|
Name |
Accession |
Description |
Interval |
E-value |
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
2-473 |
0e+00 |
|
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.
Pssm-ID: 132417 Cd Length: 472 Bit Score: 1001.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 2 QHKLLINGELVSGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVF 81
Cdd:TIGR03374 1 QHKLLINGELVSGEGEKQPVYNPATGEVILEIAEASAEQVDAAVRAADAAFAEWGQTTPKARAECLLKLADVIEENAQVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 82 AELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAP 161
Cdd:TIGR03374 81 AELESRNCGKPLHSVFNDEIPAIVDVFRFFAGAARCLSGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 162 ALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIK 241
Cdd:TIGR03374 161 ALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVVNILFGRGKTVGDPLTGHEKVRMVSLTGSIATGEHILSHTAPSIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 242 RTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGP 321
Cdd:TIGR03374 241 RTHMELGGKAPVIVFDDADIDAVVEGVRTFGFYNAGQDCTAACRIYAQRGIYDTLVEKLGAAVATLKSGAPDDESTELGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 322 LSSLAHLERVSKAVEEAKATGHIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWAND 401
Cdd:TIGR03374 321 LSSLAHLERVMKAVEEAKALGHIKVITGGEKRKGNGYYFAPTLLAGAKQDDAIVQKEVFGPVVSITSFDDEEQVVNWAND 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430616178 402 SQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMVK 473
Cdd:TIGR03374 401 SQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHIMVK 472
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
1-474 |
0e+00 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 958.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 1 MQHKLLINGELVSGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQV 80
Cdd:PRK13473 1 MQTKLLINGELVAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 81 FAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLA 160
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 161 PALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSI 240
Cdd:PRK13473 161 PALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 241 KRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELG 320
Cdd:PRK13473 241 KRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 321 PLSSLAHLERVSKAVEEAKATGHIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWAN 400
Cdd:PRK13473 321 PLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWAN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430616178 401 DSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMVKH 474
Cdd:PRK13473 401 DSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKH 474
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
21-472 |
0e+00 |
|
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: 788.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 21 VYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDE 100
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 101 IPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLT 180
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 181 ALKLAELAKDIFPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDAD 260
Cdd:cd07092 161 TLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 261 IEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEAKA 340
Cdd:cd07092 241 LDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 341 tgHIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHR 420
Cdd:cd07092 321 --HARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1430616178 421 VSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07092 399 LSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
2-474 |
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: 591.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 2 QHKLLINGELV-SGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQV 80
Cdd:COG1012 5 EYPLFIGGEWVaAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 81 FAELESRNCGKPLHSAFnDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLA 160
Cdd:COG1012 85 LAALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 161 PALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASS 239
Cdd:COG1012 164 PALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 240 IKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTEL 319
Cdd:COG1012 244 LKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 320 GPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKG-NGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNW 398
Cdd:COG1012 324 GPLISEAQLERVLAYIEDAVAEG-AELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIAL 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430616178 399 ANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFM-LVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMVKH 474
Cdd:COG1012 403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
12-470 |
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: 585.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 12 VSGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGK 91
Cdd:pfam00171 2 VDSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 92 PLHSAFnDEIPAIVDVFRFFAGAARCLNGLAAGEYlEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVL 171
Cdd:pfam00171 82 PLAEAR-GEVDRAIDVLRYYAGLARRLDGETLPSD-PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 172 KPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGK 250
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 251 APVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLER 330
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 331 VSKAVEEAKATGHiKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSV 410
Cdd:pfam00171 320 VLKYVEDAKEEGA-KLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430616178 411 WTKDVGRAHRVSARLQYGCTWVNTHFMLVSEM-PHGGQKLSGYGKDMSLYGLEDYTVVRHV 470
Cdd:pfam00171 399 FTSDLERALRVARRLEAGMVWINDYTTGDADGlPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
54-472 |
0e+00 |
|
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: 533.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 54 EWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAfNDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSM 133
Cdd:cd07078 13 AWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEA-LGEVARAADTFRYYAGLARRLHGEVIPSPDPGELAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 134 IRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLT 212
Cdd:cd07078 92 VRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLNVVTGDGDEVGAALA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 213 GHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGI 292
Cdd:cd07078 172 SHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 293 YDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKG-NGYYYAPTLLAGALQD 371
Cdd:cd07078 252 YDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEG-AKLLCGGKRLEGgKGYFVPPTVLTDVDPD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 372 DTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVS-EMPHGGQKLS 450
Cdd:cd07078 331 MPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEpSAPFGGVKQS 410
|
410 420
....*....|....*....|..
gi 1430616178 451 GYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07078 411 GIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
21-472 |
2.83e-175 |
|
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: 499.38 E-value: 2.83e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 21 VYNPATGDVLLEIAEASAEQVDAAVRAADA--AFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLhSAFN 98
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAafEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLI-RETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 99 DEIPAIVDVFRFFAGAARCLNG----LAAGEYLeghtSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPS 174
Cdd:cd07114 80 AQVRYLAEWYRYYAGLADKIEGavipVDKGDYL----NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 175 EITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPV 253
Cdd:cd07114 156 EHTPASTLELAKLAEEAgFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 254 IVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSK 333
Cdd:cd07114 236 IVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 334 AVEEAKATGHiKVITGGEKRKG----NGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASS 409
Cdd:cd07114 316 YVARAREEGA-RVLTGGERPSGadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430616178 410 VWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07114 395 IWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
21-472 |
3.71e-174 |
|
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: 496.70 E-value: 3.71e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 21 VYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDE 100
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 101 IPAIVDVFRFFAGAARCLNGLAAgEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLT 180
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESY-PQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 181 ALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDA 259
Cdd:cd07093 160 AWLLAELANEAgLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 260 DIEAVVEGVrTFGYY-NAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEA 338
Cdd:cd07093 240 DLDRAVDAA-VRSSFsNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 339 KATGHiKVITGG----EKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKD 414
Cdd:cd07093 319 RAEGA-TILTGGgrpeLPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430616178 415 VGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07093 398 LGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
1-470 |
1.70e-173 |
|
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: 495.96 E-value: 1.70e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 1 MQHKLLINGELVSGE-GEKQPVYNPATGDVLLEIAEASAE--QVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEEN 77
Cdd:cd07091 2 QPTGLFINNEFVDSVsGKTFPTINPATEEVICQVAEADEEdvDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 78 GQVFAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGlAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAW 157
Cdd:cd07091 82 RDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQG-KTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 158 KLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHI-ISH 235
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTImEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 236 TASSIKRTHMELGGKAPVIVFDDADIEAVVEGVrTFG-YYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDD 314
Cdd:cd07091 241 AKSNLKKVTLELGGKSPNIVFDDADLDKAVEWA-AFGiFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 315 ESTELGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQ 394
Cdd:cd07091 320 PDTFQGPQVSKAQFDKILSYIESGKKEG-ATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430616178 395 VVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHV 470
Cdd:cd07091 399 VIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
7-470 |
7.03e-168 |
|
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: 481.81 E-value: 7.03e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 7 INGELVSG-EGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAA--FAEWGQTTPKVRAECLLKLADVIEENGQVFAE 83
Cdd:cd07119 2 IDGEWVEAaSGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 84 LESRNCGKPLHSAFNDeIPAIVDVFRFFAGaarclngLAAGEYLEGHT------SMIRRDPLGVVASIAPWNYPLMMAAW 157
Cdd:cd07119 82 LETLNTGKTLRESEID-IDDVANCFRYYAG-------LATKETGEVYDvpphviSRTVREPVGVCGLITPWNYPLLQAAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 158 KLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHT 236
Cdd:cd07119 154 KLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 237 ASSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDES 316
Cdd:cd07119 234 AGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDAD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 317 TELGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKGN----GYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNE 392
Cdd:cd07119 314 TEMGPLVSAEHREKVLSYIQLGKEEG-ARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430616178 393 EQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHV 470
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
21-470 |
1.06e-165 |
|
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: 475.00 E-value: 1.06e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 21 VYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFnDE 100
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-GE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 101 IPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLT 180
Cdd:cd07103 80 VDYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 181 ALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDA 259
Cdd:cd07103 160 ALALAELAEEAgLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 260 DIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEAK 339
Cdd:cd07103 240 DLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 340 ATGhIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAH 419
Cdd:cd07103 320 AKG-AKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1430616178 420 RVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHV 470
Cdd:cd07103 399 RVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
21-472 |
4.81e-159 |
|
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: 457.76 E-value: 4.81e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 21 VYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAfNDE 100
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 101 IPAIVDVFRFFAGAARclnglaAGEYL---EGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEIT 177
Cdd:cd07106 80 VGGAVAWLRYTASLDL------PDEVIeddDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 178 PLTALKLAELAKDIFPAGVINVLFGrGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFD 257
Cdd:cd07106 154 PLCTLKLGELAQEVLPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 258 DADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEE 337
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 338 AKATGHiKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGR 417
Cdd:cd07106 313 AKAKGA-KVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1430616178 418 AHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
23-472 |
2.84e-155 |
|
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: 448.81 E-value: 2.84e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 23 NPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDEIP 102
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 103 AIVDVFRFFAGAARCLNGLA---AGEYLeghtSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPL 179
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVipvRGPFL----NYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 180 TALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDD 258
Cdd:cd07115 159 SALRIAELMAEAgFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 259 ADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEA 338
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 339 KATGHiKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRA 418
Cdd:cd07115 319 REEGA-RLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1430616178 419 HRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07115 398 HRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
7-465 |
3.51e-153 |
|
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: 443.63 E-value: 3.51e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 7 INGELVSGE-GEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELE 85
Cdd:cd07088 2 INGEFVPSSsGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 86 SRNCGKPLHSAFNdEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAA 165
Cdd:cd07088 82 VEEQGKTLSLARV-EVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 166 GNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTH 244
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 245 MELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSS 324
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 325 LAHLERVSKAVEEAKATGhIKVITGGEKRK-GNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQ 403
Cdd:cd07088 321 EAALDKVEEMVERAVEAG-ATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSE 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430616178 404 YGLASSVWTKDVGRAHRVSARLQYGCTWVN-THFMLVSEMpHGGQKLSGYGKDMSLYGLEDYT 465
Cdd:cd07088 400 YGLTSYIYTENLNTAMRATNELEFGETYINrENFEAMQGF-HAGWKKSGLGGADGKHGLEEYL 461
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
16-465 |
7.99e-153 |
|
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: 442.81 E-value: 7.99e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 16 GEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAA--FAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPL 93
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 94 HSAFNDEIPAIVDVFRFFAGAA-RCLNGLAAGEylEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLK 172
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIdKVYGEVAPTG--PDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 173 PSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTA-SSIKRTHMELGGK 250
Cdd:cd07112 159 PAEQSPLTALRLAELALEAgLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqSNLKRVWLECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 251 APVIVFDDA-DIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLE 329
Cdd:cd07112 239 SPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 330 RVSKAVEEAKATGhIKVITGGEK--RKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLA 407
Cdd:cd07112 319 KVLGYIESGKAEG-ARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430616178 408 SSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYT 465
Cdd:cd07112 398 ASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
3-472 |
1.39e-150 |
|
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: 437.55 E-value: 1.39e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 3 HKLLINGELVSGE-GEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVF 81
Cdd:cd07559 1 YDNFINGEWVAPSkGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 82 AELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGlAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAP 161
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEG-SLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 162 ALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIK 241
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 242 RTHMELGGKAPVIVFDDA-----DIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDES 316
Cdd:cd07559 240 PVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 317 TELGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKGN----GYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNE 392
Cdd:cd07559 320 TMMGAQVSKDQLEKILSYVDIGKEEG-AEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 393 EQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07559 399 EEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILV 478
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
54-472 |
3.99e-149 |
|
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: 429.73 E-value: 3.99e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 54 EWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLhSAFNDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSM 133
Cdd:cd06534 9 AWAALPPAERAAILRKIADLLEERREELAALETLETGKPI-EEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGEAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 134 IRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLT 212
Cdd:cd06534 88 VRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGGGDEVGAALL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 213 GHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGI 292
Cdd:cd06534 168 SHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 293 YDTLVEKLGaavatlksgapddestelgplsslahlervskaveeakatghikvitggekrkgngyyyapTLLAGALQDD 372
Cdd:cd06534 248 YDEFVEKLV-------------------------------------------------------------TVLVDVDPDM 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 373 TIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVS-EMPHGGQKLSG 451
Cdd:cd06534 267 PIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGpEAPFGGVKNSG 346
|
410 420
....*....|....*....|.
gi 1430616178 452 YGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd06534 347 IGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
21-472 |
5.90e-148 |
|
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: 430.19 E-value: 5.90e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 21 VYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDe 100
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 101 IPAIVDVFRFFAGAARCLNG----LAAGEYleGHTsmiRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEI 176
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGehvpLPGGSF--AYT---RREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 177 TPLTALKLAELAKDI-FPAGVINVLFGRGKTvGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIV 255
Cdd:cd07090 155 TPLTALLLAEILTEAgLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 256 FDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAV 335
Cdd:cd07090 234 FDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 336 EEAKATGhIKVITGGEKRKG-----NGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSV 410
Cdd:cd07090 314 ESAKQEG-AKVLCGGERVVPedgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430616178 411 WTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07090 393 FTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
7-468 |
1.31e-147 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 429.61 E-value: 1.31e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 7 INGELVSGE-GEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELE 85
Cdd:TIGR01804 2 IDGEYVEDSaGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 86 SRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGlaagEYLE---GHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPA 162
Cdd:TIGR01804 82 TLDTGKTLQETIVADMDSGADVFEFFAGLAPALNG----EIIPlggPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 163 LAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIK 241
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 242 RTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGP 321
Cdd:TIGR01804 238 HVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 322 LSSLAHLERVSKAVEEAKATGhIKVITGGEKRK----GNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVN 397
Cdd:TIGR01804 318 LISAAHRDKVLSYIEKGKAEG-ATLATGGGRPEnvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430616178 398 WANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVR 468
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
4-472 |
2.53e-147 |
|
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: 429.52 E-value: 2.53e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 4 KLLINGELV-SGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAA-FAEWGQTTPKVRAECLLKLADVIEENGQVF 81
Cdd:cd07144 9 GLFINNEFVkSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 82 AELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRrDPLGVVASIAPWNYPLMMAAWKLAP 161
Cdd:cd07144 89 AAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLH-EPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 162 ALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSI 240
Cdd:cd07144 168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 241 KRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVA-TLKSGAPDDESTEL 319
Cdd:cd07144 248 KAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 320 GPLSSLAHLERVSKAVEEAKATGHiKVITGGEKRK---GNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVV 396
Cdd:cd07144 328 GPQVSKTQYDRVLSYIEKGKKEGA-KLVYGGEKAPeglGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAI 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430616178 397 NWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07144 407 KKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
3-472 |
3.12e-146 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 426.99 E-value: 3.12e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 3 HKLLINGELVSGE-GEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVF 81
Cdd:PRK13252 7 QSLYIDGAYVEATsGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 82 AELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNG----LAAGEYLegHTsmiRRDPLGVVASIAPWNYPLMMAAW 157
Cdd:PRK13252 87 AALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGeqipLRGGSFV--YT---RREPLGVCAGIGAWNYPIQIACW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 158 KLAPALAAGNCVVLKPSEITPLTALKLAElakdIF-----PAGVINVLFGRGKtVGDPLTGHPKVRMVSLTGSIATGEHI 232
Cdd:PRK13252 162 KSAPALAAGNAMIFKPSEVTPLTALKLAE----IYteaglPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 233 ISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAP 312
Cdd:PRK13252 237 MAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 313 DDESTELGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRK----GNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTP 388
Cdd:PRK13252 317 MDPATNFGPLVSFAHRDKVLGYIEKGKAEG-ARLLCGGERLTeggfANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 389 FDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVR 468
Cdd:PRK13252 396 FDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIK 475
|
....
gi 1430616178 469 HVMV 472
Cdd:PRK13252 476 SVQV 479
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
7-474 |
1.22e-145 |
|
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: 424.93 E-value: 1.22e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 7 INGELVSGEGEKQP-VYNPATGDVLLEIAEASAEQVDAAVRAADAA-FAEWGQTTPKVRAECLLKLADVIEENGQVFAEL 84
Cdd:cd07113 4 IDGRPVAGQSEKRLdITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 85 ESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNG--------LAAGEYlegHTSMIRRDPLGVVASIAPWNYPLMMAA 156
Cdd:cd07113 84 ETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGetlapsipSMQGER---YTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 157 WKLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKtVGDPLTGHPKVRMVSLTGSIATGEHIISH 235
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 236 TASSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDE 315
Cdd:cd07113 240 AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 316 STELGPLSSLAHLERVSKAVEEAKATGHiKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQV 395
Cdd:cd07113 320 SVMFGPLANQPHFDKVCSYLDDARAEGD-EIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430616178 396 VNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMVKH 474
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIRY 477
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
21-471 |
8.81e-145 |
|
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: 422.14 E-value: 8.81e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 21 VYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDe 100
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 101 ipaIVDV---FRFFAGAARCLNGLAAGEY---LEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPS 174
Cdd:cd07110 80 ---VDDVagcFEYYADLAEQLDAKAERAVplpSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 175 EITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPV 253
Cdd:cd07110 157 ELTSLTELELAEIAAEAgLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 254 IVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSK 333
Cdd:cd07110 237 IVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 334 AVEEAKATGhIKVITGGEKRK--GNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVW 411
Cdd:cd07110 317 FIARGKEEG-ARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 412 TKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVM 471
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
3-472 |
9.80e-141 |
|
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: 412.23 E-value: 9.80e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 3 HKLLINGELVSGE-GEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVF 81
Cdd:cd07117 1 YGLFINGEWVKGSsGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 82 AELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGlAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAP 161
Cdd:cd07117 81 AMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEG-SANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 162 ALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIK 241
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 242 RTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGP 321
Cdd:cd07117 240 PATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 322 LSSLAHLERVSKAVEEAKATGhIKVITGGEKRKGN----GYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVN 397
Cdd:cd07117 320 QVNKDQLDKILSYVDIAKEEG-AKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVID 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430616178 398 WANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07117 399 MANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
4-474 |
4.64e-139 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 408.43 E-value: 4.64e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 4 KLLINGELVSGE-GEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFA 82
Cdd:TIGR02299 2 GHFIDGEFVPSEsGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKRWAELKAAERKRYLHKIADLIEQHADEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 83 ELESRNCGKPLhSAFNDEIPAIVDVFRFFAG-AARCLNGLAAgeYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAP 161
Cdd:TIGR02299 82 VLECLDCGQPL-RQTRQQVIRAAENFRFFADkCEEAMDGRTY--PVDTHLNYTVRVPVGPVGLITPWNAPFMLSTWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 162 ALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSI 240
Cdd:TIGR02299 159 ALAFGNTVVLKPAEWSPLTAARLAEIAKEAgLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMRNGADTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 241 KRTHMELGGKAPVIVFDDADIEAVVEGVrTFGYY-NAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTEL 319
Cdd:TIGR02299 239 KRFSMELGGKSPVIVFDDADLERALDAV-VFMIFsFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPETEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 320 GPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRK-------GNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNE 392
Cdd:TIGR02299 318 GPLIHPEHLAKVLGYVEAAEKEG-ATILVGGERAPtfrgedlGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFKDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 393 EQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:TIGR02299 397 EEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNVAL 476
|
..
gi 1430616178 473 KH 474
Cdd:TIGR02299 477 AL 478
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
21-472 |
1.51e-137 |
|
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: 403.66 E-value: 1.51e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 21 VYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDE 100
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 101 IPAIVDVFRFFAGAArclnGLAAGEYL---EGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEIT 177
Cdd:cd07108 81 AAVLADLFRYFGGLA----GELKGETLpfgPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 178 PLTALKLAELAKDIFPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFD 257
Cdd:cd07108 157 PLAVLLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 258 DADIEAVVEGVRT-FGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVE 336
Cdd:cd07108 237 DADLDDAVDGAIAgMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 337 EAKATGHIKVITGGEKRK----GNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWT 412
Cdd:cd07108 317 LGLSTSGATVLRGGPLPGegplADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430616178 413 KDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYG-LEDYTVVRHVMV 472
Cdd:cd07108 397 RDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTVNI 457
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
5-473 |
4.40e-136 |
|
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: 400.75 E-value: 4.40e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 5 LLINGELVSG-EGEKQPVYNPATGDVLLEIAEAS-AEQVDAAVRAADAAFAEWG-QTTPKVRAECLLKLADVIEENGQVF 81
Cdd:cd07143 9 LFINGEFVDSvHGGTVKVYNPSTGKLITKIAEATeADVDIAVEVAHAAFETDWGlKVSGSKRGRCLSKLADLMERNLDYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 82 AELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGLAAgEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAP 161
Cdd:cd07143 89 ASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVI-ETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 162 ALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASS- 239
Cdd:cd07143 168 ALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSn 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 240 IKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTEL 319
Cdd:cd07143 248 LKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 320 GPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWA 399
Cdd:cd07143 328 GPQVSQIQYERIMSYIESGKAEG-ATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRA 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430616178 400 NDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMVK 473
Cdd:cd07143 407 NDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
21-472 |
1.84e-135 |
|
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: 398.15 E-value: 1.84e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 21 VYNPATGDVLLEIAEASAEQVDAAVRAADAAFAE-WGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFND 99
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 100 eIPAIVDVFRFFAGAARCLNGLAAgEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPL 179
Cdd:cd07109 81 -VEAAARYFEYYGGAADKLHGETI-PLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 180 TALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDD 258
Cdd:cd07109 159 TALRLAELAEEAgLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 259 ADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDEsTELGPLSSLAHLERVSKAVEEA 338
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLED-PDLGPLISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 339 KATGhIKVITGG---EKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDV 415
Cdd:cd07109 318 RARG-ARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430616178 416 GRAHRVSARLQYGCTWVNTHFMLVS-EMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
21-470 |
2.33e-135 |
|
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: 398.15 E-value: 2.33e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 21 VYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWG-QTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFND 99
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 100 EIPAIVDVFRFFAGAARCL----NGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSE 175
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFpwefDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 176 ITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVI 254
Cdd:cd07089 161 DTPLSALLLGEIIAETdLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 255 VFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKA 334
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 335 VEEAKATGhIKVITGGEKRKG--NGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWT 412
Cdd:cd07089 321 IARGRDEG-ARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWS 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430616178 413 KDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHV 470
Cdd:cd07089 400 ADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
5-470 |
7.26e-134 |
|
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: 394.56 E-value: 7.26e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 5 LLINGELVSGEG-EKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAE 83
Cdd:cd07138 1 FYIDGAWVAPAGtETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 84 LESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARclnGLAAGEYLEGhtSMIRRDPLGVVASIAPWNYPLMMAAWKLAPAL 163
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALK---DFEFEERRGN--SLVVREPIGVCGLITPWNWPLNQIVLKVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 164 AAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKR 242
Cdd:cd07138 156 AAGCTVVLKPSEVAPLSAIILAEILDEAgLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 243 THMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPL 322
Cdd:cd07138 236 VALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 323 SSLAHLERV----SKAVEEAkATghikVITGGEKR-KG--NGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQV 395
Cdd:cd07138 316 ASAAQFDRVqgyiQKGIEEG-AR----LVAGGPGRpEGleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430616178 396 VNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNtHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHV 470
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
3-473 |
2.80e-131 |
|
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: 388.63 E-value: 2.80e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 3 HKLLINGELV-SGEGEKQPVYNPATGDVLLEIAE---ASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENG 78
Cdd:cd07141 7 TKIFINNEWHdSVSGKTFPTINPATGEKICEVQEgdkADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 79 QVFAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGL---AAGEYLeghtSMIRRDPLGVVASIAPWNYPLMMA 155
Cdd:cd07141 87 AYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKtipMDGDFF----TYTRHEPVGVCGQIIPWNFPLLMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 156 AWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGeHIIS 234
Cdd:cd07141 163 AWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVG-KLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 235 HTA--SSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAP 312
Cdd:cd07141 242 QAAgkSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 313 DDESTELGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNE 392
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIESGKKEG-AKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 393 EQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
gi 1430616178 473 K 473
Cdd:cd07141 481 K 481
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
21-472 |
4.71e-130 |
|
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: 384.42 E-value: 4.71e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 21 VYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLhSAFNDE 100
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPV-SAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 101 IPAIVDVFRFFAGAARCLNGlAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLT 180
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKG-ETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 181 ALKLAELAKDIFPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDAD 260
Cdd:cd07107 159 ALRLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 261 IEAVVEG-VRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEAK 339
Cdd:cd07107 239 PEAAADAaVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 340 ATGhIKVITGGEKRKG----NGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDV 415
Cdd:cd07107 319 REG-ARLVTGGGRPEGpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 416 GRAHRVSARLQYGCTWVN---THFMLVsemPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07107 398 SQAHRTARRVEAGYVWINgssRHFLGA---PFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
3-472 |
1.00e-129 |
|
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: 384.29 E-value: 1.00e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 3 HKLLINGELVSGeGEKQPVYNPA-TGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVF 81
Cdd:cd07097 1 YRNYIDGEWVAG-GDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 82 AELESRNCGKPLHSAfNDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAP 161
Cdd:cd07097 80 ARLLTREEGKTLPEA-RGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 162 ALAAGNCVVLKPSEITPLTALKLAE-LAKDIFPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSI 240
Cdd:cd07097 159 ALAYGNTVVFKPAELTPASAWALVEiLEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 241 KRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELG 320
Cdd:cd07097 239 ARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 321 PLSSLAHLERVSKAVEEAKATGHiKVITGGE--KRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNW 398
Cdd:cd07097 319 PVVSERQLEKDLRYIEIARSEGA-KLVYGGErlKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 399 ANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVN-----THFMLvsemPHGGQKLSGYG-KDMSLYGLEDYTVVRHVMV 472
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlptagVDYHV----PFGGRKGSSYGpREQGEAALEFYTTIKTVYV 473
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
5-470 |
5.43e-129 |
|
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: 382.31 E-value: 5.43e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 5 LLINGELV-SGEGEKQPVYNPATGDVLLEIAEASAE--QVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVF 81
Cdd:cd07139 1 LFIGGRWVaPSGSETIDVVSPATEEVVGRVPEATPAdvDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 82 AELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAP 161
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 162 ALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGrGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSI 240
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 241 KRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELG 320
Cdd:cd07139 240 ARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 321 PLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKG--NGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNW 398
Cdd:cd07139 320 PLASARQRERVEGYIAKGRAEG-ARLVTGGGRPAGldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430616178 399 ANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNtHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHV 470
Cdd:cd07139 399 ANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
19-465 |
4.77e-128 |
|
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: 379.25 E-value: 4.77e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 19 QPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFN 98
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 99 dEIPAIVDVFRFFAGAARCLNG----LAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPS 174
Cdd:cd07149 81 -EVDRAIETLRLSAEEAKRLAGetipFDASPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 175 EITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIIShtASSIKRTHMELGGKAPV 253
Cdd:cd07149 160 SQTPLSALKLAELLLEAgLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIAR--KAGLKKVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 254 IVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSK 333
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 334 AVEEAKATGhIKVITGGEKrkgNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTK 413
Cdd:cd07149 318 WVEEAVEGG-ARLLTGGKR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTN 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1430616178 414 DVGRAHRVSARLQYGCTWVN-THFMLVSEMPHGGQKLSGYGKDMSLYGLEDYT 465
Cdd:cd07149 394 DLQKALKAARELEVGGVMINdSSTFRVDHMPYGGVKESGTGREGPRYAIEEMT 446
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
4-470 |
5.21e-128 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 381.00 E-value: 5.21e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 4 KLLINGELVSG-EGEKQPVYNPATGDVLLEIAEASAEQVDAAVRA-----ADAAFAEWGQTTPKVRAECLLKLADVIEEN 77
Cdd:PLN02467 9 QLFIGGEWREPvLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAarkafKRNKGKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 78 GQVFAELESRNCGKPLHSAFNDeipaIVDV---FRFFAGAARCLNGLAAGEY---LEGHTSMIRRDPLGVVASIAPWNYP 151
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWD----MDDVagcFEYYADLAEALDAKQKAPVslpMETFKGYVLKEPLGVVGLITPWNYP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 152 LMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGE 230
Cdd:PLN02467 165 LLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVgLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 231 HIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVrTFG-YYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKS 309
Cdd:PLN02467 245 KIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWA-MFGcFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 310 GAPDDESTELGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKG--NGYYYAPTLLAGALQDDTIVQKEVFGPVVSVT 387
Cdd:PLN02467 324 SDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEG-ATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 388 PFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVV 467
Cdd:PLN02467 403 TFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSV 482
|
...
gi 1430616178 468 RHV 470
Cdd:PLN02467 483 KQV 485
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
6-470 |
5.13e-127 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 378.26 E-value: 5.13e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 6 LINGELV-SGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAEL 84
Cdd:PLN02278 28 LIGGKWTdAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 85 ESRNCGKPLHSAFNDEIPAIVDVfRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALA 164
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFL-EYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 165 AGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRT 243
Cdd:PLN02278 187 AGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 244 HMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLS 323
Cdd:PLN02278 267 SLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 324 SLAHLERVSKAVEEAKATGhIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQ 403
Cdd:PLN02278 347 NEAAVQKVESHVQDAVSKG-AKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTE 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430616178 404 YGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHV 470
Cdd:PLN02278 426 AGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
24-472 |
1.35e-126 |
|
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: 375.52 E-value: 1.35e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 24 PATGDVLLEIAEASAE--QVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNdEI 101
Cdd:cd07118 4 PAHGVVVARYAEGTVEdvDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 102 PAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTA 181
Cdd:cd07118 83 EGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 182 LKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDAD 260
Cdd:cd07118 163 LMLAELLIEAgLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 261 IEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEAKA 340
Cdd:cd07118 243 LDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 341 TGhIKVITGGEK-RKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAH 419
Cdd:cd07118 323 EG-ATLLLGGERlASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1430616178 420 RVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07118 402 TVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
4-470 |
4.19e-126 |
|
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: 374.91 E-value: 4.19e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 4 KLLINGELV-SGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAE--WGQTTPKVRAECLLKLADVIEENGQV 80
Cdd:cd07142 5 KLFINGQFVdAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 81 FAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGL---AAGEYlEGHTsmiRRDPLGVVASIAPWNYPLMMAAW 157
Cdd:cd07142 85 LAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMtlpADGPH-HVYT---LHEPIGVVGQIIPWNFPLLMFAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 158 KLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHT 236
Cdd:cd07142 161 KVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 237 A-SSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDE 315
Cdd:cd07142 241 AkSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 316 STELGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQV 395
Cdd:cd07142 321 GVEQGPQVDKEQFEKILSYIEHGKEEG-ATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430616178 396 VNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHV 470
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
5-466 |
1.16e-125 |
|
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: 374.04 E-value: 1.16e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 5 LLINGELVSGEGEKQ-PVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAE 83
Cdd:cd07111 24 HFINGKWVKPENRKSfPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 84 LESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNglaageyleghTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPAL 163
Cdd:cd07111 104 LESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLD-----------TELAGWKPVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 164 AAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTvGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKR 242
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAGTGKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 243 THMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPL 322
Cdd:cd07111 252 LSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 323 SSLAHLERVSKAVEEAKATGHIKVITGGEKRKgNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDS 402
Cdd:cd07111 332 VDPAQLKRIRELVEEGRAEGADVFQPGADLPS-KGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNT 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430616178 403 QYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTV 466
Cdd:cd07111 411 PYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLR 474
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
20-465 |
6.35e-123 |
|
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: 366.29 E-value: 6.35e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 20 PVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAfND 99
Cdd:cd07145 2 EVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS-RV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 100 EIPAIVDVFRFFAGAARCLNG----LAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSE 175
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGetipVDAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 176 ITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVI 254
Cdd:cd07145 161 NTPLTAIELAKILEEAgLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 255 VFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKA 334
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 335 VEEAKATGHiKVITGGEKRKgnGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKD 414
Cdd:cd07145 321 VNDAVEKGG-KILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTND 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1430616178 415 VGRAHRVSARLQYGCTWVN--THFMLVSeMPHGGQKLSGYGKDMSLYGLEDYT 465
Cdd:cd07145 398 INRALKVARELEAGGVVINdsTRFRWDN-LPFGGFKKSGIGREGVRYTMLEMT 449
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
20-472 |
3.02e-121 |
|
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: 361.65 E-value: 3.02e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 20 PVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNd 99
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 100 EIPAIVDVFRFFAGAARclngLAAGEYL----EGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSE 175
Cdd:cd07150 81 ETTFTPELLRAAAGECR----RVRGETLpsdsPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 176 ITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVI 254
Cdd:cd07150 157 ETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 255 VFDDADIEAVVEgVRTFG-YYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSK 333
Cdd:cd07150 237 VLADADLDYAVR-AAAFGaFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 334 AVEEAKATGhIKVITGGekrKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTK 413
Cdd:cd07150 316 QVEDAVAKG-AKLLTGG---KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 414 DVGRAHRVSARLQYGCTWVN-THFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07150 392 DLQRAFKLAERLESGMVHINdPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
1-474 |
3.85e-120 |
|
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: 360.27 E-value: 3.85e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 1 MQHKLLINGELVSGEGEKQ-PVYNPATGDVLLEIAEASAEQVDAAVRAADAA--FAEWGQTTPKVRAECLLKLADVIEEN 77
Cdd:cd07140 4 MPHQLFINGEFVDAEGGKTyNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 78 GQVFAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGLA---AGEYLEGHTSMIRRDPLGVVASIAPWNYPLMM 154
Cdd:cd07140 84 QEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTipiNQARPNRNLTLTKREPIGVCGIVIPWNYPLMM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 155 AAWKLAPALAAGNCVVLKPSEITPLTALKLAEL-AKDIFPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHII 233
Cdd:cd07140 164 LAWKMAACLAAGNTVVLKPAQVTPLTALKFAELtVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 234 SHTA-SSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAP 312
Cdd:cd07140 244 KSCAvSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 313 DDESTELGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNE 392
Cdd:cd07140 324 LDRSTDHGPQNHKAHLDKLVEYCERGVKEG-ATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 393 --EQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHV 470
Cdd:cd07140 403 dvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
....
gi 1430616178 471 MVKH 474
Cdd:cd07140 483 TIEY 486
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
22-470 |
1.90e-118 |
|
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: 354.73 E-value: 1.90e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 22 YNPATGDVLLEIAEASAE--QVDAAVRAADAAFAEWGQTtPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAfND 99
Cdd:cd07120 2 IDPATGEVIGTYADGGVAeaEAAIAAARRAFDETDWAHD-PRLRARVLLELADAFEANAERLARLLALENGKILGEA-RF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 100 EIPAIVDVFRFFAGAARCLNGlAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPL 179
Cdd:cd07120 80 EISGAISELRYYAGLARTEAG-RMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 180 TALKLAELAKDI--FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFD 257
Cdd:cd07120 159 INAAIIRILAEIpsLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 258 DADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEE 337
Cdd:cd07120 239 DADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVER 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 338 AKATGhIKVITGGEK---RKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKD 414
Cdd:cd07120 319 AIAAG-AEVVLRGGPvteGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430616178 415 VGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHV 470
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
54-472 |
6.99e-118 |
|
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: 352.22 E-value: 6.99e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 54 EWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAfNDEIPAIVDVFRFFAGAARclngLAAGEYL----EG 129
Cdd:cd07104 15 AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKA-AFEVGAAIAILREAAGLPR----RPEGEILpsdvPG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 130 HTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLT-ALKLAELAKDI-FPAGVINVLFGRGKTV 207
Cdd:cd07104 90 KESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAgLPKGVLNVVPGGGSEI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 208 GDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEgVRTFG-YYNAGQDCTAACRI 286
Cdd:cd07104 170 GDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVS-AAAFGaFLHQGQICMAAGRI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 287 YAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEAKATGhIKVITGGekrKGNGYYYAPTLLA 366
Cdd:cd07104 249 LVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAG-ARLLTGG---TYEGLFYQPTVLS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 367 GALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFML-VSEMPHG 445
Cdd:cd07104 325 DVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNdEPHVPFG 404
|
410 420
....*....|....*....|....*..
gi 1430616178 446 GQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07104 405 GVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
7-474 |
3.18e-117 |
|
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: 352.52 E-value: 3.18e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 7 INGELVSG-EGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELE 85
Cdd:cd07116 5 IGGEWVAPvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 86 SRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGlAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAA 165
Cdd:cd07116 85 TWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEG-SISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 166 GNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHM 245
Cdd:cd07116 164 GNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 246 ELGGKAPVIVF------DDADIEAVVEGVRTFGyYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTEL 319
Cdd:cd07116 244 ELGGKSPNIFFadvmdaDDAFFDKALEGFVMFA-LNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 320 GPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRK----GNGYYYAPTLLAGAlQDDTIVQKEVFGPVVSVTPFDNEEQV 395
Cdd:cd07116 323 GAQASLEQLEKILSYIDIGKEEG-AEVLTGGERNElgglLGGGYYVPTTFKGG-NKMRIFQEEIFGPVLAVTTFKDEEEA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430616178 396 VNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMVKH 474
Cdd:cd07116 401 LEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLVSY 479
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
4-471 |
4.92e-117 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 352.59 E-value: 4.92e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 4 KLLINGELV-SGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAA--FAEWGQTTPKVRAECLLKLADVIEENGQV 80
Cdd:PLN02766 22 KLFINGEFVdAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 81 FAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNG--LAAGEYLEGHTsmiRRDPLGVVASIAPWNYPLMMAAWK 158
Cdd:PLN02766 102 LAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGetLKMSRQLQGYT---LKEPIGVVGHIIPWNFPSTMFFMK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 159 LAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTA 237
Cdd:PLN02766 179 VAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 238 -SSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDES 316
Cdd:PLN02766 259 tSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 317 TELGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVV 396
Cdd:PLN02766 339 ARQGPQVDKQQFEKILSYIEHGKREG-ATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAI 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430616178 397 NWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVM 471
Cdd:PLN02766 418 KKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVV 492
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
22-472 |
8.15e-116 |
|
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: 348.06 E-value: 8.15e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 22 YNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNdEI 101
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL-EV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 102 PAIVDVFRFFAG-AARCL--NGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITP 178
Cdd:cd07099 80 LLALEAIDWAARnAPRVLapRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 179 LTALKLAELAKDI-FPAGVINVLFGRGKTvGDPLTGHpKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFD 257
Cdd:cd07099 160 LVGELLAEAWAAAgPPQGVLQVVTGDGAT-GAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 258 DADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEE 337
Cdd:cd07099 238 DADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 338 AKATGhIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGR 417
Cdd:cd07099 318 AVAKG-AKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1430616178 418 AHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07099 397 AEAIARRLEAGAVSINDVLLtaGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
6-453 |
5.88e-115 |
|
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: 346.64 E-value: 5.88e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 6 LINGELV-SGEGEKQPVYNPATG-DVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAE 83
Cdd:cd07131 2 YIGGEWVdSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 84 LESRNCGKPLHSAFNDEIPAIvDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPAL 163
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAI-DMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 164 AAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKR 242
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 243 THMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPL 322
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 323 SSLAHLERVSKAVEEAKATGhIKVITGGEKRKGN----GYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNW 398
Cdd:cd07131 321 INEAQLEKVLNYNEIGKEEG-ATLLLGGERLTGGgyekGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430616178 399 ANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVN-------THfmlvseMPHGGQKLSGYG 453
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNaptigaeVH------LPFGGVKKSGNG 455
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
6-453 |
3.27e-114 |
|
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: 344.55 E-value: 3.27e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 6 LINGELVSGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELE 85
Cdd:cd07086 2 VIGGEWVGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 86 SRNCGKPLHSAFNdEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAA 165
Cdd:cd07086 82 SLEMGKILPEGLG-EVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 166 GNCVVLKPSEITPLTALKLAELAKDI-----FPAGVINVLFGRGkTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSI 240
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVlekngLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 241 KRTHMELGGKAPVIVFDDADIEAVVEGVrTFGYY-NAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTEL 319
Cdd:cd07086 240 GRVLLELGGNNAIIVMDDADLDLAVRAV-LFAAVgTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 320 GPLSSLAHLERVSKAVEEAKATGhIKVITGGE--KRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVN 397
Cdd:cd07086 319 GPLINQAAVEKYLNAIEIAKSQG-GTVLTGGKriDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIA 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430616178 398 WANDSQYGLASSVWTKDVGRAHR-VSAR-LQYGCTWVNT-------HfmlvseMPHGGQKLSGYG 453
Cdd:cd07086 398 INNDVPQGLSSSIFTEDLREAFRwLGPKgSDCGIVNVNIptsgaeiG------GAFGGEKETGGG 456
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
54-472 |
3.08e-113 |
|
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: 340.21 E-value: 3.08e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 54 EWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAfNDEIPAIVDVFRFFA--GAArclngLAAGEYLE--G 129
Cdd:cd07100 14 AWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYAenAEA-----FLADEPIEtdA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 130 HTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVG 208
Cdd:cd07100 88 GKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAgFPEGVFQNLLIDSDQVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 209 DpLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYA 288
Cdd:cd07100 168 A-IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 289 QKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKGNGYYYAPTLLAGA 368
Cdd:cd07100 247 HEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAG-ATLLLGGKRPDGPGAFYPPTVLTDV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 369 LQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQK 448
Cdd:cd07100 326 TPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGVK 405
|
410 420
....*....|....*....|....
gi 1430616178 449 LSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07100 406 RSGYGRELGRFGIREFVNIKTVWV 429
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
67-464 |
2.49e-111 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 334.78 E-value: 2.49e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 67 LLKLADVIEENGQVFAELESRNCGKPLHSAfNDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIA 146
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 147 PWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGS 225
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 226 IATGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVA 305
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 306 TLKSGAPDDEST-ELGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVV 384
Cdd:PRK10090 240 AVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEG-ARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 385 SVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDY 464
Cdd:PRK10090 319 PVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEY 398
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
2-453 |
1.47e-110 |
|
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: 334.92 E-value: 1.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 2 QHKLLINGELVSGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTP-KVRAECLLKLADVIEENGQV 80
Cdd:cd07082 1 QFKYLINGEWKESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 81 FAELESRNCGKPLHSAfNDEIPAIVDVFRFFAGAARCLNGlaagEYLEGHTS--------MIRRDPLGVVASIAPWNYPL 152
Cdd:cd07082 81 VANLLMWEIGKTLKDA-LKEVDRTIDYIRDTIEELKRLDG----DSLPGDWFpgtkgkiaQVRREPLGVVLAIGPFNYPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 153 MMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEH 231
Cdd:cd07082 156 NLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 232 IIShtASSIKRTHMELGGKAPVIVFDDADIE-AVVEGVR-TFGYynAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKS 309
Cdd:cd07082 236 LKK--QHPMKRLVLELGGKDPAIVLPDADLElAAKEIVKgALSY--SGQRCTAIKRVLVHESVADELVELLKEEVAKLKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 310 GAPDDESTELGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKGNgyYYAPTLLAGALQDDTIVQKEVFGPVVSVTPF 389
Cdd:cd07082 312 GMPWDNGVDITPLIDPKSADFVEGLIDDAVAKG-ATVLNGGGREGGN--LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRV 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430616178 390 DNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNT-------HFmlvsemPHGGQKLSGYG 453
Cdd:cd07082 389 NDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSkcqrgpdHF------PFLGRKDSGIG 453
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
4-471 |
1.66e-110 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 337.16 E-value: 1.66e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 4 KLLINGELV-SGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAE--WGQTTPKVRAECLLKLADVIEENGQV 80
Cdd:PLN02466 59 QLLINGQFVdAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 81 FAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGL---AAGEylegHTSMIRRDPLGVVASIAPWNYPLMMAAW 157
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLtvpADGP----HHVQTLHEPIGVAGQIIPWNFPLLMFAW 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 158 KLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHT 236
Cdd:PLN02466 215 KVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 237 A-SSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDE 315
Cdd:PLN02466 295 AkSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 316 STELGPLSSLAHLERVSKAVE---EAKATghikVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNE 392
Cdd:PLN02466 375 GVEQGPQIDSEQFEKILRYIKsgvESGAT----LECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDL 450
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430616178 393 EQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVM 471
Cdd:PLN02466 451 DEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
9-474 |
7.63e-109 |
|
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: 330.42 E-value: 7.63e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 9 GELVSGEGEK-QPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESR 87
Cdd:cd07151 1 GEWRDGTSERtIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 88 NCGKPLHSAfNDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGN 167
Cdd:cd07151 81 ESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 168 CVVLKPSEITPLTA-LKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHM 245
Cdd:cd07151 160 AVVLKPASDTPITGgLLLAKIFEEAgLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 246 ELGGKAPVIVFDDADIEAVVEGVrTFG-YYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSS 324
Cdd:cd07151 240 ELGGNNPFVVLEDADIDAAVNAA-VFGkFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLIN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 325 LAHLERVSKAVEEAKATGhIKVITGGEKrkgNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQY 404
Cdd:cd07151 319 ESQVDGLLDKIEQAVEEG-ATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEY 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430616178 405 GLASSVWTKDVGRAHRVSARLQYGCTWVNTHfmLVSEMPH---GGQKLSGYGKDMSLYGLEDYTVVRHVMVKH 474
Cdd:cd07151 395 GLSGAVFTSDLERGVQFARRIDAGMTHINDQ--PVNDEPHvpfGGEKNSGLGRFNGEWALEEFTTDKWISVQH 465
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
5-453 |
1.46e-107 |
|
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: 328.80 E-value: 1.46e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 5 LLINGELVSGEgEKQPVYNPA-TGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAE 83
Cdd:cd07124 35 LVIGGKEVRTE-EKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 84 LESRNCGKPLHSAFNDEIPAIvDVFRFFAGAARCLNGLAAGEYlEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPAL 163
Cdd:cd07124 114 WMVLEVGKNWAEADADVAEAI-DFLEYYAREMLRLRGFPVEMV-PGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 164 AAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASS--- 239
Cdd:cd07124 192 VTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqpg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 240 ---IKRTHMELGGKAPVIVFDDADIEAVVEGV--RTFGYynAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDD 314
Cdd:cd07124 272 qkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIvrSAFGF--QGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPED 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 315 ESTELGPLSSLAHLERVSKAVEEAKATGhiKVITGGEKRKG--NGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNE 392
Cdd:cd07124 350 PEVYMGPVIDKGARDRIRRYIEIGKSEG--RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 393 EQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYG-------CT--WVNTHfmlvsemPHGGQKLSGYG 453
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGnlyanrkITgaLVGRQ-------PFGGFKMSGTG 490
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
21-472 |
4.37e-107 |
|
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: 325.54 E-value: 4.37e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 21 VYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNdE 100
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV-E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 101 IPAIVDVFRFFAGAARCLNG----LAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEI 176
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGeeipLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 177 TPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIisHTASSIKRTHMELGGKAPVIV 255
Cdd:cd07094 162 TPLSALELAKILVEAgVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNAPVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 256 FDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAV 335
Cdd:cd07094 240 DRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 336 EEAKATGHiKVITGGEkRKGNGYYyaPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDV 415
Cdd:cd07094 320 EEAVEAGA-RLLCGGE-RDGALFK--PTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430616178 416 GRAHRVSARLQYGCTWVNTHFMLVSE-MPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDSSAFRTDwMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
1-465 |
2.96e-106 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 324.93 E-value: 2.96e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 1 MQHKLLINGEL-VSGEGEKQPVYNPATGDVLLEIAE-ASAE-QVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEEN 77
Cdd:PRK09847 18 IENRLFINGEYtAAAENETFETVDPVTQAPLAKIARgKSVDiDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 78 GQVFAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGLAAGEYlEGHTSMIRRDPLGVVASIAPWNYPLMMAAW 157
Cdd:PRK09847 98 AEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTS-SHELAMIVREPVGVIAAIVPWNFPLLLTCW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 158 KLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHT 236
Cdd:PRK09847 177 KLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 237 A-SSIKRTHMELGGKAPVIVFDDA-DIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDD 314
Cdd:PRK09847 257 GdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 315 ESTELGPLSSLAHLERVSKAVEEAKATGHIkVITGgeKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQ 394
Cdd:PRK09847 337 PATTMGTLIDCAHADSVHSFIREGESKGQL-LLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQ 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430616178 395 VVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYT 465
Cdd:PRK09847 414 ALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFT 484
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
20-472 |
1.34e-105 |
|
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: 321.50 E-value: 1.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 20 PVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAfND 99
Cdd:cd07147 2 EVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA-RG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 100 EIPAIVDVFRFFAGAARCLNG----LAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSE 175
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGevlpLDISARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 176 ITPLTALKLAE-LAKDIFPAGVINVLFGRgKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASsiKRTHMELGGKAPVI 254
Cdd:cd07147 161 RTPLSALILGEvLAETGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 255 VFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKA 334
Cdd:cd07147 238 VDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 335 VEEAKATGhIKVITGGeKRKGNgyYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKD 414
Cdd:cd07147 318 VNEAVDAG-AKLLTGG-KRDGA--LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 415 VGRAHRVSARLQYGCTWVN--THFMlVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRhVMV 472
Cdd:cd07147 394 LEKALRAWDELEVGGVVINdvPTFR-VDHMPYGGVKDSGIGREGVRYAIEEMTEPR-LLV 451
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
6-470 |
6.64e-104 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 318.39 E-value: 6.64e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 6 LINGELVSGE-GEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAEL 84
Cdd:PRK11241 14 LINGEWLDANnGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 85 ESRNCGKPLHSAfNDEIPAIVDVFRFFAGAARCLnglaAGEYLEGHTS----MIRRDPLGVVASIAPWNYPLMMAAWKLA 160
Cdd:PRK11241 94 MTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRI----YGDTIPGHQAdkrlIVIKQPIGVTAAITPWNFPAAMITRKAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 161 PALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASS 239
Cdd:PRK11241 169 PALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 240 IKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTEL 319
Cdd:PRK11241 249 IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 320 GPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWA 399
Cdd:PRK11241 329 GPLIDEKAVAKVEEHIADALEKG-ARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQA 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430616178 400 NDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHV 470
Cdd:PRK11241 408 NDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYM 478
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
22-465 |
4.50e-100 |
|
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: 307.25 E-value: 4.50e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 22 YNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNdEI 101
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG-EI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 102 PAIVDVFRFFAG-AARCLNGLAAGEYlEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLT 180
Cdd:cd07102 80 RGMLERARYMISiAEEALADIRVPEK-DGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 181 ALKLAELAKDI-FPAGVINVLFGRGKTVGDpLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDA 259
Cdd:cd07102 159 GERFAAAFAEAgLPEGVFQVLHLSHETSAA-LIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 260 DIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEAK 339
Cdd:cd07102 238 DLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 340 ATGHIKVITGGE--KRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGR 417
Cdd:cd07102 318 AKGARALIDGALfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIAR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1430616178 418 AHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYT 465
Cdd:cd07102 398 AEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLT 445
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
9-474 |
1.34e-99 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 308.73 E-value: 1.34e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 9 GELVSGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRN 88
Cdd:PRK09407 24 ARVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 89 CGKPLHSAFnDEIPAIVDVFRFFAGAARCLngLAAgeylEGHTSMI--------RRDPLGVVASIAPWNYPLMMAAWKLA 160
Cdd:PRK09407 104 TGKARRHAF-EEVLDVALTARYYARRAPKL--LAP----RRRAGALpvltktteLRQPKGVVGVISPWNYPLTLAVSDAI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 161 PALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHpkVRMVSLTGSIATGEHIISHTASS 239
Cdd:PRK09407 177 PALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 240 IKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTEL 319
Cdd:PRK09407 255 LIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 320 GPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKGNG-YYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNW 398
Cdd:PRK09407 335 GSLISEAQLETVSAHVDDAVAKG-ATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVER 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 399 ANDSQYGLASSVWTKDVGRAHRVSARLQ---------YGCTWVNThfmlvsEMPHGGQKLSGYGKDMSLYGLEDYTVVRH 469
Cdd:PRK09407 414 ANDTPYGLNASVWTGDTARGRAIAARIRagtvnvnegYAAAWGSV------DAPMGGMKDSGLGRRHGAEGLLKYTESQT 487
|
....*
gi 1430616178 470 VMVKH 474
Cdd:PRK09407 488 IATQR 492
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
4-460 |
6.06e-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: 6.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 4 KLLINGELVSGEGEK-QPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFA 82
Cdd:cd07085 2 KLFINGEWVESKTTEwLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 83 ELESRNCGKPLHSAFNDEIPAIvDVFRFFAGAARclngLAAGEYLE----GHTSMIRRDPLGVVASIAPWNYPLMMAAWK 158
Cdd:cd07085 82 RLITLEHGKTLADARGDVLRGL-EVVEFACSIPH----LLKGEYLEnvarGIDTYSYRQPLGVVAGITPFNFPAMIPLWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 159 LAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGrGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTA 237
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 238 SSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDEST 317
Cdd:cd07085 236 ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 318 ELGPLSSLAHLERVSKAVEEAKATGHIKVITG-GEKRKG--NGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQ 394
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGrGVKVPGyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430616178 395 VVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNT-------HFmlvsemPHGGQKLSGYGkDMSLYG 460
Cdd:cd07085 396 AIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVpipvplaFF------SFGGWKGSFFG-DLHFYG 461
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
24-472 |
8.05e-97 |
|
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: 299.22 E-value: 8.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 24 PATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFnDEIPA 103
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAF-EEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 104 IVDVFRFFAGAA-RCLNGLAAGEYLEGHTSMIR-RDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTA 181
Cdd:cd07101 82 VAIVARYYARRAeRLLKPRRRRGAIPVLTRTTVnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 182 LKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHpkVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDAD 260
Cdd:cd07101 162 LWAVELLIEAgLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 261 IEAVVEG-VR-TFGyyNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEA 338
Cdd:cd07101 240 LDKAAAGaVRaCFS--NAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 339 KATGhIKVITGGEKRKGNG-YYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGR 417
Cdd:cd07101 318 VAKG-ATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430616178 418 AHRVSARLQYGCTWVNTHFMLV---SEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07101 397 GRRIAARLRAGTVNVNEGYAAAwasIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
54-470 |
1.05e-94 |
|
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: 292.94 E-value: 1.05e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 54 EWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSA-FNdeIPAIVDVFRFFAGAARclngLAAGEYL----E 128
Cdd:cd07105 15 AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAgFN--VDLAAGMLREAASLIT----QIIGGSIpsdkP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 129 GHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGR---G 204
Cdd:cd07105 89 GTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAgLPKGVLNVVTHSpedA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 205 KTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVrTFG-YYNAGQDCTAA 283
Cdd:cd07105 169 PEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAA-LFGaFLNSGQICMST 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 284 CRIYAQKGIYDTLVEKLGAAVATLKSGAPDdesteLGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKG-NGYYYAP 362
Cdd:cd07105 248 ERIIVHESIADEFVEKLKAAAEKLFAGPVV-----LGSLVSAAAADRVKELVDDALSKG-AKLVVGGLADESpSGTSMPP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 363 TLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNThfMLV--- 439
Cdd:cd07105 322 TILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHING--MTVhde 399
|
410 420 430
....*....|....*....|....*....|.
gi 1430616178 440 SEMPHGGQKLSGYGKDMSLYGLEDYTVVRHV 470
Cdd:cd07105 400 PTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
21-468 |
3.63e-90 |
|
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: 281.94 E-value: 3.63e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 21 VYNPATGDVLLEIAEASAEQVDAAVRAADAAFaewGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPL-HSAFnd 99
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALAASYR---STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLkDTRY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 100 EIPAIVDVFRFFAGAARCLNG--LAAGEYLEGHTSMI--RRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSE 175
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGesFSCDLTANGKARKIftLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 176 ITPLTALKLAE-LAKDIFPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGeHIISHTASsIKRTHMELGGKAPVI 254
Cdd:cd07146 158 KTPLSAIYLADlLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVG-KAIAATAG-YKRQLLELGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 255 VFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKA 334
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 335 VEEAKATGhIKVITGGEKRkgnGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKD 414
Cdd:cd07146 316 VEEAIAQG-ARVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430616178 415 VGRAHRVSARLQYGCTWVNTHFMLVSEM-PHGGQKLSGYG-KDMSLYGLEDYTVVR 468
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNEVPGFRSELsPFGGVKDSGLGgKEGVREAMKEMTNVK 447
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
5-451 |
5.45e-90 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 283.36 E-value: 5.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 5 LLINGELVSGEgEKQPVYNPA-TGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAE 83
Cdd:PRK03137 39 LIIGGERITTE-DKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 84 LESRNCGKPLHSAFNDEIPAIvDVFRFFAgaaRCLNGLAAG---EYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLA 160
Cdd:PRK03137 118 WLVKEAGKPWAEADADTAEAI-DFLEYYA---RQMLKLADGkpvESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 161 PALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASS 239
Cdd:PRK03137 194 AAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 240 ------IKRTHMELGGKAPVIVFDDADIEAVVEGVRT--FGYynAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGA 311
Cdd:PRK03137 274 qpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVAsaFGF--SGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 312 PDDeSTELGPLSSLAHLERVSKAVEEAKATGhiKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDN 391
Cdd:PRK03137 352 PED-NAYMGPVINQASFDKIMSYIEIGKEEG--RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430616178 392 EEQVVNWANDSQYGLASSVWTKDvgRAHRVSARLQY---------GCTWVnthfmLVSEMPHGGQKLSG 451
Cdd:PRK03137 429 FDHALEIANNTEYGLTGAVISNN--REHLEKARREFhvgnlyfnrGCTGA-----IVGYHPFGGFNMSG 490
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
27-457 |
1.57e-87 |
|
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: 274.94 E-value: 1.57e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 27 GDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAfNDEIPAIVD 106
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKA-GFEVGAAIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 107 VFRFFAGaarcLNGLAAGEYL---EGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTA-L 182
Cdd:cd07152 80 ELHEAAG----LPTQPQGEILpsaPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 183 KLAELAKDI-FPAGVINVLFGrGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDADI 261
Cdd:cd07152 156 VIARLFEEAgLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 262 EAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEAKAT 341
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 342 GhIKVITGGEKrkgNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRV 421
Cdd:cd07152 315 G-ARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMAL 390
|
410 420 430
....*....|....*....|....*....|....*..
gi 1430616178 422 SARLQYGCTWVNTHFML-VSEMPHGGQKLSGYGKDMS 457
Cdd:cd07152 391 ADRLRTGMLHINDQTVNdEPHNPFGGMGASGNGSRFG 427
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
5-474 |
6.22e-84 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 267.50 E-value: 6.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 5 LLINGELVSGEGEKQPVyNPA-TGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAE 83
Cdd:TIGR01237 35 LVINGERVETENKIVSI-NPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 84 LESRNCGKPLHSAFNDEIPAIvDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPAL 163
Cdd:TIGR01237 114 LLVKEVGKPWNEADAEVAEAI-DFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 164 AAGNCVVLKPSEITPLTALKLAE-LAKDIFPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTA----- 237
Cdd:TIGR01237 193 VTGNCVVLKPAEAAPVIAAKFVEiLEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkvqpg 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 238 -SSIKRTHMELGGKAPVIVFDDADIEAVVEGVRT--FGYynAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDD 314
Cdd:TIGR01237 273 qKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTsaFGF--AGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDS 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 315 ESTELGPLSSLAHLERVSKAVEEAKATGhiKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQ 394
Cdd:TIGR01237 351 ADVYVGPVIDQKSFNKIMEYIEIGKAEG--RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 395 VVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKLSGYGkdmSLYGLEDYtVVRHVMV 472
Cdd:TIGR01237 429 ALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITgaIVGYQPFGGFKMSGTD---SKAGGPDY-LALFMQA 504
|
..
gi 1430616178 473 KH 474
Cdd:TIGR01237 505 KT 506
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
22-472 |
3.20e-82 |
|
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: 261.85 E-value: 3.20e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 22 YNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDEI 101
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 102 PAIVDVFRFFAGaarclNGLAA-------GEYLEGH-TSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKP 173
Cdd:cd07098 81 LVTCEKIRWTLK-----HGEKAlrpesrpGGLLMFYkRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 174 SEITPLTALKLAELAKDIF-----PAGVINVLFGRGKTvGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELG 248
Cdd:cd07098 156 SEQVAWSSGFFLSIIRECLaacghDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 249 GKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHL 328
Cdd:cd07098 235 GKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 329 ERVSKAVEEAKATGhIKVITGGEKRKG----NGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQY 404
Cdd:cd07098 315 DRLEELVADAVEKG-ARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEY 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 405 GLASSVWTKDVGRAHRVSARLQYGCTWVN--THFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07098 394 GLGASVFGKDIKRARRIASQLETGMVAINdfGVNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
23-464 |
1.32e-81 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 260.06 E-value: 1.32e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 23 NPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAfNDEIP 102
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA-KAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 103 AIVDVFRFFAGAARclnGLAAGEYLEGHTS-----MIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEIT 177
Cdd:PRK09406 86 KCAKGFRYYAEHAE---ALLADEPADAAAVgasraYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 178 PLTALKLAEL-AKDIFPAGVINVLFGRGKTVGDPLTgHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVF 256
Cdd:PRK09406 163 PQTALYLADLfRRAGFPDGCFQTLLVGSGAVEAILR-DPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 257 DDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVE 336
Cdd:PRK09406 242 PSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 337 EAKATGhIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVG 416
Cdd:PRK09406 322 DAVAAG-ATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1430616178 417 RAHRVSARLQYGCTWVNThfMLVS--EMPHGGQKLSGYGKDMSLYGLEDY 464
Cdd:PRK09406 401 EQERFIDDLEAGQVFING--MTVSypELPFGGVKRSGYGRELSAHGIREF 448
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
8-420 |
2.21e-79 |
|
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: 254.82 E-value: 2.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 8 NGELVsGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESR 87
Cdd:cd07130 4 DGEWG-GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 88 NCGKPLHSAFNdEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGN 167
Cdd:cd07130 83 EMGKILPEGLG-EVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 168 CVVLKPSEITPLTAL---KLAE--LAKDIFPAGVINVLFGrGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKR 242
Cdd:cd07130 162 VVVWKPSPTTPLTAIavtKIVArvLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 243 THMELGGKAPVIVFDDADIEAVVEGVrTFGYY-NAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGP 321
Cdd:cd07130 241 SLLELGGNNAIIVMEDADLDLAVRAV-LFAAVgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 322 LSSLAHLERVSKAVEEAKATGHiKVITGGEKRKGNGYYYAPTLLAGaLQDDTIVQKEVFGPVVSVTPFDNEEQVVNWAND 401
Cdd:cd07130 320 LHTKAAVDNYLAAIEEAKSQGG-TVLFGGKVIDGPGNYVEPTIVEG-LSDAPIVKEETFAPILYVLKFDTLEEAIAWNNE 397
|
410
....*....|....*....
gi 1430616178 402 SQYGLASSVWTKDVGRAHR 420
Cdd:cd07130 398 VPQGLSSSIFTTDLRNAFR 416
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
23-470 |
3.16e-75 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 243.62 E-value: 3.16e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 23 NPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAfNDEIP 102
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA-RAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 103 AIVDVFRFFA--GAARclngLAAGEYL-EGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPL 179
Cdd:PRK13968 92 KSANLCDWYAehGPAM----LKAEPTLvENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 180 TALKLAELAKDI-FPAGVINVLFGRGKTVGDpLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDD 258
Cdd:PRK13968 168 CAQLIAQVFKDAgIPQGVYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLND 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 259 ADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEA 338
Cdd:PRK13968 247 ADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 339 KATGhIKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRA 418
Cdd:PRK13968 327 LAEG-ARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQA 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1430616178 419 HRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHV 470
Cdd:PRK13968 406 RQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
1-453 |
9.11e-72 |
|
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: 235.55 E-value: 9.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 1 MQHKLLINGELVSGEGEKQPVYNP-ATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQ 79
Cdd:cd07083 16 GRAYPLVIGGEWVDTKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 80 VFAELESRNCGKPLHSAFnDEIPAIVDVFRFFAGAARCLNG---LAAGEYLEGHTSMIRrdPLGVVASIAPWNYPLMMAA 156
Cdd:cd07083 96 ELIATLTYEVGKNWVEAI-DDVAEAIDFIRYYARAALRLRYpavEVVPYPGEDNESFYV--GLGAGVVISPWNFPVAIFT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 157 WKLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISH 235
Cdd:cd07083 173 GMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 236 TA------SSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKS 309
Cdd:cd07083 253 AArlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 310 GAPDDESTELGPLSSLAHLERVSKAVEEAKATGhiKVITGGEKRKGNGYYYAPTLLAGALQDDTIVQKEVFGPVVSV--T 387
Cdd:cd07083 333 GPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG--QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVirY 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430616178 388 PFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKLSGYG 453
Cdd:cd07083 411 KDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITgaLVGVQPFGGFKLSGTN 478
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
5-453 |
2.83e-71 |
|
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: 234.78 E-value: 2.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 5 LLINGELVSGEGekQPVYNPATGDVLL-EIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAE 83
Cdd:cd07125 36 IINGEETETGEG--APVIDPADHERTIgEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 84 LESRNCGKPLHSAfNDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPAL 163
Cdd:cd07125 114 LAAAEAGKTLADA-DAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 164 AAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHI---ISHTASS 239
Cdd:cd07125 193 AAGNTVIAKPAEQTPLIAARAVELLHEAgVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLInraLAERDGP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 240 IKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTEL 319
Cdd:cd07125 273 ILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 320 GPLSSLAHLERVSKAVEEAKATGhiKVITGGEKRKGNGYYYAPTLLAGalqdDTI--VQKEVFGPVVSVTPFDNE--EQV 395
Cdd:cd07125 353 GPLIDKPAGKLLRAHTELMRGEA--WLIAPAPLDDGNGYFVAPGIIEI----VGIfdLTTEVFGPILHVIRFKAEdlDEA 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 396 VNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVN--THFMLVSEMPHGGQKLSGYG 453
Cdd:cd07125 427 IEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrnITGAIVGRQPFGGWGLSGTG 486
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
4-460 |
2.00e-69 |
|
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: 229.00 E-value: 2.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 4 KLLINGELVSGEGEKQ-PVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFA 82
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYiPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 83 ELESRNCGKPLHSAFNDeipaivdVFRFF--AGAARCLNGLAAGEYLEGHTSMIR----RDPLGVVASIAPWNYPLMMAA 156
Cdd:TIGR01722 82 ELITAEHGKTHSDALGD-------VARGLevVEHACGVNSLLKGETSTQVATRVDvysiRQPLGVCAGITPFNFPAMIPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 157 WKLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGrGKTVGDPLTGHPKVRMVSLTGSIATGEHIISH 235
Cdd:TIGR01722 155 WMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAgAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 236 TASSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQkGIYDTLVEKLGAAVATLKSGAPDDE 315
Cdd:TIGR01722 234 GSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLV-GAADEWVPEIRERAEKIRIGPGDDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 316 STELGPLSSLAHLERVSKAVEEAKATGHIKVITG-GEKRKG--NGYYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNE 392
Cdd:TIGR01722 313 GAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGrGYKVDGyeEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTL 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430616178 393 EQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFML-VSEMPHGGQKLSGYGkDMSLYG 460
Cdd:TIGR01722 393 EEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVpLPYFSFTGWKDSFFG-DHHIYG 460
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
63-453 |
2.44e-65 |
|
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: 217.29 E-value: 2.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 63 RAECLLKLADVIEENGQVFAELESRNCGKPLhsafndeIPAIVDVFRFFAG---AARCLNGLAAGEYLEGHT-------S 132
Cdd:cd07148 46 RIAILERLADLMEERADELALLIAREGGKPL-------VDAKVEVTRAIDGvelAADELGQLGGREIPMGLTpasagriA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 133 MIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGrGKTVGDPL 211
Cdd:cd07148 119 FTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAgLPEGWCQAVPC-ENAVAEKL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 212 TGHPKVRMVSLTGSIATGEHIISHTASSiKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKG 291
Cdd:cd07148 198 VTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 292 IYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEAKATGHiKVITGGeKRKGNGyYYAPTLLAGALQD 371
Cdd:cd07148 277 IADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGA-RLLCGG-KRLSDT-TYAPTVLLDPPRD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 372 DTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFML-VSEMPHGGQKLS 450
Cdd:cd07148 354 AKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFrVDWMPFAGRRQS 433
|
...
gi 1430616178 451 GYG 453
Cdd:cd07148 434 GYG 436
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
9-453 |
1.37e-59 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 211.21 E-value: 1.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 9 GELVSGEGEKQPVYNPA-TGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESR 87
Cdd:PRK11904 554 GPIINGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVR 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 88 NCGKPLHSAFnDEIPAIVDVFRFFAGAARCLngLAAGEYLEGHT---SMIRRDPLGVVASIAPWNYPLMMAAWKLAPALA 164
Cdd:PRK11904 634 EAGKTLQDAI-AEVREAVDFCRYYAAQARRL--FGAPEKLPGPTgesNELRLHGRGVFVCISPWNFPLAIFLGQVAAALA 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 165 AGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIAtgehiishTASSIKRT 243
Cdd:PRK11904 711 AGNTVIAKPAEQTPLIAAEAVKLLHEAgIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTE--------TARIINRT 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 244 HM-----------ELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTaACRI-YAQKGIYDTLVEKLGAAVATLKSGA 311
Cdd:PRK11904 783 LAardgpivpliaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCS-ALRVlFVQEDIADRVIEMLKGAMAELKVGD 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 312 PDDESTELGP---------LssLAHLERVSKaveEAKATGHIKVITGGEkrkgNGYYYAPTLLagALQDDTIVQKEVFGP 382
Cdd:PRK11904 862 PRLLSTDVGPvidaeakanL--DAHIERMKR---EARLLAQLPLPAGTE----NGHFVAPTAF--EIDSISQLEREVFGP 930
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430616178 383 VVSVTPFDNEE--QVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHfML---VSEMPHGGQKLSGYG 453
Cdd:PRK11904 931 ILHVIRYKASDldKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRN-QIgavVGVQPFGGQGLSGTG 1005
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
56-472 |
2.17e-59 |
|
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: 200.83 E-value: 2.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 56 GQTTP-KVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDEIPAIVDVFRFfagAARCLNGLAAGE------YLE 128
Cdd:cd07087 14 GKTRSlEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDH---ALKHLKKWMKPRrvsvplLLQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 129 GHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGrGKTVG 208
Cdd:cd07087 91 PAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVEG-GVEVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 209 DPLTGHPkVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVrTFG-YYNAGQDCTAACRIY 287
Cdd:cd07087 170 TALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRI-AWGkFLNAGQTCIAPDYVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 288 AQKGIYDTLVEKLGAAVATLkSGAPDDESTELGPLSSLAHLERVSKAVEEAkatghiKVITGGEKRKGNgYYYAPTLLAG 367
Cdd:cd07087 248 VHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDG------KVVIGGQVDKEE-RYIAPTILDD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 368 ALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVN--THFMLVSEMPHG 445
Cdd:cd07087 320 VSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvLLHAAIPNLPFG 399
|
410 420
....*....|....*....|....*..
gi 1430616178 446 GQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07087 400 GVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
3-453 |
9.71e-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: 201.29 E-value: 9.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 3 HKLLINGELVSGEGEKQPVYNPATGDVLL-EIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVF 81
Cdd:TIGR01238 37 QAAPIIGHSYKADGEAQPVTNPADRRDIVgQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 82 AELESRNCGKPLHSAFnDEIPAIVDVFRFFAGAARCLNGLAAGEyleghtsmirrdPLGVVASIAPWNYPLMMAAWKLAP 161
Cdd:TIGR01238 117 MALCVREAGKTIHNAI-AEVREAVDFCRYYAKQVRDVLGEFSVE------------SRGVFVCISPWNFPLAIFTGQISA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 162 ALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSI 240
Cdd:TIGR01238 184 ALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 241 KRTH---MELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDEST 317
Cdd:TIGR01238 264 DAPVpliAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 318 ELGPLSSLAHLERVSKAVEEAKATGHI--KVITGGEKRKGNGYYYAPTLLagALQDDTIVQKEVFGPVVSVTPFDNEE-- 393
Cdd:TIGR01238 344 DVGPVIDAEAKQNLLAHIEHMSQTQKKiaQLTLDDSRACQHGTFVAPTLF--ELDDIAELSEEVFGPVLHVVRYKAREld 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430616178 394 QVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKLSGYG 453
Cdd:TIGR01238 422 QIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVgaVVGVQPFGGQGLSGTG 483
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
3-453 |
6.75e-58 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 198.83 E-value: 6.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 3 HKLLINGE-LVSGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVF 81
Cdd:PLN00412 16 YKYYADGEwRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 82 AELESRNCGKPLHSAFNdEIPAIVDVFRFfaGAARCLNGLAAGEYLEGHT---------SMIRRDPLGVVASIAPWNYPL 152
Cdd:PLN00412 96 AECLVKEIAKPAKDAVT-EVVRSGDLISY--TAEEGVRILGEGKFLVSDSfpgnernkyCLTSKIPLGVVLAIPPFNYPV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 153 MMAAWKLAPALAAGNCVVLKPSEITPLTALKLAE-LAKDIFPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSiATGEH 231
Cdd:PLN00412 173 NLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHcFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 232 IiSHTASSIKrTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGA 311
Cdd:PLN00412 252 I-SKKAGMVP-LQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 312 PDDEStELGPLSSLAHLERVSKAVEEAKATGhiKVITGGEKRKGNGYYyaPTLLAGALQDDTIVQKEVFGPVVSVTPFDN 391
Cdd:PLN00412 330 PEDDC-DITPVVSESSANFIEGLVMDAKEKG--ATFCQEWKREGNLIW--PLLLDNVRPDMRIAWEEPFGPVLPVIRINS 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430616178 392 EEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNT-------HFmlvsemPHGGQKLSGYG 453
Cdd:PLN00412 405 VEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSapargpdHF------PFQGLKDSGIG 467
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
54-465 |
6.13e-57 |
|
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: 194.41 E-value: 6.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 54 EWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAfNDEIPAIVDVFRFFAGAARCLNGLAAgEYLEGHTSM 133
Cdd:cd07095 15 GWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA-QTEVAAMAGKIDISIKAYHERTGERA-TPMAQGRAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 134 IRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAEL-AKDIFPAGVINVLFGrGKTVGDPLT 212
Cdd:cd07095 93 LRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELwEEAGLPPGVLNLVQG-GRETGEALA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 213 GHPKVRMVSLTGSIATGEHIISHTASSI-KRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKG 291
Cdd:cd07095 172 AHEGIDGLLFTGSAATGLLLHRQFAGRPgKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 292 IY-DTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEAKATGHiKVITGGEKRKGNGYYYAPTLL----A 366
Cdd:cd07095 252 AVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGG-EPLLAMERLVAGTAFLSPGIIdvtdA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 367 GALQDDtivqkEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCtwVNTHFMLV---SEMP 443
Cdd:cd07095 331 ADVPDE-----EIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGI--VNWNRPTTgasSTAP 403
|
410 420
....*....|....*....|..
gi 1430616178 444 HGGQKLSGYGKDmSLYGLEDYT 465
Cdd:cd07095 404 FGGVGLSGNHRP-SAYYAADYC 424
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
6-453 |
4.36e-55 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 198.55 E-value: 4.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 6 LINGELVSGEGekQPVYNPA-TGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAEL 84
Cdd:PRK11905 558 LLAGGDVDGGT--RPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFAL 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 85 ESRNCGKPLHSAFnDEIPAIVDVFRFFAGAARCLnglaageyleghTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALA 164
Cdd:PRK11905 636 AVREAGKTLANAI-AEVREAVDFLRYYAAQARRL------------LNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALV 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 165 AGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRT 243
Cdd:PRK11905 703 AGNTVLAKPAEQTPLIAARAVRLLHEAgVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPP 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 244 HM---ELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTaACRI-YAQKGIYDTLVEKLGAAVATLKSGAPDDESTEL 319
Cdd:PRK11905 783 VPliaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCS-ALRVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDV 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 320 GPLSSLAHLERVSKAVEEAKATGH-IKVITGGEKRKgNGYYYAPTLLA-GALQDdtiVQKEVFGPVVSVTPFDNEE--QV 395
Cdd:PRK11905 862 GPVIDAEAQANIEAHIEAMRAAGRlVHQLPLPAETE-KGTFVAPTLIEiDSISD---LEREVFGPVLHVVRFKADEldRV 937
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 396 VNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKLSGYG 453
Cdd:PRK11905 938 IDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIgaVVGVQPFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
6-453 |
4.87e-54 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 195.54 E-value: 4.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 6 LINGELVSGEGekQPVYNPA-TGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAEL 84
Cdd:COG4230 561 LIAGEAASGEA--RPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMAL 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 85 ESRNCGKPLHSAFnDEIPAIVDVFRFFAGAARCLngLAAGEYLEghtsmirrdPLGVVASIAPWNYPL-----MMAAwkl 159
Cdd:COG4230 639 LVREAGKTLPDAI-AEVREAVDFCRYYAAQARRL--FAAPTVLR---------GRGVFVCISPWNFPLaiftgQVAA--- 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 160 apALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGeHIISHTAS 238
Cdd:COG4230 704 --ALAAGNTVLAKPAEQTPLIAARAVRLLHEAgVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETA-RLINRTLA 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 239 siKRTHM------ELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCtAACRI-YAQKGIYDTLVEKLGAAVATLKSGA 311
Cdd:COG4230 781 --ARDGPivpliaETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRC-SALRVlCVQEDIADRVLEMLKGAMAELRVGD 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 312 PDDESTELGPLSSLAHLERVSKAVEEAKATGhiKVITGGEKRKG--NGYYYAPTLLA-GALQDdtiVQKEVFGPVVSVTP 388
Cdd:COG4230 858 PADLSTDVGPVIDAEARANLEAHIERMRAEG--RLVHQLPLPEEcaNGTFVAPTLIEiDSISD---LEREVFGPVLHVVR 932
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430616178 389 FDNEE--QVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNthfmlvSEM--------PHGGQKLSGYG 453
Cdd:COG4230 933 YKADEldKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN------RNIigavvgvqPFGGEGLSGTG 1001
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
56-471 |
7.98e-54 |
|
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: 186.27 E-value: 7.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 56 GQTTP-KVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDEIPAIVDVFRFfagAARCLNGLAAGEYLEG----- 129
Cdd:cd07135 21 GKTKDlEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILH---MLKNLKKWAKDEKVKDgplaf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 130 --HTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGrgktv 207
Cdd:cd07135 98 mfGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAFQVVQG----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 208 GDPLTGhpkvRMVSL-------TGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEgvRTF--GYYNAGQ 278
Cdd:cd07135 173 GVPETT----ALLEQkfdkifyTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAK--RILwgKFGNAGQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 279 DCTAACRIYAQKGIYDTLVEKLGAAVATL-KSGApdDESTELGPLSSLAHLERVSKAVEEAKAtghiKVITGGEKRKGNg 357
Cdd:cd07135 247 ICVAPDYVLVDPSVYDEFVEELKKVLDEFyPGGA--NASPDYTRIVNPRHFNRLKSLLDTTKG----KVVIGGEMDEAT- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 358 YYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYG-CTWVNT-- 434
Cdd:cd07135 320 RFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGgVVINDTli 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 1430616178 435 HFMLVSeMPHGGQKLSGYGKDMSLYGLEDYTVVRHVM 471
Cdd:cd07135 400 HVGVDN-APFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
127-472 |
9.77e-52 |
|
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: 180.89 E-value: 9.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 127 LEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGrGKT 206
Cdd:cd07134 89 LFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEG-DAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 207 VGDPLTGHPkVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRI 286
Cdd:cd07134 168 VAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 287 YAQKGIYDTLVEKLGAAVAT-LKSGAPDDESTELGPLSSLAHLERVSKAVEEAKATGhIKVITGGEKRKgNGYYYAPTLL 365
Cdd:cd07134 247 FVHESVKDAFVEHLKAEIEKfYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKG-AKVEFGGQFDA-AQRYIAPTVL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 366 AGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNT---HFmLVSEM 442
Cdd:cd07134 325 TNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDvvlHF-LNPNL 403
|
330 340 350
....*....|....*....|....*....|
gi 1430616178 443 PHGGQKLSGYGKDMSLYGLEDYTVVRHVMV 472
Cdd:cd07134 404 PFGGVNNSGIGSYHGVYGFKAFSHERAVLR 433
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
132-453 |
2.61e-51 |
|
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: 180.01 E-value: 2.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 132 SMIRRDPLGVVASIAPWNYPLMMAawkLAP---ALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGrGKTVG 208
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAVVEG-GVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 209 DPLTgHPKVRMVSLTGSIATG--------EHIISHTassikrthMELGGKAPVIVFDDADIEAVVEGVrTFG-YYNAGQD 279
Cdd:cd07136 170 QELL-DQKFDYIFFTGSVRVGkivmeaaaKHLTPVT--------LELGGKSPCIVDEDANLKLAAKRI-VWGkFLNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 280 CTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPdDESTELGPLSSLAHLERVSKAVEEAkatghiKVITGGEKRKgNGYY 359
Cdd:cd07136 240 CVAPDYVLVHESVKEKFIKELKEEIKKFYGEDP-LESPDYGRIINEKHFDRLAGLLDNG------KIVFGGNTDR-ETLY 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 360 YAPTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVN---THF 436
Cdd:cd07136 312 IEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtiMHL 391
|
330
....*....|....*..
gi 1430616178 437 MlVSEMPHGGQKLSGYG 453
Cdd:cd07136 392 A-NPYLPFGGVGNSGMG 407
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
5-407 |
8.22e-51 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 179.77 E-value: 8.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 5 LLINGELVSGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAEL 84
Cdd:PRK09457 3 LWINGDWIAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 85 ESRNCGKPLHSAfNDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGhTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALA 164
Cdd:PRK09457 83 IARETGKPLWEA-ATEVTAMINKIAISIQAYHERTGEKRSEMADG-AAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 165 AGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGrGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSI-KR 242
Cdd:PRK09457 161 AGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPeKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 243 THMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIY-DTLVEKLGAAVATLKSGAPDDESTE-LG 320
Cdd:PRK09457 240 LALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDAEPQPfMG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 321 PLSSLAHLERVSKAVEEAKATGHIKVITGGEKRKGNGyyyaptLLAGALQDDTIVQ----KEVFGPVVSVTPFDNEEQVV 396
Cdd:PRK09457 320 AVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTG------LLTPGIIDVTGVAelpdEEYFGPLLQVVRYDDFDEAI 393
|
410
....*....|.
gi 1430616178 397 NWANDSQYGLA 407
Cdd:PRK09457 394 RLANNTRFGLS 404
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
56-474 |
9.76e-50 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 176.76 E-value: 9.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 56 GQTTP-KVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAarcLNGLAAGEYLEGH---- 130
Cdd:PTZ00381 23 GKTRPlEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKH---LDEYLKPEKVDTVgvfg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 131 --TSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGrGKTVG 208
Cdd:PTZ00381 100 pgKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIEG-GVEVT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 209 DPLTGHPkVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYA 288
Cdd:PTZ00381 179 TELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 289 QKGIYDTLVEKLGAAVATLkSGAPDDESTELGPLSSLAHLERVSKAVEEAKAtghiKVITGGEKRKGNgYYYAPTLLAGA 368
Cdd:PTZ00381 258 HRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKDHGG----KVVYGGEVDIEN-KYVAPTIIVNP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 369 LQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVN---THFmLVSEMPHG 445
Cdd:PTZ00381 332 DLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcvFHL-LNPNLPFG 410
|
410 420
....*....|....*....|....*....
gi 1430616178 446 GQKLSGYGKDMSLYGLEDYTVVRHVMVKH 474
Cdd:PTZ00381 411 GVGNSGMGAYHGKYGFDTFSHPKPVLNKS 439
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
23-413 |
1.58e-49 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 176.56 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 23 NPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNdEIP 102
Cdd:PLN02315 40 NPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIG-EVQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 103 AIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTAL 182
Cdd:PLN02315 119 EIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 183 KLAE-----LAKDIFPAGVINVLFGrGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFD 257
Cdd:PLN02315 199 AMTKlvaevLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 258 DADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEE 337
Cdd:PLN02315 278 DADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEI 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430616178 338 AKATGHiKVITGGEKRKGNGYYYAPTLLAGAlQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTK 413
Cdd:PLN02315 358 IKSQGG-KILTGGSAIESEGNFVQPTIVEIS-PDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTR 431
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
15-453 |
2.08e-48 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 179.01 E-value: 2.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 15 EGEKQPVYNPA-TGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPL 93
Cdd:PRK11809 657 AGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTF 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 94 HSAFNdEIPAIVDVFRFFAGaarclnglaageyleghtsMIRRD-------PLGVVASIAPWNYPLMMAAWKLAPALAAG 166
Cdd:PRK11809 737 SNAIA-EVREAVDFLRYYAG-------------------QVRDDfdndthrPLGPVVCISPWNFPLAIFTGQVAAALAAG 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 167 NCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIAtgehiishTASSIKRTH- 244
Cdd:PRK11809 797 NSVLAKPAEQTPLIAAQAVRILLEAgVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTE--------VARLLQRNLa 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 245 -------------MELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGA 311
Cdd:PRK11809 869 grldpqgrpipliAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGN 948
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 312 PDDESTELGPLSSLAHLERVSKAVEEAKATGH--IKVITGGEKRKGNGYYYAPTLLagALQDDTIVQKEVFGPVVSVTPF 389
Cdd:PRK11809 949 PDRLSTDIGPVIDAEAKANIERHIQAMRAKGRpvFQAARENSEDWQSGTFVPPTLI--ELDSFDELKREVFGPVLHVVRY 1026
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430616178 390 DNEE--QVVNWANDSQYGLASSVWTK-DVGRAHrVSARLQYGCTWVNTHFM--LVSEMPHGGQKLSGYG 453
Cdd:PRK11809 1027 NRNQldELIEQINASGYGLTLGVHTRiDETIAQ-VTGSAHVGNLYVNRNMVgaVVGVQPFGGEGLSGTG 1094
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
59-453 |
3.51e-46 |
|
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: 165.74 E-value: 3.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 59 TPKVRAECLLKLADVIEENGQVFAELESRNCGKplHSAFNDeipAIVDVFRFFAGAARCLNGLA---------AGEYLEG 129
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADFGH--RSRHET---LLAEILPSIAGIKHARKHLKkwmkpsrrhVGLLFLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 130 HTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGrGKTVGD 209
Cdd:cd07133 93 AKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAVVTG-GADVAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 210 PLTGHPKVRMVsLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQ 289
Cdd:cd07133 172 AFSSLPFDHLL-FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 290 KGIYDTLVEKLGAAVATLksgAPDD-ESTELGPLSSLAHLERVSKAVEEAKATGhIKVIT-------GGEKRKgngyyYA 361
Cdd:cd07133 251 EDKLEEFVAAAKAAVAKM---YPTLaDNPDYTSIINERHYARLQGLLEDARAKG-ARVIElnpagedFAATRK-----LP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 362 PTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVN---THFMl 438
Cdd:cd07133 322 PTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINdtlLHVA- 400
|
410
....*....|....*
gi 1430616178 439 VSEMPHGGQKLSGYG 453
Cdd:cd07133 401 QDDLPFGGVGASGMG 415
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
6-460 |
4.92e-46 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 168.77 E-value: 4.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 6 LINGELVSGEGEK-QPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAEL 84
Cdd:PLN02419 117 LIGGSFVESQSSSfIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 85 ESRNCGKPLHSAFNDEIPAIvDVFRFFAGAARclngLAAGEYL----EGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLA 160
Cdd:PLN02419 197 ITTEQGKTLKDSHGDIFRGL-EVVEHACGMAT----LQMGEYLpnvsNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 161 PALAAGNCVVLKPSEITPLTALKLAELAKDI-FPAGVINVLFGRGKTVgDPLTGHPKVRMVSLTGSIATGEHIISHTASS 239
Cdd:PLN02419 272 VAVTCGNTFILKPSEKDPGASVILAELAMEAgLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 240 IKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIY---AQKGIYDTLVEKLGAAVATLKSgAPDdes 316
Cdd:PLN02419 351 GKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVfvgDAKSWEDKLVERAKALKVTCGS-EPD--- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 317 TELGPLSSLAHLERVSKAVEEAKATGHIKVITGGE-----KRKGNgyYYAPTLLAGALQDDTIVQKEVFGPVVSVTPFDN 391
Cdd:PLN02419 427 ADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpgYEKGN--FIGPTILSGVTPDMECYKEEIFGPVLVCMQANS 504
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 392 EEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFML-VSEMPHGGQKLSgYGKDMSLYG 460
Cdd:PLN02419 505 FDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVpLPFFSFTGNKAS-FAGDLNFYG 573
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
5-451 |
6.61e-46 |
|
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: 166.99 E-value: 6.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 5 LLINGELV-SGEGEKQPvyNPAT-GDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEEN----- 77
Cdd:cd07123 35 LVIGGKEVrTGNTGKQV--MPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKyryel 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 78 ------GQvfaelesrncGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGL-----AAGEYleghTSMIRRdPL-GVVASI 145
Cdd:cd07123 113 naatmlGQ----------GKNVWQAEIDAACELIDFLRFNVKYAEELYAQqplssPAGVW----NRLEYR-PLeGFVYAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 146 APWNYPLMMAAWKLAPALAaGNCVVLKPSEitplTALKLAELAKDIF-----PAGVINVLFGRGKTVGDPLTGHPKVRMV 220
Cdd:cd07123 178 SPFNFTAIGGNLAGAPALM-GNVVLWKPSD----TAVLSNYLVYKILeeaglPPGVINFVPGDGPVVGDTVLASPHLAGL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 221 SLTGSIATGEHIISHTASSIKRTHM------ELGGKAPVIVFDDADIEAVVEG-VR-TFGYynAGQDCTAACRIYAQKGI 292
Cdd:cd07123 253 HFTGSTPTFKSLWKQIGENLDRYRTyprivgETGGKNFHLVHPSADVDSLVTAtVRgAFEY--QGQKCSAASRAYVPESL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 293 YDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEAKATGHIKVITGGEKRKGNGYYYAPTLLAGALQDD 372
Cdd:cd07123 331 WPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVEPTVIETTDPKH 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 373 TIVQKEVFGPVVSVTPFDNEE-----QVVNwaNDSQYGLASSVWTKDV------GRAHRVSArlqyGCTWVNTHFM--LV 439
Cdd:cd07123 411 KLMTEEIFGPVLTVYVYPDSDfeetlELVD--TTSPYALTGAIFAQDRkaireaTDALRNAA----GNFYINDKPTgaVV 484
|
490
....*....|..
gi 1430616178 440 SEMPHGGQKLSG 451
Cdd:cd07123 485 GQQPFGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
133-473 |
7.37e-44 |
|
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: 159.69 E-value: 7.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 133 MIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAE-----LAKDIFPagvinVLFGrGKTV 207
Cdd:cd07132 95 YIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAElipkyLDKECYP-----VVLG-GVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 208 GDPLTGHpKVRMVSLTGSIATGehIISHTASS--IKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACR 285
Cdd:cd07132 169 TTELLKQ-RFDYIFYTGSTSVG--KIVMQAAAkhLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 286 IYAQKGIYDTLVEKLGaavATLKS--GAPDDESTELGPLSSLAHLERVSKAVEEAkatghiKVITGGEKRKGNgYYYAPT 363
Cdd:cd07132 246 VLCTPEVQEKFVEALK---KTLKEfyGEDPKESPDYGRIINDRHFQRLKKLLSGG------KVAIGGQTDEKE-RYIAPT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 364 LLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFM--LVSE 441
Cdd:cd07132 316 VLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMhyTLDS 395
|
330 340 350
....*....|....*....|....*....|..
gi 1430616178 442 MPHGGQKLSGYGKDMSLYGLEDYTVVRHVMVK 473
Cdd:cd07132 396 LPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
67-453 |
2.36e-39 |
|
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: 147.56 E-value: 2.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 67 LLKLADviEENGQVFAELESrNCGKPLHSAFNDEIPAIVDVFRFfagAARCLNGLAAGEYLEG------HTSMIRRDPLG 140
Cdd:cd07137 30 LLRLVD--ENEDDIFAALRQ-DLGKPSAESFRDEVSVLVSSCKL---AIKELKKWMAPEKVKTplttfpAKAEIVSEPLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 141 VVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGrGKTVGDPLTGHpKVRMV 220
Cdd:cd07137 104 VVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEG-GVPETTALLEQ-KWDKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 221 SLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVrTFGYY--NAGQDCTAACRIYAQKGIYDTLVE 298
Cdd:cd07137 182 FFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRI-AGGKWgcNNGQACIAPDYVLVEESFAPTLID 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 299 KLgaaVATLKS--GAPDDESTELGPLSSLAHLERVSKAVEEAKATGhiKVITGGEKRKGNgYYYAPTLLAGALQDDTIVQ 376
Cdd:cd07137 261 AL---KNTLEKffGENPKESKDLSRIVNSHHFQRLSRLLDDPSVAD--KIVHGGERDEKN-LYIEPTILLDPPLDSSIMT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 377 KEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVN---THFMlVSEMPHGGQKLSGYG 453
Cdd:cd07137 335 EEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdtvVQYA-IDTLPFGGVGESGFG 413
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
7-414 |
9.11e-34 |
|
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: 133.16 E-value: 9.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 7 INGELVSGEGEKQPVYNPATGDVlleIAEASAEqvdaavRAADAAFAEWGQTT--PKV-------RAECLLKLADVIEEN 77
Cdd:cd07128 5 VAGQWHAGTGDGRTLHDAVTGEV---VARVSSE------GLDFAAAVAYAREKggPALraltfheRAAMLKALAKYLMER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 78 GQVFAELESRNCGKPLHSAFNDEiPAIVDVFRFFAGAARCLNGlaAGEYLEGHTSMIRRD----------PL-GVVASIA 146
Cdd:cd07128 76 KEDLYALSAATGATRRDSWIDID-GGIGTLFAYASLGRRELPN--AHFLVEGDVEPLSKDgtfvgqhiltPRrGVAVHIN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 147 PWNYPlmmaAW----KLAPALAAGNCVVLKPSEITPLTALKLAELAKD--IFPAGVINVLFGRGKTVGDPLTGHPkvrMV 220
Cdd:cd07128 153 AFNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVEsgLLPEGALQLICGSVGDLLDHLGEQD---VV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 221 SLTGSIATGEHIISH---TASSIkRTHME--------LGgkaPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQ 289
Cdd:cd07128 226 AFTGSAATAAKLRAHpniVARSI-RFNAEadslnaaiLG---PDATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 290 KGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEAKATGHIkVITGGEKRKGN------GYYYAPT 363
Cdd:cd07128 302 EARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEV-VFGGPDRFEVVgadaekGAFFPPT 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1430616178 364 LL--AGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKD 414
Cdd:cd07128 381 LLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
131-453 |
3.70e-30 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 122.46 E-value: 3.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 131 TSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGRGKTVGDP 210
Cdd:PLN02174 105 SAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTETTAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 211 LtgHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGY-YNAGQDCTAACRIYAQ 289
Cdd:PLN02174 185 L--EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 290 KGIYDTLVEKLGAAVATLKSGAPdDESTELGPLSSLAHLERVSKAVEEAKATGhiKVITGGEKRKGNgYYYAPTLLAGAL 369
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNP-MESKDMSRIVNSTHFDRLSKLLDEKEVSD--KIVYGGEKDREN-LKIAPTILLDVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 370 QDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVN---THFMLVSeMPHGG 446
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiaVHLALHT-LPFGG 417
|
....*..
gi 1430616178 447 QKLSGYG 453
Cdd:PLN02174 418 VGESGMG 424
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
63-395 |
3.00e-29 |
|
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: 119.26 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 63 RAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRD--PLG 140
Cdd:cd07084 23 RADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPHEPGNHLGQGLKQQSHGYrwPYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 141 VVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKD--IFPAGVINVLFGRGKTvGDPLTGHPKVR 218
Cdd:cd07084 103 PVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGDGKT-MQALLLHPNPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 219 MVSLTGSIATGEHIISHTASSikRTHMELGGKAPVIVFDDADIEAVV--EGVRTFgYYNAGQDCTAACRIYAQKGIYDT- 295
Cdd:cd07084 182 MVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYVawQCVQDM-TACSGQKCTAQSMLFVPENWSKTp 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 296 LVEKLGAAVATLKsgapdDESTELGPLSSLAHLERvskaVEEAKATGHIKVITGGEKRKGN------GYYYAPTLLAGAL 369
Cdd:cd07084 259 LVEKLKALLARRK-----LEDLLLGPVQTFTTLAM----IAHMENLLGSVLLFSGKELKNHsipsiyGACVASALFVPID 329
|
330 340
....*....|....*....|....*....
gi 1430616178 370 QDDT---IVQKEVFGPVVSVTPFDNEEQV 395
Cdd:cd07084 330 EILKtyeLVTEEIFGPFAIVVEYKKDQLA 358
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
7-460 |
7.28e-27 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 113.26 E-value: 7.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 7 INGELVSGEGEKQPVYNPATGDVLleiAEASAEqvDAAVRAADAAFAEWGQT-----TPKVRAECLLKLADVIEENGQVF 81
Cdd:PRK11903 9 VAGRWQAGSGAGTPLFDPVTGEEL---VRVSAT--GLDLAAAFAFAREQGGAalralTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 82 AELESRNCGkplhSAFNDeipAIVDVfrffAGAARCLN-----GLAAGE---YLEGHTSMIRRDPL-----------GVV 142
Cdd:PRK11903 84 YDIATANSG----TTRND---SAVDI----DGGIFTLGyyaklGAALGDarlLRDGEAVQLGKDPAfqgqhvlvptrGVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 143 ASIAPWNYPlmmaAW----KLAPALAAGNCVVLKPSEITPLTALKLAE--LAKDIFPAGVINVLFGRGKTVGDPLTGHPk 216
Cdd:PRK11903 153 LFINAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKdvVAAGILPAGALSVVCGSSAGLLDHLQPFD- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 217 vrMVSLTGSIATGEHIISHTASSIKRTHMELGG---KAPVIVFDDA-DIEA----VVEGVRTFGYyNAGQDCTAACRIYA 288
Cdd:PRK11903 228 --VVSFTGSAETAAVLRSHPAVVQRSVRVNVEAdslNSALLGPDAApGSEAfdlfVKEVVREMTV-KSGQKCTAIRRIFV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 289 QKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVSKAVEEAKAtgHIKVITGGEKRK------GNGYYYAP 362
Cdd:PRK11903 305 PEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRA--QAEVLFDGGGFAlvdadpAVAACVGP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 363 TLL--AGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDvgRAHrvSARLQYGCTWVNTHFMLVS 440
Cdd:PRK11903 383 TLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD--AAF--LAAAALELADSHGRVHVIS 458
|
490 500
....*....|....*....|..
gi 1430616178 441 emPHGGQKLSGYGKDM--SLYG 460
Cdd:PRK11903 459 --PDVAALHTGHGNVMpqSLHG 478
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
54-465 |
2.89e-25 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 108.28 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 54 EWGQTtpKVRAecLLKLadVIEENGQVFAELEsRNCGKPLHSAFNDEIPAIVDVFRFfagAARCLNGLAAGEYLE----- 128
Cdd:PLN02203 28 EWRKS--QLKG--LLRL--LKDNEEAIFKALH-QDLGKHRVEAYRDEVGVLTKSANL---ALSNLKKWMAPKKAKlplva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 129 -GHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFGrGKTV 207
Cdd:PLN02203 98 fPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEG-GPAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 208 GDPLTGHPKVRmVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIV--FDDA-DIEAVVEGV--RTFGYYnAGQDCTA 282
Cdd:PLN02203 177 GEQLLQHKWDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIvgGKWGSC-AGQACIA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 283 ACRIYAQKGIYDTLVEKLGaavATLKS--GAPDDESTELGPLSSLAHLERVSKAVEEAKATGHIkvITGGEKRKGNgYYY 360
Cdd:PLN02203 255 IDYVLVEERFAPILIELLK---STIKKffGENPRESKSMARILNKKHFQRLSNLLKDPRVAASI--VHGGSIDEKK-LFI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 361 APTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRV------------SARLQYG 428
Cdd:PLN02203 329 EPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRIlsetssgsvtfnDAIIQYA 408
|
410 420 430
....*....|....*....|....*....|....*..
gi 1430616178 429 CtwvnthfmlvSEMPHGGQKLSGYGKDMSLYGLEDYT 465
Cdd:PLN02203 409 C----------DSLPFGGVGESGFGRYHGKYSFDTFS 435
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
48-426 |
8.06e-23 |
|
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: 100.69 E-value: 8.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 48 ADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAfNDEIPAIVDVFRFFAGAARclnglaAGEYL 127
Cdd:cd07129 8 AAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARL-QGELGRTTGQLRLFADLVR------EGSWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 128 E------------GHTSMIRRD--PLGVVASIAPWNYPLM--MAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDI 191
Cdd:cd07129 81 DaridpadpdrqpLPRPDLRRMlvPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAIRAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 192 -----FPAGVINVLFGRGKTVGDPLTGHPKVRMVSLTGSIATGEhIISHTASsiKRT-----HMELGGKAPVIVFDDA-- 259
Cdd:cd07129 161 lratgLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGR-ALFDAAA--ARPepipfYAELGSVNPVFILPGAla 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 260 -DIEAVVEGVR---TFGyynAGQDCTAACRIYAQKGI-YDTLVEKLGAAVAtlksGAPDdestelGPLSSLAHLERVSKA 334
Cdd:cd07129 238 eRGEAIAQGFVgslTLG---AGQFCTNPGLVLVPAGPaGDAFIAALAEALA----AAPA------QTMLTPGIAEAYRQG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 335 VEEAKATGHIKVITGGEKRkGNGYYYAPTLL---AGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVW 411
Cdd:cd07129 305 VEALAAAPGVRVLAGGAAA-EGGNQAAPTLFkvdAAAFLADPALQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIH 383
|
410
....*....|....*..
gi 1430616178 412 --TKDVGRAHRVSARLQ 426
Cdd:cd07129 384 geEDDLALARELLPVLE 400
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
142-402 |
4.06e-14 |
|
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: 74.44 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 142 VASIAPWN-YPLMMAAwklapaLAAGNCVVLKPSEITPLTALKLAELAKDIF------PAGVINVLFGRGKTVGDPLTGH 214
Cdd:cd07127 202 CSTFPTWNgYPGLFAS------LATGNPVIVKPHPAAILPLAITVQVAREVLaeagfdPNLVTLAADTPEEPIAQTLATR 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 215 PKVRMVSLTGSIATGEHIISHTASsiKRTHMELGGKAPVIVFDDADIEAVVEGV-RTFGYYnAGQDCTAACRIYAQK-GI 292
Cdd:cd07127 276 PEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVVDSTDDLKAMLRNLaFSLSLY-SGQMCTTPQNIYVPRdGI 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 293 --------YDTLVEKLGAAVATLkSGAPDDESTELGPLSSLAHLERVskaveeAKATGHIKVITGGEKRKGNGYYYA--- 361
Cdd:cd07127 353 qtddgrksFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARI------AEARQLGEVLLASEAVAHPEFPDArvr 425
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1430616178 362 -PTLLAGALQDDTIVQKEVFGPVVSVTPFDNEEQVVNWANDS 402
Cdd:cd07127 426 tPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARES 467
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
106-393 |
1.94e-11 |
|
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: 65.98 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 106 DVFRFFAgaaRCLNglAAGEYLeGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLA 185
Cdd:cd07126 116 DQVRFLA---RSFN--VPGDHQ-GQQSSGYRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 186 ELAKDI-FPAGVINVLFGRGKTVGDPLTgHPKVRMVSLTGSIATGEHIISHTASSIKrthMELGGKAPVIVFDD-ADIEA 263
Cdd:cd07126 190 RLLHLCgMPATDVDLIHSDGPTMNKILL-EANPRMTLFTGSSKVAERLALELHGKVK---LEDAGFDWKILGPDvSDVDY 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 264 VVEGVRTFGYYNAGQDCTAACRIYAQKGIYDT-LVEKLGAAVATLKSgapddESTELGPLSSLAHlERVSKAVEEAKATG 342
Cdd:cd07126 266 VAWQCDQDAYACSGQKCSAQSILFAHENWVQAgILDKLKALAEQRKL-----EDLTIGPVLTWTT-ERILDHVDKLLAIP 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430616178 343 HIKVITGGEKRKGNGY-----YYAPTLLAGALQDDTI------VQKEVFGPVVSVTPFDNEE 393
Cdd:cd07126 340 GAKVLFGGKPLTNHSIpsiygAYEPTAVFVPLEEIAIeenfelVTTEVFGPFQVVTEYKDEQ 401
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
59-338 |
2.53e-09 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 59.16 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 59 TPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGLAAGEyleGHT------- 131
Cdd:cd07077 14 HDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGITASV---GHIqdvllpd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 132 ---SMIRRDPLGVVASIAPWNYPLMmAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINVLFG----RG 204
Cdd:cd07077 91 ngeTYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVLyvphPS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 205 KTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASsiKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNaGQDCTAAC 284
Cdd:cd07077 170 DELAEELLSHPKIDLIVATGGRDAVDAAVKHSPH--IPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQ 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430616178 285 RIYAQKGIYDTLVE--KLGAAVATLK--------SGAPDDES-----TELGPLSSLAHLERVSKAVEEA 338
Cdd:cd07077 247 NLYVVDDVLDPLYEefKLKLVVEGLKvpqetkplSKETTPSFddealESMTPLECQFRVLDVISAVENA 315
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
132-305 |
3.86e-06 |
|
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: 49.16 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 132 SMIRRDPLGVVASIAPWNYP--------LMMaawklapaLAAGNCVVLKPSEITPLTALKLAEL-AKDIFPAGVINVLFg 202
Cdd:cd07121 91 TLVEYAPFGVIGAITPSTNPtetiinnsISM--------LAAGNAVVFNPHPGAKKVSAYAVELiNKAIAEAGGPDNLV- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 203 rgKTVGDP-------LTGHPKVRMVSLTGsiatGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVrtfgYYN 275
Cdd:cd07121 162 --VTVEEPtiettneLMAHPDINLLVVTG----GPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAARDI----VQG 231
|
170 180 190
....*....|....*....|....*....|....
gi 1430616178 276 AGQD----CTAACRIYAQKGIYDTLVEKLGAAVA 305
Cdd:cd07121 232 ASFDnnlpCIAEKEVIAVDSVADYLIAAMQRNGA 265
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
132-300 |
1.87e-05 |
|
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: 46.88 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 132 SMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKD-IFPAGVINVLFGrgkTVGDP 210
Cdd:cd07081 89 TLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQaAVAAGAPENLIG---WIDNP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 211 -------LTGHPKVRMVSLTGsiatGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAA 283
Cdd:cd07081 166 sielaqrLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASE 241
|
170
....*....|....*..
gi 1430616178 284 CRIYAQKGIYDTLVEKL 300
Cdd:cd07081 242 QSVIVVDSVYDEVMRLF 258
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
133-305 |
8.82e-05 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 44.89 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 133 MIRRDPLGVVASIAPWNYP--------LMMaawklapaLAAGNCVVLKPSEITPLTALKLAELAKD-IFPAGVINVLFGr 203
Cdd:PRK15398 124 LIEYAPFGVIGAVTPSTNPtetiinnaISM--------LAAGNSVVFSPHPGAKKVSLRAIELLNEaIVAAGGPENLVV- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 204 gkTVGDP-------LTGHPKVRMVSLTGsiatGEHIISHTASSIKRTHMELGGKAPVIVFDDADIE----AVVEGvrtfg 272
Cdd:PRK15398 195 --TVAEPtietaqrLMKHPGIALLVVTG----GPAVVKAAMKSGKKAIGAGAGNPPVVVDETADIEkaarDIVKG----- 263
|
170 180 190
....*....|....*....|....*....|....*..
gi 1430616178 273 yynAGQD----CTAACRIYAQKGIYDTLVEKLGAAVA 305
Cdd:PRK15398 264 ---ASFDnnlpCIAEKEVIVVDSVADELMRLMEKNGA 297
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
138-300 |
1.50e-04 |
|
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: 44.02 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 138 PLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIF-----PAGVINVLfgrgKTVGDPLT 212
Cdd:cd07122 95 PVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAvaagaPEGLIQWI----EEPSIELT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 213 ----GHPKVRMVsltgsIATGEHIISHTA-SSIKRThmeLG---GKAPVIVFDDADIEAVVEGV---RTFGYynaGQDCT 281
Cdd:cd07122 171 qelmKHPDVDLI-----LATGGPGMVKAAySSGKPA---IGvgpGNVPAYIDETADIKRAVKDIilsKTFDN---GTICA 239
|
170
....*....|....*....
gi 1430616178 282 AACRIYAQKGIYDTLVEKL 300
Cdd:cd07122 240 SEQSVIVDDEIYDEVRAEL 258
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
125-305 |
1.57e-03 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 40.89 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 125 EYLEGHTSMIRRDPLGVVASIAPWNYPLMmAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFP----AGVINVL 200
Cdd:pfam05893 75 EWLPTKPSYEKAFPPGLVFHVLSGNVPLL-PVMSILMGLLVKNVNLLKVSSSDPFTAAALLASFADLDPthplADSLSVV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430616178 201 FGRGktvgdPLTGHPKVRMVSLTGSIATGehiiSHTASSIKRTHmeLGGKAPVIVFD----------DADIEAVVEGVRT 270
Cdd:pfam05893 154 YWDG-----GSTQLEDLIVANADVVIAWG----GEDAINAIREC--LKPGKQWIDFGakisfavvdrEAALDKAAERAAD 222
|
170 180 190
....*....|....*....|....*....|....*....
gi 1430616178 271 -FGYYNAgQDCTAACRIYAQKG---IYDTLVEKLGAAVA 305
Cdd:pfam05893 223 dICVFDQ-QACLSPQTVFVESDdkiTPDEFAERLAAALA 260
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
131-197 |
3.64e-03 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 39.57 E-value: 3.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430616178 131 TSMIRRDPLGVVASIAPWNYPLMmAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVI 197
Cdd:cd07080 105 GGYIRAQPRGLVVHIIAGNVPLL-PVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLADVDPNHPL 170
|
|
| |
