERTGERATPMAQGR-AVLRHRPHGVMAVFGPFNFPGHLPnGHIV-PALLAGNTVVFKPSELTPAVAELMVELWEEAGLPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 198 GALNIISGpGSTVGEAIVKNDYVASITFTGSPKVGIGIKQK-AGL--KRVTLELGSNAAVIIDEDVELTDEIIERVKwGA 274
Cdd:cd07095 155 GVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRpgKILALEMGGNNPLVVWDVADIDAAAYLIVQ-SA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 275 FVNNGQVCISVQRVFVHETKMH-EFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKK 353
Cdd:cd07095 233 FLTAGQRCTCARRLIVPDGAVGdAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 354 RDAR-------IFEPTVLKNVPNhvsvqcQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEV 426
Cdd:cd07095 313 LVAGtaflspgIIDVTDAADVPD------EEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRA 386
|
410 420 430
....*....|....*....|....*....|....*
gi 446639112 427 GGVMINDIPTFRVDHMPYGGVKESGTGREGIKYAI 461
Cdd:cd07095 387 GIVNWNRPTTGASSTAPFGGVGLSGNHRPSAYYAA 421
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
21-454 |
2.61e-75 |
|
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: 243.75 E-value: 2.61e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 21 YAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKP-IRAARGEV 99
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 100 DRTVQTYKFAAEeakriYGE-TLPLDAAPGA------DGRIAYtirKPIGVIGAITPFNFPL-NLVahkvGPAIAA---G 168
Cdd:cd07098 81 LVTCEKIRWTLK-----HGEkALRPESRPGGllmfykRARVEY---EPLGVVGAIVSWNYPFhNLL----GPIIAAlfaG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 169 NTVVLKPADQTPLSSYALVELFEEA----GLPNGALNIISGPGSTvGEAIVKNDYVASITFTGSPKVGIGIKQKAG--LK 242
Cdd:cd07098 149 NAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAesLT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 243 RVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVS 322
Cdd:cd07098 228 PVVLELGGKDPAIVLDDADL-DQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 323 ALISKRDVERIDMWVQEAIKEGATVLCGGK------KRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIE 396
Cdd:cd07098 307 AMISPARFDRLEELVADAVEKGARLLAGGKryphpeYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVE 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 446639112 397 QVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDI-PTFRVDHMPYGGVKESGTGR 454
Cdd:cd07098 387 IANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFgVNYYVQQLPFGGVKGSGFGR 445
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
6-455 |
1.18e-74 |
|
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: 242.50 E-value: 1.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 6 YINGDWKSVNTYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIA 85
Cdd:cd07130 2 VYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 86 KEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPLDAApgadGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAI 165
Cdd:cd07130 82 LEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERP----GHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 166 AAGNTVVLKPADQTPLSSYA----LVELFEEAGLPNGALNIISGpGSTVGEAIVKNDYVASITFTGSPKVG--IGIKQKA 239
Cdd:cd07130 158 VCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGrqVGQAVAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 240 GLKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEET 319
Cdd:cd07130 237 RFGRSLLELGGNNAIIVMEDADL-DLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 320 DVSALISKRDVERIDMWVQEAIKEGATVLCGGKK--RDARIFEPTVLKnVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQ 397
Cdd:cd07130 316 LVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVidGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446639112 398 VNNSRYGLQAGVFTNNLFKAMRAIDEL--EVGGVMINdIPT--------FrvdhmpyGGVKESGTGRE 455
Cdd:cd07130 395 NNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVN-IGTsgaeiggaF-------GGEKETGGGRE 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
5-470 |
2.22e-73 |
|
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: 239.79 E-value: 2.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDWKSVNTYKPLYAPYSE-ETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEI 83
Cdd:cd07083 21 LVIGGEWVDTKERMVSVSPFAPsEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 84 IAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPLDAAPGADGRIAYtirKPIGVIGAITPFNFPLNLVAHKVGP 163
Cdd:cd07083 101 LTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFY---VGLGAGVVISPWNFPVAIFTGMIVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 164 AIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--- 240
Cdd:cd07083 178 PVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAArla 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 241 -----LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPL 315
Cdd:cd07083 258 pgqtwFKRLYVETGGKNAIIVDETADF-ELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 316 LEETDVSALISKRDVERIDMWVqEAIKEGATVLCGGKKRDAR--IFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFK--EF 391
Cdd:cd07083 337 ENGTDLGPVIDAEQEAKVLSYI-EHGKNEGQLVLGGKRLEGEgyFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKddDF 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 392 DEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFR-VDHMPYGGVKESGTG-REGIKYAIEEMTEMKL 469
Cdd:cd07083 416 AEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGAlVGVQPFGGFKLSGTNaKTGGPHYLRRFLEMKA 495
|
.
gi 446639112 470 V 470
Cdd:cd07083 496 V 496
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
23-470 |
5.41e-72 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 235.14 E-value: 5.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRT 102
Cdd:PRK13968 14 PATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 103 VQTYKFAAEeakriYGETLpLDAAP----GADGRIAYtirKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQ 178
Cdd:PRK13968 94 ANLCDWYAE-----HGPAM-LKAEPtlveNQQAVIEY---RPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 179 TPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIvKNDYVASITFTGSPKVG--IGIKQKAGLKRVTLELGSNAAVII 256
Cdd:PRK13968 165 VMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMI-NDSRIAAVTVTGSVRAGaaIGAQAGAALKKCVLELGGSDPFIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 257 DEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVS--ALISKRDveRID 334
Cdd:PRK13968 244 LNDADL-ELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGpmARFDLRD--ELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 335 MWVQEAIKEGATVLCGGKK--RDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTN 412
Cdd:PRK13968 321 HQVEATLAEGARLLLGGEKiaGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTT 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 413 NLFKAMRAIDELEVGGVMINDIPTF--RVdhmPYGGVKESGTGREGIKYAIEEMTEMKLV 470
Cdd:PRK13968 401 DETQARQMAARLECGGVFINGYCASdaRV---AFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
5-453 |
8.28e-70 |
|
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: 230.93 E-value: 8.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDWKSVNTYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEII 84
Cdd:cd07125 36 IINGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 85 AKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGEtlplDAAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPA 164
Cdd:cd07125 116 AAEAGKTLADADAEVREAIDFCRYYAAQARELFSD----PELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 165 IAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGI-KQKAGLKR 243
Cdd:cd07125 192 LAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLInRALAERDG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 244 VTLEL-----GSNaAVIIDE--DVEL-TDEIIErvkwGAFVNNGQVCiSVQRV-FVHETKMHEFLSKLKKAMESVVVGDP 314
Cdd:cd07125 272 PILPLiaetgGKN-AMIVDStaLPEQaVKDVVQ----SAFGSAGQRC-SALRLlYLQEEIAERFIEMLKGAMASLKVGDP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 315 LLEETDVSALISKRDVERIDMWVQEAIKEgATVLCGGK--KRDARIFEPTVLKNVpnHVSVQCQEVFGPLMTVNTFK--E 390
Cdd:cd07125 346 WDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPldDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKaeD 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446639112 391 FDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINdiptfR------VDHMPYGGVKESGTG 453
Cdd:cd07125 423 LDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN-----RnitgaiVGRQPFGGWGLSGTG 486
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
56-472 |
3.68e-69 |
|
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: 226.64 E-value: 3.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 56 TLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKP-IRAARGEVDRTVQTYKFAAE------EAKRIYgetLPLDAAPG 128
Cdd:cd07087 16 TRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPpAEAYLTEIAVVLGEIDHALKhlkkwmKPRRVS---VPLLLQPA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 129 AdgriAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAgLPNGALNIISGpGS 208
Cdd:cd07087 93 K----AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-GV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 209 TVGEAIVKN--DYvasITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCIS 284
Cdd:cd07087 167 EVATALLAEpfDH---IFFTGSPAVGKIVMEAAAkhLTPVTLELGGKSPCIVDKDANL-EVAARRIAWGKFLNAGQTCIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 285 VQRVFVHETKMHEFLSKLKKAMESvVVGDPLLEETDVSALISKRDVERIdmwvqEAIKEGATVLCGGK-KRDARIFEPTV 363
Cdd:cd07087 243 PDYVLVHESIKDELIEELKKAIKE-FYGEDPKESPDYGRIINERHFDRL-----ASLLDDGKVVIGGQvDKEERYIAPTI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 364 LKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIND-IPTFRVDHM 442
Cdd:cd07087 317 LDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDvLLHAAIPNL 396
|
410 420 430
....*....|....*....|....*....|
gi 446639112 443 PYGGVKESGTGREGIKYAIEEMTEMKLVCI 472
Cdd:cd07087 397 PFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
5-460 |
1.33e-63 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 213.67 E-value: 1.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 5 LYINGDW--------KSVNtykplyaPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDER 76
Cdd:PRK09457 3 LWINGDWiagqgeafESRN-------PVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 77 REEFAEIIAKEAAKPIRAARGEV-------DRTVQTYkfaaeeAKRIyGETlpldAAPGADGRIAytIR-KPIGVIGAIT 148
Cdd:PRK09457 76 KEELAEVIARETGKPLWEAATEVtaminkiAISIQAY------HERT-GEK----RSEMADGAAV--LRhRPHGVVAVFG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 149 PFNFPLNLV-AHKVgPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGpGSTVGEAIVKNDYVASITFTG 227
Cdd:PRK09457 143 PYNFPGHLPnGHIV-PALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 228 SPKVGIGI-KQKAGL--KRVTLELGSNAAVIIDeDVELTDEIIERVKWGAFVNNGQVCISVQRVFVHETKM-HEFLSKLK 303
Cdd:PRK09457 221 SANTGYLLhRQFAGQpeKILALEMGGNNPLVID-EVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 304 KAMESVVVGDPLLEETD-VSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDAR-------IFEPTVLKNVPNhvsvqc 375
Cdd:PRK09457 300 AVAKRLTVGRWDAEPQPfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGtglltpgIIDVTGVAELPD------ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 376 QEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFRVDHMPYGGVKESGTGRE 455
Cdd:PRK09457 374 EEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASSAAPFGGVGASGNHRP 453
|
....*
gi 446639112 456 GIKYA 460
Cdd:PRK09457 454 SAYYA 458
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
62-474 |
3.66e-63 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 212.58 E-value: 3.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 62 RATILEKVAQKMDERREEFAEIIAKEAAKP--------IRAARGEVDRTVQTYKfaaEEAKRIYGETlPLDAAPGAdgri 133
Cdd:PTZ00381 31 RKQQLRNLLRMLEENKQEFSEAVHKDLGRHpfetkmteVLLTVAEIEHLLKHLD---EYLKPEKVDT-VGVFGPGK---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 134 AYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAgLPNGALNIISGpGSTVGEA 213
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 214 IVKN--DYvasITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDVELTdEIIERVKWGAFVNNGQVCISVQRVF 289
Cdd:PTZ00381 181 LLKEpfDH---IFFTGSPRVGKLVMQAAAenLTPCTLELGGKSPVIVDKSCNLK-VAARRIAWGKFLNAGQTCVAPDYVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 290 VHETKMHEFLSKLKKAMESVVVGDPlLEETDVSALISKRDVERIdmwvQEAIKE-GATVLCGGK-KRDARIFEPTVLKNV 367
Cdd:PTZ00381 257 VHRSIKDKFIEALKEAIKEFFGEDP-KKSEDYSRIVNEFHTKRL----AELIKDhGGKVVYGGEvDIENKYVAPTIIVNP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 368 -PNHVSVQcQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIND-IPTFRVDHMPYG 445
Cdd:PTZ00381 332 dLDSPLMQ-EEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDcVFHLLNPNLPFG 410
|
410 420
....*....|....*....|....*....
gi 446639112 446 GVKESGTGREGIKYAIEEMTEMKLVCIKK 474
Cdd:PTZ00381 411 GVGNSGMGAYHGKYGFDTFSHPKPVLNKS 439
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
46-454 |
9.02e-62 |
|
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: 207.46 E-value: 9.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 46 AAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPiraaRGEVDRT--VQTYKFAAEEAKRIYGETLPL 123
Cdd:cd07134 6 AQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKP----AAEVDLTeiLPVLSEINHAIKHLKKWMKPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 124 DAAP-----GADGRIAYtirKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPng 198
Cdd:cd07134 82 RVRTplllfGTKSKIRY---EPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDE-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 199 alniisgpgSTVgeAIVKNDYVAS----------ITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDVELtDEI 266
Cdd:cd07134 157 ---------DEV--AVFEGDAEVAqallelpfdhIFFTGSPAVGKIVMAAAAkhLASVTLELGGKSPTIVDETADL-KKA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 267 IERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEET-DVSALISKRDVERIDMWVQEAIKEGA 345
Cdd:cd07134 225 AKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDAVAKGA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 346 TVLCGGKKRDA-RIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDEL 424
Cdd:cd07134 305 KVEFGGQFDAAqRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLART 384
|
410 420 430
....*....|....*....|....*....|.
gi 446639112 425 EVGGVMINDIPTFRVD-HMPYGGVKESGTGR 454
Cdd:cd07134 385 SSGGVVVNDVVLHFLNpNLPFGGVNNSGIGS 415
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
16-470 |
1.43e-59 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 202.80 E-value: 1.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 16 TYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAA 95
Cdd:TIGR01722 16 TYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 96 RGEVDRTVQTYKFAAEEAKRIYGETLPlDAAPGADgriAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKP 175
Cdd:TIGR01722 96 LGDVARGLEVVEHACGVNSLLKGETST-QVATRVD---VYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 176 ADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVgEAIVKNDYVASITFTGSPKVGIGIKQKAGL--KRVTLELGSNAA 253
Cdd:TIGR01722 172 SEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAV-DRLLEHPDVKAVSFVGSTPIGRYIHTTGSAhgKRVQALGGAKNH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 254 VIIDEDVELtDEIIERVKWGAFVNNGQVCISVQR-VFVHETKmhEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVER 332
Cdd:TIGR01722 251 MVVMPDADK-DAAADALVGAAYGAAGQRCMAISAaVLVGAAD--EWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 333 IDMWVQEAIKEGATVLCGGKKRDARIFE------PTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQ 406
Cdd:TIGR01722 328 VASLIAGGAAEGAEVLLDGRGYKVDGYEegnwvgPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNG 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446639112 407 AGVFTNNLFKAMRAIDELEVGGVMIN-DIPTfRVDHMPYGGVKESGTGREGI--KYAIEEMTEMKLV 470
Cdd:TIGR01722 408 TAIFTRDGAAARRFQHEIEVGQVGVNvPIPV-PLPYFSFTGWKDSFFGDHHIygKQGTHFYTRGKTV 473
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
37-470 |
6.02e-59 |
|
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: 199.94 E-value: 6.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 37 EEDVKEAVTAAKNAMTKmntlSAYDRATILEKVAQKMDERREEFAEIIAKEAAKP-IRAARGEVDRTVQTYKFAAEEAKR 115
Cdd:cd07137 2 PRLVRELRETFRSGRTR----SAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPsAESFRDEVSVLVSSCKLAIKELKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 116 IYGE---TLPLDAAPgADGRIaytIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEE 192
Cdd:cd07137 78 WMAPekvKTPLTTFP-AKAEI---VSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 193 AgLPNGALNIISGpGSTVGEAIVKNDYvASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDVELtDEIIERV 270
Cdd:cd07137 154 Y-LDTKAIKVIEG-GVPETTALLEQKW-DKIFFTGSPRVGRIIMAAAAkhLTPVTLELGGKCPVIVDSTVDL-KVAVRRI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 271 ---KWGAfvNNGQVCISVQRVFVHEtkmhEFLSKLKKAMESVV---VGDPLLEETDVSALISKRDVERIDMWVQEAIKEG 344
Cdd:cd07137 230 aggKWGC--NNGQACIAPDYVLVEE----SFAPTLIDALKNTLekfFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVAD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 345 ATVLCGGKKRDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDEL 424
Cdd:cd07137 304 KIVHGGERDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAET 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446639112 425 EVGGVMIND-IPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLV 470
Cdd:cd07137 384 SSGGVTFNDtVVQYAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
7-453 |
7.56e-59 |
|
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: 201.68 E-value: 7.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 7 INGDWKSVNTYKPLYAPYS-EETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIA 85
Cdd:TIGR01238 42 IGHSYKADGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 86 KEAAKPIRAARGEVDRTVQTYKFAAEEAKriygETLPLDAApgadgriaytirKPIGVIGAITPFNFPLNLVAHKVGPAI 165
Cdd:TIGR01238 122 REAGKTIHNAIAEVREAVDFCRYYAKQVR----DVLGEFSV------------ESRGVFVCISPWNFPLAIFTGQISAAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 166 AAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQ---KAGLK 242
Cdd:TIGR01238 186 AAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQtlaQREDA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 243 RVTL--ELGSNAAVIIDEDVeLTDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETD 320
Cdd:TIGR01238 266 PVPLiaETGGQNAMIVDSTA-LPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 321 VSALISKRDVERIDMWVQEAIKEGATV--LCGGKKRDAR--IFEPTVLKNVPNHVSVQcQEVFGPLMTVNTFK--EFDEA 394
Cdd:TIGR01238 345 VGPVIDAEAKQNLLAHIEHMSQTQKKIaqLTLDDSRACQhgTFVAPTLFELDDIAELS-EEVFGPVLHVVRYKarELDQI 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 395 IEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIN-DIPTFRVDHMPYGGVKESGTG 453
Cdd:TIGR01238 424 VDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNrNQVGAVVGVQPFGGQGLSGTG 483
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
18-453 |
1.20e-58 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 208.51 E-value: 1.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 18 KPLYAPY-SEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAAR 96
Cdd:PRK11904 564 RPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 97 GEVDRTVQTYKFAAEEAKRIYGETLPLdaaPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPA 176
Cdd:PRK11904 644 AEVREAVDFCRYYAAQARRLFGAPEKL---PGPTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPA 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 177 DQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQ----KAGlKRVTL--ELGS 250
Cdd:PRK11904 721 EQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRtlaaRDG-PIVPLiaETGG 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 251 NAAVIID-----EDVelTDEIIErvkwGAFVNNGQVCiSVQRV-FVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSAL 324
Cdd:PRK11904 800 QNAMIVDstalpEQV--VDDVVT----SAFRSAGQRC-SALRVlFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPV 872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 325 ISKRDVERIDMWVqEAIKEGATVLCGGKKRDA---------RIFEptvlknVPNhVSVQCQEVFGPLMTVNTFK--EFDE 393
Cdd:PRK11904 873 IDAEAKANLDAHI-ERMKREARLLAQLPLPAGtenghfvapTAFE------IDS-ISQLEREVFGPILHVIRYKasDLDK 944
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446639112 394 AIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINdiptfR------VDHMPYGGVKESGTG 453
Cdd:PRK11904 945 VIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN-----RnqigavVGVQPFGGQGLSGTG 1005
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
66-465 |
4.90e-57 |
|
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: 195.13 E-value: 4.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 66 LEKVAQKMDERREEFAEIIAKEAAKPIRAAR-GEVDRTVQTYKFAAEEAKR-IYGETLPLDAAPGADGRIayTIRK-PIG 142
Cdd:cd07135 33 LKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKNDILHMLKNLKKwAKDEKVKDGPLAFMFGKP--RIRKePLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 143 VIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAgLPNGALNIISG--PGSTvgeAIVKNDYv 220
Cdd:cd07135 111 VVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGgvPETT---ALLEQKF- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 221 ASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEF 298
Cdd:cd07135 186 DKIFYTGSGRVGRIIAEAAAkhLTPVTLELGGKSPVIVTKNADL-ELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 299 LSKLKKAMESVVVGDPlLEETDVSALISKRDVERIDMWVQEAikEGATVLCGGKKRDARIFEPTVLKNVPNHVSVQCQEV 378
Cdd:cd07135 265 VEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLLDTT--KGKVVIGGEMDEATRFIPPTIVSDVSWDDSLMSEEL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 379 FGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDipTF---RVDHMPYGGVKESGTGRE 455
Cdd:cd07135 342 FGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVIND--TLihvGVDNAPFGGVGDSGYGAY 419
|
410
....*....|
gi 446639112 456 GIKYAIEEMT 465
Cdd:cd07135 420 HGKYGFDTFT 429
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
134-454 |
6.92e-55 |
|
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: 189.23 E-value: 6.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 134 AYTIRKPIGVIGAITPFNFPLNLVahkVGP---AIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNgALNIISGpGSTV 210
Cdd:cd07133 95 AEVEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTG-GADV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 211 GEAIVKNDYvASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRV 288
Cdd:cd07133 170 AAAFSSLPF-DHLLFTGSTAVGRHVMRAAAenLTPVTLELGGKSPAIIAPDADL-AKAAERIAFGKLLNAGQTCVAPDYV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 289 FVHETKMHEFLSKLKKAMESV---VVGDPlleetDVSALISKRDVERIDMWVQEAIKEGATVL-CGGKKRDA---RIFEP 361
Cdd:cd07133 248 LVPEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIeLNPAGEDFaatRKLPP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 362 TVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNlfKAMRA--IDELEVGGVMINDIpTFRV 439
Cdd:cd07133 323 TLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGED--KAEQDrvLRRTHSGGVTINDT-LLHV 399
|
330
....*....|....*..
gi 446639112 440 --DHMPYGGVKESGTGR 454
Cdd:cd07133 400 aqDDLPFGGVGASGMGA 416
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
134-454 |
7.31e-55 |
|
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: 189.64 E-value: 7.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 134 AYTIRKPIGVIGAITPFNFPLNL-VAHKVGpAIAAGNTVVLKPADQTPLSSYALVELFEEAgLPNGALNIISGpGSTVGE 212
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLaLAPLIG-AIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 213 AIV--KNDYvasITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRV 288
Cdd:cd07136 171 ELLdqKFDY---IFFTGSVRVGKIVMEAAAkhLTPVTLELGGKSPCIVDEDANL-KLAAKRIVWGKFLNAGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 289 FVHETKMHEFLSKLKKAMESVVVGDPLLEEtDVSALISKRDVERIdmwvqEAIKEGATVLCGGK-KRDARIFEPTVLKNV 367
Cdd:cd07136 247 LVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRL-----AGLLDNGKIVFGGNtDRETLYIEPTILDNV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 368 PNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIND-IPTFRVDHMPYGG 446
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDtIMHLANPYLPFGG 400
|
....*...
gi 446639112 447 VKESGTGR 454
Cdd:cd07136 401 VGNSGMGS 408
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
28-452 |
6.95e-54 |
|
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: 188.56 E-value: 6.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 28 TLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKM-DERReefAEIIAKEA---AKPIRAArgEVD--- 100
Cdd:cd07123 59 VLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLsGKYR---YELNAATMlgqGKNVWQA--EIDaac 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 101 RTVQTYKFAAEEAKRIYGETlPLDAAPGADGRIAYtirKPI-GVIGAITPFNFP---LNLVAhkvGPAIAaGNTVVLKPA 176
Cdd:cd07123 134 ELIDFLRFNVKYAEELYAQQ-PLSSPAGVWNRLEY---RPLeGFVYAVSPFNFTaigGNLAG---APALM-GNVVLWKPS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 177 DQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAG--------LKRVTLEL 248
Cdd:cd07123 206 DTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGenldryrtYPRIVGET 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 249 GSNAAVIIDE--DVELTDEIIERvkwGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALIS 326
Cdd:cd07123 286 GGKNFHLVHPsaDVDSLVTATVR---GAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVID 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 327 KRDVERIDMWVQEAIKE-GATVLCGGKKRDARIF--EPTVL--KNvPNHVSVQcQEVFGPLMTVNTF--KEFDEAIEQVN 399
Cdd:cd07123 363 EKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYfvEPTVIetTD-PKHKLMT-EEIFGPVLTVYVYpdSDFEETLELVD 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446639112 400 N-SRYGLQAGVFTNNLfKAMR-AIDELE--VGGVMINDIPTFR-VDHMPYGGVKESGT 452
Cdd:cd07123 441 TtSPYALTGAIFAQDR-KAIReATDALRnaAGNFYINDKPTGAvVGQQPFGGARASGT 497
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
23-470 |
8.63e-53 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 187.65 E-value: 8.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 23 PYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRT 102
Cdd:PLN02419 136 PATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 103 VQTYKFAAEEAKRIYGETLPlDAAPGADgriAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLS 182
Cdd:PLN02419 216 LEVVEHACGMATLQMGEYLP-NVSNGVD---TYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 183 SYALVELFEEAGLPNGALNIISGPGSTVgEAIVKNDYVASITFTGSPKVGIGIKQKAGL--KRVTLELGS--NAAVIIDE 258
Cdd:PLN02419 292 SVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAkgKRIQSNMGAknHGLVLPDA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 259 DVELTDEIIERVKWGAfvnNGQVCISVQR-VFVHETKMHE-FLSKLKKAMESVVVGDPlleETDVSALISKRDVERIDMW 336
Cdd:PLN02419 371 NIDATLNALLAAGFGA---AGQRCMALSTvVFVGDAKSWEdKLVERAKALKVTCGSEP---DADLGPVISKQAKERICRL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 337 VQEAIKEGATVLCGGKK------RDARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVF 410
Cdd:PLN02419 445 IQSGVDDGAKLLLDGRDivvpgyEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIF 524
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446639112 411 TNNLFKAMRAIDELEVGGVMINDIPTFRVDHMPYGGVKESGTGREGI--KYAIEEMTEMKLV 470
Cdd:PLN02419 525 TSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFygKAGVDFFTQIKLV 586
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
36-453 |
1.63e-51 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 188.15 E-value: 1.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 36 TEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAkr 115
Cdd:PRK11905 588 SAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQA-- 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 116 iygETLPLDAApgadgriaytiRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGL 195
Cdd:PRK11905 666 ---RRLLNGPG-----------HKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGV 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 196 PNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIkQKAGLKR----VTL--ELGSNAAVIID-----EDVelTD 264
Cdd:PRK11905 732 PKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLI-QRTLAKRsgppVPLiaETGGQNAMIVDssalpEQV--VA 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 265 EIIErvkwGAFVNNGQVCiSVQRV-FVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEAIKE 343
Cdd:PRK11905 809 DVIA----SAFDSAGQRC-SALRVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAA 883
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 344 GATVLCGGKKRDA---RIFEPTVLKnvPNHVSVQCQEVFGPLMTVNTFK--EFDEAIEQVNNSRYGLQAGVFTnnlfkam 418
Cdd:PRK11905 884 GRLVHQLPLPAETekgTFVAPTLIE--IDSISDLEREVFGPVLHVVRFKadELDRVIDDINATGYGLTFGLHS------- 954
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 446639112 419 RaIDE--------LEVGGVMINdiptfR------VDHMPYGGVKESGTG 453
Cdd:PRK11905 955 R-IDEtiahvtsrIRAGNIYVN-----RniigavVGVQPFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
18-453 |
4.58e-51 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 186.68 E-value: 4.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 18 KPLYAPY-SEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAAR 96
Cdd:COG4230 572 RPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAI 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 97 GEVDRTVQTYKFAAEEAKRiygetlpLDAAPgadgriayTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPA 176
Cdd:COG4230 652 AEVREAVDFCRYYAAQARR-------LFAAP--------TVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPA 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 177 DQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIkQKAGLKR----VTL--ELGS 250
Cdd:COG4230 717 EQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLI-NRTLAARdgpiVPLiaETGG 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 251 NAAVIID-----EDVelTDEIIErvkwGAFVNNGQVCiSVQRV-FVHETKMHEFLSKLKKAMESVVVGDPLLEETDVSAL 324
Cdd:COG4230 796 QNAMIVDssalpEQV--VDDVLA----SAFDSAGQRC-SALRVlCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPV 868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 325 ISKRDVERIDMWVQEAIKEGATVlcggkkrdARIFEPTVLKN---VP------NHVSVQCQEVFGPLMTVNTFK--EFDE 393
Cdd:COG4230 869 IDAEARANLEAHIERMRAEGRLV--------HQLPLPEECANgtfVAptlieiDSISDLEREVFGPVLHVVRYKadELDK 940
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446639112 394 AIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINdiptfRvdHM--------PYGGVKESGTG 453
Cdd:COG4230 941 VIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN-----R--NIigavvgvqPFGGEGLSGTG 1001
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
6-455 |
1.32e-48 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 174.25 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 6 YINGDWKSVNTYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIA 85
Cdd:PLN02315 24 YVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 86 KEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPLDAApgadGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAI 165
Cdd:PLN02315 104 LEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERP----NHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 166 AAGNTVVLKPADQTPLSSYALV----ELFEEAGLPNGALNIISGpGSTVGEAIVKNDYVASITFTGSPKVGIGIKQ--KA 239
Cdd:PLN02315 180 VCGNCVVWKGAPTTPLITIAMTklvaEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQtvNA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 240 GLKRVTLELGSNAAVII--DEDVELTdeiIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLE 317
Cdd:PLN02315 259 RFGKCLLELSGNNAIIVmdDADIQLA---VRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 318 ETDVSALISKRDVERIDMWVQEAIKEGATVLCGGK--KRDARIFEPTVLKNVPNHVSVQcQEVFGPLMTVNTFKEFDEAI 395
Cdd:PLN02315 336 GTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSaiESEGNFVQPTIVEISPDADVVK-EELFGPVLYVMKFKTLEEAI 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446639112 396 EQVNNSRYGLQAGVFTNNLFKAMRAIDEL--EVGGVMINdIPTFRVD-HMPYGGVKESGTGRE 455
Cdd:PLN02315 415 EINNSVPQGLSSSIFTRNPETIFKWIGPLgsDCGIVNVN-IPTNGAEiGGAFGGEKATGGGRE 476
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
41-474 |
9.35e-45 |
|
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: 162.39 E-value: 9.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 41 KEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIR-AARGEVDRTVQTYKFAAEEAKR-IYG 118
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFeAVLSEILLVKNEIKYAISNLPEwMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 119 ETLPLDAAPGADGriAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELfeeagLP-- 196
Cdd:cd07132 81 EPVKKNLATLLDD--VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPky 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 197 --NGALNIISGpGSTVGEAIVKN--DYvasITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDVELtDEIIERV 270
Cdd:cd07132 154 ldKECYPVVLG-GVEETTELLKQrfDY---IFYTGSTSVGKIVMQAAAkhLTPVTLELGGKSPCYVDKSCDI-DVAARRI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 271 KWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPlLEETDVSALISKRDVERIdmwvqEAIKEGATVLCG 350
Cdd:cd07132 229 AWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDP-KESPDYGRIINDRHFQRL-----KKLLSGGKVAIG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 351 GKKRDA-RIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGV 429
Cdd:cd07132 303 GQTDEKeRYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGV 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446639112 430 MIND-IPTFRVDHMPYGGVKESGTGREGIKYAIEEMTEMKLVCIKK 474
Cdd:cd07132 383 CVNDtIMHYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVKS 428
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
74-470 |
5.02e-44 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 161.05 E-value: 5.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 74 DERREEFAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGE---TLPLDAAPGAdgriAYTIRKPIGVIGAITPF 150
Cdd:PLN02203 43 DNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMAPkkaKLPLVAFPAT----AEVVPEPLGVVLIFSSW 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 151 NFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEeAGLPNGALNIISGpGSTVGEAIVKNDYvASITFTGSPK 230
Cdd:PLN02203 119 NFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIP-KYLDSKAVKVIEG-GPAVGEQLLQHKW-DKIFFTGSPR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 231 VGIGIKQKAG--LKRVTLELGSNAAVIID-----EDVELTDEIIERVKWGAFvnNGQVCISVQRVFVHEtKMHEFLSKLK 303
Cdd:PLN02203 196 VGRIIMTAAAkhLTPVALELGGKCPCIVDslsssRDTKVAVNRIVGGKWGSC--AGQACIAIDYVLVEE-RFAPILIELL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 304 KAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDARIFEPTVLKNVPNHVSVQCQEVFGPLM 383
Cdd:PLN02203 273 KSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 384 TVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIND-IPTFRVDHMPYGGVKESGTGREGIKYAIE 462
Cdd:PLN02203 353 PIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDaIIQYACDSLPFGGVGESGFGRYHGKYSFD 432
|
....*...
gi 446639112 463 EMTEMKLV 470
Cdd:PLN02203 433 TFSHEKAV 440
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
34-453 |
2.15e-43 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 163.99 E-value: 2.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 34 QGTEEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEA 113
Cdd:PRK11809 678 EATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQV 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 114 KRIYG-ETlpldaapgadgriaytiRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEE 192
Cdd:PRK11809 758 RDDFDnDT-----------------HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLE 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 193 AGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGiGIKQKAGLKRVT---------LELGSNAAVIIDEDVeLT 263
Cdd:PRK11809 821 AGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVA-RLLQRNLAGRLDpqgrpipliAETGGQNAMIVDSSA-LT 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 264 DEIIERVKWGAFVNNGQVCiSVQRVF-VHETKMHEFLSKLKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEAIK 342
Cdd:PRK11809 899 EQVVADVLASAFDSAGQRC-SALRVLcLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRA 977
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 343 EGATVLCGGKKRDARI----FEPTVLKNVpNHVSVQCQEVFGPLMTVNTFK--EFDEAIEQVNNSRYGLQAGVFTNnlfk 416
Cdd:PRK11809 978 KGRPVFQAARENSEDWqsgtFVPPTLIEL-DSFDELKREVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTR---- 1052
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446639112 417 amraIDE--------LEVGGVMIN-DIPTFRVDHMPYGGVKESGTG 453
Cdd:PRK11809 1053 ----IDEtiaqvtgsAHVGNLYVNrNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
6-413 |
5.86e-39 |
|
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: 147.80 E-value: 5.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 6 YINGDWKS-VNTYKPLYAPYSEETLAEIAqGTEEDVKEAVTAAK----NAMTKMntlSAYDRATILEKVAQKMDERREEF 80
Cdd:cd07128 4 YVAGQWHAgTGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYARekggPALRAL---TFHERAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 81 AEIIAKEAAKPiRAARGEVDRTVQTYKFAAEEAKR--------IYGETLPLDAAPGADGRIAYTIRKpiGVIGAITPFNF 152
Cdd:cd07128 80 YALSAATGATR-RDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPLSKDGTFVGQHILTPRR--GVAVHINAFNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 153 PLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAG-LPNGALNIISGPGSTVGEAIVKNDYVasiTFTGSPKV 231
Cdd:cd07128 157 PVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGEQDVV---AFTGSAAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 232 GIGIKQKAGLK----RVTLELGS-NAAVI---IDEDVELTDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLK 303
Cdd:cd07128 234 AAKLRAHPNIVarsiRFNAEADSlNAAILgpdATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 304 KAMESVVVGDPLLEETDVSALISKRDVEriDMWVQ-EAIKEGATVLCGGKKRDARI---------FEPTVL--KNVPNHV 371
Cdd:cd07128 314 ARLAKVVVGDPRLEGVRMGPLVSREQRE--DVRAAvATLLAEAEVVFGGPDRFEVVgadaekgafFPPTLLlcDDPDAAT 391
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446639112 372 SVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNN 413
Cdd:cd07128 392 AVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
134-470 |
1.74e-37 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 143.26 E-value: 1.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 134 AYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAgLPNGALNIISGpGSTVGEA 213
Cdd:PLN02174 106 AEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEG-AVTETTA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 214 IVKNDYvASITFTGSPKVGIGIKQKAG--LKRVTLELGSNAAVIIDEDVEL--TDEIIERVKWGAfvNNGQVCISVQRVF 289
Cdd:PLN02174 184 LLEQKW-DKIFYTGSSKIGRVIMAAAAkhLTPVVLELGGKSPVVVDSDTDLkvTVRRIIAGKWGC--NNGQACISPDYIL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 290 VHETKMHEFLSKLKKAMESVVVGDPLlEETDVSALISKRDVERIDMWVQEAIKEGATVLCGGKKRDARIFEPTVLKNVPN 369
Cdd:PLN02174 261 TTKEYAPKVIDAMKKELETFYGKNPM-ESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 370 HVSVQCQEVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMINDIPTFRVDH-MPYGGVK 448
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHtLPFGGVG 419
|
330 340
....*....|....*....|..
gi 446639112 449 ESGTGREGIKYAIEEMTEMKLV 470
Cdd:PLN02174 420 ESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
40-460 |
2.48e-35 |
|
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: 136.60 E-value: 2.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 40 VKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAArGEVDRTVQTYKFAAEEAKRIYGE 119
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAFVIYSYRIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 120 TLPLDAAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAG-LPNG 198
Cdd:cd07084 80 HEPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 199 ALNIISGPGSTvGEAIVKNDYVASITFTGSPKVGIGIKQKAGLKRVTLELGSNAAVIIDEDVELTDEIIERVKWGAFVNN 278
Cdd:cd07084 160 DVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDAQAVDYVAWQCVQDMTACS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 279 GQVCISVQRVFVHETKMHE-FLSKLKKAMESVVVGDPLL---EETDVSALISKRDVEridmwvqeaikEGATVLCGGKKR 354
Cdd:cd07084 239 GQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLEDLLLgpvQTFTTLAMIAHMENL-----------LGSVLLFSGKEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 355 DARIFEPTVLKNVPNHVSVQC-----------QEVFGPLMTVNTFKEFDEA--IEQVNNSRYGLQAGVFTNNLFKAMRAI 421
Cdd:cd07084 308 KNHSIPSIYGACVASALFVPIdeilktyelvtEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELI 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446639112 422 DELEV-----------GGVMINDIPTFrvdHMPYGGVKESGTGREGIKYA 460
Cdd:cd07084 388 GNLWVagrtyailrgrTGVAPNQNHGG---GPAADPRGAGIGGPEAIKLV 434
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
6-456 |
4.82e-27 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 113.65 E-value: 4.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 6 YINGDWKS-VNTYKPLYAPYSEETLAEiAQGTEEDVKEAVTAAKN-AMTKMNTLSAYDRATILEKVAQKMDERREEFAEI 83
Cdd:PRK11903 8 YVAGRWQAgSGAGTPLFDPVTGEELVR-VSATGLDLAAAFAFAREqGGAALRALTYAQRAALLAAIVKVLQANRDAYYDI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 84 IAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRIYGETLPLDAAPGADGR--------IAYTIRkpiGVIGAITPFNFPLN 155
Cdd:PRK11903 87 ATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKdpafqgqhVLVPTR---GVALFINAFNFPAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 156 LVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAG-LPNGALNIISGPGSTVGEAIVKNDYVAsitFTGSPKVGIG 234
Cdd:PRK11903 164 GLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDHLQPFDVVS---FTGSAETAAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 235 IKQKAGLK----RVTLELGS-NAAVII---DEDVELTDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAM 306
Cdd:PRK11903 241 LRSHPAVVqrsvRVNVEADSlNSALLGpdaAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 307 ESVVVGDPLLEETDVSALISKRDVERIDMWVqEAIKEGATVLCGGKKRDARIFEPTVLKNVP----------NHVSVQCQ 376
Cdd:PRK11903 321 AKTTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFALVDADPAVAACVGptllgasdpdAATAVHDV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 377 EVFGPLMTVNTFKEFDEAIEQVNNSRYGLQAGVFTNNLFKAMRAIDELEV--GGVMINDiPTFRVDHMPYGGVK----ES 450
Cdd:PRK11903 400 EVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADshGRVHVIS-PDVAALHTGHGNVMpqslHG 478
|
....*.
gi 446639112 451 GTGREG 456
Cdd:PRK11903 479 GPGRAG 484
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
40-436 |
3.60e-26 |
|
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: 110.32 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 40 VKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIRAARGEVDRTVQTYKFAAEEAKRiyGE 119
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVRE--GS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 120 tlPLDA-----------APGADGRiayTIRKPIGVIGAITPFNFPLnlvAHKVG-----PAIAAGNTVVLK--PA--DQT 179
Cdd:cd07129 79 --WLDAridpadpdrqpLPRPDLR---RMLVPLGPVAVFGASNFPL---AFSVAggdtaSALAAGCPVVVKahPAhpGTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 180 PLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAgLKR-----VTLELGS-NAA 253
Cdd:cd07129 151 ELVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAA-AARpepipFYAELGSvNPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 254 VIIDEDV-----ELTDEIIERVKWGAfvnnGQVCISVQRVFVHETK-MHEFLSKLKKAMESVVVGdPLLEETDVSALisK 327
Cdd:cd07129 230 FILPGALaergeAIAQGFVGSLTLGA----GQFCTNPGLVLVPAGPaGDAFIAALAEALAAAPAQ-TMLTPGIAEAY--R 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 328 RDVERIdmwvqEAIKEGATVLCGGKKRDARIFEPTVLK----NVPNHVSVQcQEVFGP---LMTVNTFKEFDEAIEQVNN 400
Cdd:cd07129 303 QGVEAL-----AAAPGVRVLAGGAAAEGGNQAAPTLFKvdaaAFLADPALQ-EEVFGPaslVVRYDDAAELLAVAEALEG 376
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 446639112 401 SrygLQAGVF--TNNLFKAMRAIDELE--VGGVMINDIPT 436
Cdd:cd07129 377 Q---LTATIHgeEDDLALARELLPVLErkAGRLLFNGWPT 413
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
6-413 |
8.49e-24 |
|
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: 103.73 E-value: 8.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 6 YINGDWKSVNTYKPLYAPYSEETLAEIAQGTEEDVKEAVTAAKnAMTKM---NTLSAYDR----ATILEKVAQKMDERRE 78
Cdd:cd07126 2 LVAGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLR-QCPKSglhNPLKNPERyllyGDVSHRVAHELRKPEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 79 E--FAEIIAKEAAKPIRAARGEVDRTVQTYK-FAAEEAKRI-YGETLPLDAApgadGRIAYTIRKPIGVIGAITPFNFPL 154
Cdd:cd07126 81 EdfFARLIQRVAPKSDAQALGEVVVTRKFLEnFAGDQVRFLaRSFNVPGDHQ----GQQSSGYRWPYGPVAIITPFNFPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 155 NLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEAGLPNGALNIISGPGSTVGEAIVKNDYvASITFTGSPKVGig 234
Cdd:cd07126 157 EIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANP-RMTLFTGSSKVA-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 235 ikqkaglKRVTLELGSNAAV--------IIDEDVELTDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHE-FLSKLKKA 305
Cdd:cd07126 234 -------ERLALELHGKVKLedagfdwkILGPDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAgILDKLKAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 306 -----MESVVVGdPLLEETdvsaliSKRDVERIDMWVQeaiKEGATVLCGGKK-------------RDARIFEPTVLKNV 367
Cdd:cd07126 307 aeqrkLEDLTIG-PVLTWT------TERILDHVDKLLA---IPGAKVLFGGKPltnhsipsiygayEPTAVFVPLEEIAI 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 446639112 368 PNHVSVQCQEVFGPLMTVNTFK--EFDEAIEQVNNSRYGLQAGVFTNN 413
Cdd:cd07126 377 EENFELVTTEVFGPFQVVTEYKdeQLPLVLEALERMHAHLTAAVVSND 424
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
38-396 |
6.13e-14 |
|
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: 73.43 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 38 EDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEaakpirAARGEVDRTVQTYKFAAEEAKRIy 117
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEE------TGMGRVEDKIAKNHLAAEKTPGT- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 118 gETLPLDAAPGaDGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEA---- 193
Cdd:cd07121 77 -EDLTTTAWSG-DNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAiaea 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 194 GLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGigikqKAGL---KRVTLELGSNAAVIIDE--DVELTDEIIe 268
Cdd:cd07121 155 GGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVV-----KAALssgKKAIGAGAGNPPVVVDEtaDIEKAARDI- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 269 rVKWGAFVNNgQVCISVQRVFVHETKMHEFLSKLKKAMESVVVGDPLLEETDVsaLISKRDVERIDM-WV-QEA--IKEG 344
Cdd:cd07121 229 -VQGASFDNN-LPCIAEKEVIAVDSVADYLIAAMQRNGAYVLNDEQAEQLLEV--VLLTNKGATPNKkWVgKDAskILKA 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446639112 345 ATVLCGGKKRdaRIFEPTvlknVPNHVSVQCqEVFGPLMTVNTFKEFDEAIE 396
Cdd:cd07121 305 AGIEVPADIR--LIIVET----DKDHPFVVE-EQMMPILPVVRVKNFDEAIE 349
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
38-305 |
1.07e-11 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 66.46 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 38 EDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEaakpirAARGEVDRTVQTYKFAAEEAKRIy 117
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEE------TGMGRVEDKIAKNVAAAEKTPGV- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 118 gETLPLDAAPGADGRIAYTiRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEA---- 193
Cdd:PRK15398 109 -EDLTTEALTGDNGLTLIE-YAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAivaa 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 194 GLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGigikqKAGL---KRVTLELGSNAAVIIDE--DVELTDEIIe 268
Cdd:PRK15398 187 GGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVV-----KAAMksgKKAIGAGAGNPPVVVDEtaDIEKAARDI- 260
|
250 260 270
....*....|....*....|....*....|....*..
gi 446639112 269 rVKWGAFVNNgQVCISVQRVFVHETKMHEFLSKLKKA 305
Cdd:PRK15398 261 -VKGASFDNN-LPCIAEKEVIVVDSVADELMRLMEKN 295
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
42-396 |
4.27e-11 |
|
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: 64.59 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 42 EAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKpiraarGEVDRTVQTYKFAAEEAKRIYGETL 121
Cdd:cd07081 3 DAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGM------GRVEDKVIKNHFAAEYIYNVYKDEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 122 PLDAAPGADGRIAYTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKP----ADQTPLSSYALVELFEEAGLPN 197
Cdd:cd07081 77 TCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 198 GALNIISGPGSTVGEAIVKNDYVASITFTGSPKVgIGIKQKAGLKRVTLELGsNAAVIIDEDVELTDEIIERVKwGAFVN 277
Cdd:cd07081 157 NLIGWIDNPSIELAQRLMKFPGIGLLLATGGPAV-VKAAYSSGKPAIGVGAG-NTPVVIDETADIKRAVQSIVK-SKTFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 278 NGQVCISVQRVFV----HETKMHEFLSK---LKKAMESVVVGDPLLEETDVSALISKRDVERIDMWVQEAIKEGATVLCG 350
Cdd:cd07081 234 NGVICASEQSVIVvdsvYDEVMRLFEGQgayKLTAEELQQVQPVILKNGDVNRDIVGQDAYKIAAAAGLKVPQETRILIG 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446639112 351 gkkrdarifEPTVLKNVPNHVSvqcqEVFGPLMTVNTFKEFDEAIE 396
Cdd:cd07081 314 ---------EVTSLAEHEPFAH----EKLSPVLAMYRAANFADADA 346
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
46-302 |
3.36e-10 |
|
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: 61.86 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 46 AAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAEIIAKEAAKPIR--AARGEVDRTVQTYKFA--AEEAKRIYG-ET 120
Cdd:cd07077 2 SAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRslIANWIAMMGCSESKLYknIDTERGITAsVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 121 LPLDAAPGADGRIaYTIRKPIGVIGAITPFNFPLnLVAHKVGPAIAAGNTVVLKPADQTPLSSYALVELFEEA---GLPN 197
Cdd:cd07077 82 HIQDVLLPDNGET-YVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 198 GALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAGLKRVTLELGSNAAVIIDEDVELtDEIIERVKWGAFVN 277
Cdd:cd07077 160 ILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADE-ERASGSVHDSKFFD 238
|
250 260
....*....|....*....|....*....
gi 446639112 278 NgQVCISVQRVFVHET----KMHEFLSKL 302
Cdd:cd07077 239 Q-NACASEQNLYVVDDvldpLYEEFKLKL 266
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
40-432 |
1.52e-09 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, 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: 143440 [Multi-domain] Cd Length: 436 Bit Score: 59.81 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 40 VKEAVTAAKNAMTKMNTLS--AYDRatILEKVAQKMDERREEFAEIIAKE---------AAKPIRAARGEVD--RTVQTY 106
Cdd:cd07122 1 VDELVERARKAQREFATFSqeQVDK--IVEAVAWAAADAAEELAKMAVEEtgmgvvedkVIKNHFASEYVYNdiKDMKTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 107 KFAAE-EAKRIYgetlpldaapgadgriayTIRKPIGVIGAITPFNFPLNLVAHKVGPAIAAGNTVVLKPADQTPLSSYA 185
Cdd:cd07122 79 GVIEEdEEKGIV------------------EIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 186 LVEL----FEEAGLPNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKV------------GIGikqkAGlkrvtlelg 249
Cdd:cd07122 141 AAKImreaAVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGGPGMvkaayssgkpaiGVG----PG--------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 250 sNAAVIIDEDVELtDEIIERVKWGAFVNNGQVCISVQRVFVHETKMHEFLSKLKKAmesvvvGDPLLEETDVSALiskrd 329
Cdd:cd07122 208 -NVPAYIDETADI-KRAVKDIILSKTFDNGTICASEQSVIVDDEIYDEVRAELKRR------GAYFLNEEEKEKL----- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 330 veridmwvqeaikeGATVLCGGKKRDARIFEPTVLK-------NVPNHVSVQCQEVFG-------------PLMTVNTFK 389
Cdd:cd07122 275 --------------EKALFDDGGTLNPDIVGKSAQKiaelagiEVPEDTKVLVAEETGvgpeeplsreklsPVLAFYRAE 340
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446639112 390 EFDEAIE----QVNNSRYGLQAGVFTNNLFKAMRAIDELEVGGVMIN 432
Cdd:cd07122 341 DFEEALEkareLLEYGGAGHTAVIHSNDEEVIEEFALRMPVSRILVN 387
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
39-396 |
2.54e-09 |
|
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: 59.41 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 39 DVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEFAE----------IIAKEAAKPiraarGEVDRTVQTYKF 108
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHavmhttgqafMMAFQAGGP-----HAQDRGLEAVAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 109 AAEEAKRIYGETLpLDAAPGADGRIA----YTIrKPIGVIGAITPFNFPL-----NLVAhkvgpAIAAGNTVVLKPADQT 179
Cdd:cd07127 160 AWREMSRIPPTAE-WEKPQGKHDPLAmektFTV-VPRGVALVIGCSTFPTwngypGLFA-----SLATGNPVIVKPHPAA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 180 PLSSYALV----ELFEEAGL-PNGALNIISGPGSTVGEAIVKNDYVASITFTGSPKVGIGIKQKAGLKRVTLELGSNAAV 254
Cdd:cd07127 233 ILPLAITVqvarEVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQVYTEKAGVNTV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 255 IIDEdvelTDEIIERVKWGAF---VNNGQVCISVQRVFVHETKMH---------EFLSKLKKAMESvVVGDPLLEETDVS 322
Cdd:cd07127 313 VVDS----TDDLKAMLRNLAFslsLYSGQMCTTPQNIYVPRDGIQtddgrksfdEVAADLAAAIDG-LLADPARAAALLG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 323 ALISKRDVERIdmwvqEAIKEGATVLCGGKKR------DARIFEPTVLKNVPNHVSVQCQEVFGPLMTVNTFKEFDEAIE 396
Cdd:cd07127 388 AIQSPDTLARI-----AEARQLGEVLLASEAVahpefpDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIE 462
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
41-220 |
3.06e-07 |
|
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).
Pssm-ID: 143398 Cd Length: 406 Bit Score: 52.44 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 41 KEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEfaeiIAKEAAKPIRAARGE------VDR---TVQTYKFAAE 111
Cdd:cd07079 1 EELAKRAKAASRALATLSTEQKNAALLAIADALEANRDE----ILEANAKDLAAAREAglsealLDRlllTPERIEAMAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 112 EAKRIYGETLPLDAAPGA----DGRIAYTIRKPIGVIGAItpF-NFPlNLVAHKVGPAIAAGNTVVLKPADQTPLSSYAL 186
Cdd:cd07079 77 GLRQVAALPDPVGEVLRGwtlpNGLQIEKVRVPLGVIGII--YeSRP-NVTVDAAALCLKSGNAVILRGGSEALHSNRAL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 446639112 187 VELF----EEAGLPNGALNIISGPGSTVGEAIVK-NDYV 220
Cdd:cd07079 154 VEIIqealEEAGLPEDAVQLIPDTDREAVQELLKlDDYI 192
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
37-220 |
1.67e-05 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 46.98 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 37 EEDVKEAVTAAKNAMTKMNTLSAYDRATILEKVAQKMDERREEfaeiIAKEAAKPIRAARGE------VDRTVQTykfaa 110
Cdd:PRK00197 3 MEYLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAE----ILAANAKDLAAARANglsaamLDRLLLT----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446639112 111 eeAKRI----------------YGETLPLDAAPgaDGRIAYTIRKPIGVIGAI---TPfnfplNLVAHKVGPAIAAGNTV 171
Cdd:PRK00197 74 --EARIegiaeglrqvaalpdpVGEVLDGWTLP--NGLRIGRVRVPLGVIGVIyesRP-----NVTVDAAALCLKSGNAV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446639112 172 VLKPADQTPLSSYALVELF----EEAGLPNGALNIISGPG-STVGEAIVKNDYV 220
Cdd:PRK00197 145 ILRGGSEAIHSNRALVAVIqealEEAGLPADAVQLVETTDrAAVGELLKLDGYV 198
|
|
| |
