|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
25-546 |
0e+00 |
|
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: 1011.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 25 VANEPILEFKPGSLERAALQKALNDLKGKTEAIPCVVGGQEVWTADVRYQLSPYNHAHKVAKYCYADKDLINKAINAAVA 104
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 105 VRREWDLRPIQDRAQIFFKAADLLSGPRRAEVLAKTMIGQGKTVIQAEIDAAAELIDFFRFNAKYAMELEEEQLISVP-V 183
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPaG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 184 STNSMVYRGLEGFVAAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFG 263
Cdd:cd07123 161 VWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 264 DTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYRTFPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSA 343
Cdd:cd07123 241 DTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 344 CSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSPNLTILAGGKCDDKVGYFIE 423
Cdd:cd07123 321 ASRAYVPESLWPEVKERLLEELKEIKMGDPD-DFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 424 PCIVETKDPKDRIMKEEIFGPVLAVYVYPEKQYKDILQLVDTTSPYGLTGAVFAQDKNVIQEARKLLRNAAGNFYINDKS 503
Cdd:cd07123 400 PTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1121863746 504 TGAVVAQQPFGGARASGTNDKPGGRHYILRWTSPQAIKETHVP 546
Cdd:cd07123 480 TGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETFVP 522
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
26-556 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 900.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 26 ANEPILEFKPGSLERAALQKALNDLKGKTEAIPCVVGGQEVWTADVR-YQLSPYNHAHKVAKYCYADKDLINKAINAAVA 104
Cdd:TIGR01236 1 ANEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEVYDSNERiPQVNPHNHQAVLAKATNATEEDAMKAVEAALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 105 VRREWDLRPIQDRAQIFFKAADLLSGPRRAEVLAKTMIGQGKTVIQAEIDAAAELIDFFRFNAKYAMELEEEQLISVPVS 184
Cdd:TIGR01236 81 AKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPISAPGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 185 TNSMVYRGLEGFVAAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGD 264
Cdd:TIGR01236 161 WNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 265 TVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYRTFPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSAC 344
Cdd:TIGR01236 241 QVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 345 SRLYVPDLLWPQIKAKLLEEHGKIKVGDPaGDFETFFSAVIDDKSFARIKKWIQHAETSP-NLTILAGGKCDDKVGYFIE 423
Cdd:TIGR01236 321 SRLYVPHSKWPEFKSDLLAELQSVKVGDP-DDFRGFMGAVIDEQSFDKIVKYIEDAKKDPeALTILYGGKYDDSQGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 424 PCIVETKDPKDRIMKEEIFGPVLAVYVYPEKQYKDILQLVDTTSPYGLTGAVFAQDKNVIQEARKLLRNAAGNFYINDKS 503
Cdd:TIGR01236 400 PTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYINDKC 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1121863746 504 TGAVVAQQPFGGARASGTNDKPGGRHYILRWTSPQAIKETHVPLEDWKYSYMQ 556
Cdd:TIGR01236 480 TGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
40-544 |
0e+00 |
|
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: 695.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 40 RAALQKALNDLKG-KTEAIPCVVGGQEVWTADVRYQLSPYNHAHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRA 118
Cdd:cd07083 1 RRAMREALRRVKEeFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 119 QIFFKAADLLSGPRRAEVLAKTMIGqGKTVIQaEIDAAAELIDFFRFNAKYAMELEEEQ--LISVPVSTNSMVYRGLeGF 196
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEV-GKNWVE-AIDDVAEAIDFIRYYARAALRLRYPAveVVPYPGEDNESFYVGL-GA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 197 VAAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGL 275
Cdd:cd07083 158 GVVISPWNFPvAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 276 NFTGSVPTFKRLWKQVSENLDRYRTFPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWP 355
Cdd:cd07083 238 NFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 356 QIKAKLLEEHGKIKVGDPAGDfETFFSAVIDDKSFARIKKWIQHAETSpnLTILAGGKCDDKVGYFIEPCIVETKDPKDR 435
Cdd:cd07083 318 PVLERLLKRAERLSVGPPEEN-GTDLGPVIDAEQEAKVLSYIEHGKNE--GQLVLGGKRLEGEGYFVAPTVVEEVPPKAR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 436 IMKEEIFGPVLAVYVYPEKQYKDILQLVDTTsPYGLTGAVFAQDKNVIQEARKLLrnAAGNFYINDKSTGAVVAQQPFGG 515
Cdd:cd07083 395 IAQEEIFGPVLSVIRYKDDDFAEALEVANST-PYGLTGGVYSRKREHLEEARREF--HVGNLYINRKITGALVGVQPFGG 471
|
490 500
....*....|....*....|....*....
gi 1121863746 516 ARASGTNDKPGGRHYILRWTSPQAIKETH 544
Cdd:cd07083 472 FKLSGTNAKTGGPHYLRRFLEMKAVAERF 500
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
53-544 |
3.02e-138 |
|
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: 409.13 E-value: 3.02e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 53 KTEAIPCVVGGQEVWTADVRYQ--LSPYNhAHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSg 130
Cdd:COG1012 2 TTPEYPLFIGGEWVAAASGETFdvINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 131 pRRAEVLAKTM-IGQGKTVIQAEIDAAaELIDFFRFNAKYAMELEEEQLISVPVSTNSMVYRglE--GFVAAVSPFNFTA 207
Cdd:COG1012 80 -ERREELAALLtLETGKPLAEARGEVD-RAADFLRYYAGEARRLYGETIPSDAPGTRAYVRR--EplGVVGAITPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 208 IGGNLAGAPAL-MGNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKR 286
Cdd:COG1012 156 ALAAWKLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 287 LWKQVSENLdryrtfPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHG 366
Cdd:COG1012 236 IAAAAAENL------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 367 KIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAEtSPNLTILAGGKC-DDKVGYFIEPCIVETKDPKDRIMKEEIFGPV 445
Cdd:COG1012 310 ALKVGDPL-DPGTDMGPLISEAQLERVLAYIEDAV-AEGAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 446 LAVYVYpeKQYKDILQLVDTTsPYGLTGAVFAQDKNVIQEARKLLRnaAGNFYINDKSTGAvVAQQPFGGARASGTNDKp 525
Cdd:COG1012 388 LSVIPF--DDEEEAIALANDT-EYGLAASVFTRDLARARRVARRLE--AGMVWINDGTTGA-VPQAPFGGVKQSGIGRE- 460
|
490
....*....|....*....
gi 1121863746 526 GGRHYILRWTSPQAIKETH 544
Cdd:COG1012 461 GGREGLEEYTETKTVTIRL 479
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
96-540 |
4.52e-128 |
|
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: 381.56 E-value: 4.52e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 96 NKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTM-IGQGKTVIQAEIDAAaELIDFFRFNAKYAMELE 174
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLE--ERREELAALEtLETGKPIEEALGEVA-RAADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 175 EEQLISVPVSTNSMVYRGLEGFVAAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQ 253
Cdd:cd07078 78 GEVIPSPDPGELAIVRREPLGVVGAITPWNFPlLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 254 FVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLdryrtfPRLAGECGGKNFHLVHSSADVPTVVNGTLRSA 333
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 334 FEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAEtSPNLTILAGGK 413
Cdd:cd07078 232 FGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPL-DPDTDMGPLISAAQLDRVLAYIEDAK-AEGAKLLCGGK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 414 CDD-KVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDTTsPYGLTGAVFAQDKNVIQEARKLLRn 492
Cdd:cd07078 310 RLEgGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPF--KDEEEAIELANDT-EYGLAAGVFTRDLERALRVAERLE- 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1121863746 493 aAGNFYINDKSTGAvVAQQPFGGARASGTNdKPGGRHYILRWTSPQAI 540
Cdd:cd07078 386 -AGTVWINDYSVGA-EPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
27-542 |
5.60e-127 |
|
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: 381.57 E-value: 5.60e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 27 NEPILEFKPGSLeRAALQKALNDLK---GKTeaIPCVVGGQEVWTADVRYQLSPYNHAHKVAKYCYADKDLINKAINAAV 103
Cdd:cd07124 3 NEPFTDFADEEN-RAAFRAALARVReelGRE--YPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 104 AVRREWDLRPIQDRAQIFFKAADLLSgPRRAEVLAKTMIGQGKTVIQAEIDAAaELIDFFRFNAKYAMELEEEQLISVPV 183
Cdd:cd07124 80 AAFPTWRRTPPEERARLLLRAAALLR-RRRFELAAWMVLEVGKNWAEADADVA-EAIDFLEYYAREMLRLRGFPVEMVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 184 STNSMVYRGLeGFVAAVSPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVF 262
Cdd:cd07124 158 EDNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 263 GDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYRTFPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCS 342
Cdd:cd07124 237 GDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 343 ACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETspNLTILAGGKCDDKV--GY 420
Cdd:cd07124 317 ACSRVIVHESVYDEFLERLVERTKALKVGDPE-DPEVYMGPVIDKGARDRIRRYIEIGKS--EGRLLLGGEVLELAaeGY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 421 FIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDTTsPYGLTGAVFAQDKNVIQEARKLLRnaAGNFYIN 500
Cdd:cd07124 394 FVQPTIFADVPPDHRLAQEEIFGPVLAVIKA--KDFDEALEIANDT-EYGLTGGVFSRSPEHLERARREFE--VGNLYAN 468
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1121863746 501 DKSTGAVVAQQPFGGARASGTNDKPGGRHYILRWTSPQAIKE 542
Cdd:cd07124 469 RKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTE 510
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
75-540 |
7.28e-120 |
|
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: 361.46 E-value: 7.28e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 75 LSPYNHaHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTM-IGQGKTVIQAEI 153
Cdd:pfam00171 12 INPATG-EVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLE--ERKDELAELEtLENGKPLAEARG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 154 DAAaELIDFFRFNAKYAMELEEEQLISVPVSTNSMVYRGLeGFVAAVSPFNFTAiggNLAG---APALM-GNVVLWKPSD 229
Cdd:pfam00171 89 EVD-RAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPL-GVVGAITPWNFPL---LLPAwkiAPALAaGNTVVLKPSE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 230 TAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLdryrtfPRLAGECG 309
Cdd:pfam00171 164 LTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 310 GKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKS 389
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPL-DPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 390 FARIKKWIQHAeTSPNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDTTsPY 469
Cdd:pfam00171 317 LERVLKYVEDA-KEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRF--KDEEEAIEIANDT-EY 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1121863746 470 GLTGAVFAQDKNVIQEARKLLRnaAGNFYINDKSTGAVVAqQPFGGARASGTNDKpGGRHYILRWTSPQAI 540
Cdd:pfam00171 393 GLAAGVFTSDLERALRVARRLE--AGMVWINDYTTGDADG-LPFGGFKQSGFGRE-GGPYGLEEYTEVKTV 459
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
27-543 |
7.78e-110 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 337.68 E-value: 7.78e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 27 NEPILEFkpgSLE--RAALQKALNDLK---GKTeaIPCVVGGQEVWTADVRYQLSPYNHAHKVAKYCYADKDLINKAINA 101
Cdd:PRK03137 7 HEPFTDF---SVEenVEAFEEALKKVEkelGQD--YPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 102 AVAVRREWDLRPIQDRAQIFFKAADLLSgPRRAEVLAKTMIGQGKTVIQAEIDAAaELIDFFRFNAKYAMELEEEQ-LIS 180
Cdd:PRK03137 82 ALEAFETWKKWSPEDRARILLRAAAIIR-RRKHEFSAWLVKEAGKPWAEADADTA-EAIDFLEYYARQMLKLADGKpVES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 181 VPVSTNSMVYRGLeGFVAAVSPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASG 259
Cdd:PRK03137 160 RPGEHNRYFYIPL-GVGVVISPWNFpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 260 PVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYRTFPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQ 339
Cdd:PRK03137 239 SEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 340 KCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDfeTFFSAVIDDKSFARIKKWIQHAETSPNLtiLAGGKCDDKVG 419
Cdd:PRK03137 319 KCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN--AYMGPVINQASFDKIMSYIEIGKEEGRL--VLGGEGDDSKG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 420 YFIEPCIVETKDPKDRIMKEEIFGPVLAvyVYPEKQYKDILQLVDTTsPYGLTGAVFAQDKNVIQEARKLLRnaAGNFYI 499
Cdd:PRK03137 395 YFIQPTIFADVDPKARIMQEEIFGPVVA--FIKAKDFDHALEIANNT-EYGLTGAVISNNREHLEKARREFH--VGNLYF 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1121863746 500 NDKSTGAVVAQQPFGGARASGTNDKPGGRHYILRWTSPQAIKET 543
Cdd:PRK03137 470 NRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEM 513
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
27-542 |
3.56e-97 |
|
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: 304.87 E-value: 3.56e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 27 NEPILEFKPGSLeRAALQKAL---NDLKGKTeaIPCVVGGQEVWTADVRYQLSPYNHAHKVAKYCYADKDLINKAINAAV 103
Cdd:TIGR01237 3 HEPFTDFADEEN-RQAFFKALatvKEQLGKT--YPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 104 AVRREWDLRPIQDRAQIFFKAADLLSgPRRAEVLAKTMIGQGKTVIQAEIDAAaELIDFFRFNAKYAMELEEEQLI-SVP 182
Cdd:TIGR01237 80 KAFEAWKKTDPEERAAILFKAAAIVR-RRRHEFSALLVKEVGKPWNEADAEVA-EAIDFMEYYARQMIELAKGKPVnSRE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 183 VSTNSMVYRGLeGFVAAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPV 261
Cdd:TIGR01237 158 GETNQYVYTPT-GVTVVISPWNFPfAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 262 FGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYRTFPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKC 341
Cdd:TIGR01237 237 VGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 342 SACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSPNLTIlaGGKCDDKVGYF 421
Cdd:TIGR01237 317 SAGSRAVVHEKVYDEVVERFVEITESLKVGPPD-SADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVS--GGCGDDSKGYF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 422 IEPCIVETKDPKDRIMKEEIFGPVLAvyVYPEKQYKDILQLVDTTSpYGLTGAVFAQDKNVIQEARKLLRnaAGNFYIND 501
Cdd:TIGR01237 394 IGPTIFADVDRKARLAQEEIFGPVVA--FIRASDFDEALEIANNTE-YGLTGGVISNNRDHINRAKAEFE--VGNLYFNR 468
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1121863746 502 KSTGAVVAQQPFGGARASGTNDKPGGRHYILRWTSPQAIKE 542
Cdd:TIGR01237 469 NITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKTVTE 509
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
101-540 |
1.49e-93 |
|
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: 290.28 E-value: 1.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 101 AAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTM-IGQGKTvIQAEIDAAAELIDFFRFNAKYAMELEEEQLI 179
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLE--ERREELAALEtLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 180 SVPVSTNSMVYRGLEGFVAAVSPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPAS 258
Cdd:cd06534 79 SPDPGGEAYVRREPLGVVGVITPWNFpLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 259 GPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLdryrtfPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGG 338
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 339 QKCSACSRLYVPDLLWPQIKAKLLeehgkikvgdpagdfetffsaviddksfarikkwiqhaetspnltilaggkcddkv 418
Cdd:cd06534 233 QICTAASRLLVHESIYDEFVEKLV-------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 419 gyfiepCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDTTsPYGLTGAVFAQDKNVIQEARKLLRnaAGNFY 498
Cdd:cd06534 257 ------TVLVDVDPDMPIAQEEIFGPVLPVIRF--KDEEEAIALANDT-EYGLTAGVFTRDLNRALRVAERLR--AGTVY 325
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1121863746 499 INDKSTGaVVAQQPFGGARASGTNDKpGGRHYILRWTSPQAI 540
Cdd:cd06534 326 INDSSIG-VGPEAPFGGVKNSGIGRE-GGPYGLEEYTRTKTV 365
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
40-533 |
2.92e-93 |
|
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: 294.87 E-value: 2.92e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 40 RAALQKALNDLKGKT-EAIPCVVGGQEVW--TADVRyqlSPYNHAHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQD 116
Cdd:cd07125 16 LEALADALKAFDEKEwEAIPIINGEETETgeGAPVI---DPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 117 RAQIFFKAADLLSGpRRAEVLAKTMIGQGKTVIQAeIDAAAELIDFFRFNAKYAMELEEEQLISVPVS-TNSMVYRGLeG 195
Cdd:cd07125 93 RAEILEKAADLLEA-NRGELIALAAAEAGKTLADA-DAEVREAIDFCRYYAAQARELFSDPELPGPTGeLNGLELHGR-G 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 196 FVAAVSPFNF---TAIGGNLAgapALM-GNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEH 271
Cdd:cd07125 170 VFVCISPWNFplaIFTGQIAA---ALAaGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 272 FAGLNFTGSVPTFKRLWKQVSEnldRYRTFPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPD 351
Cdd:cd07125 247 IDGVIFTGSTETAKLINRALAE---RDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 352 LLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSPNLtiLAGGKCDDKVGYFIEPCIVEtkD 431
Cdd:cd07125 324 EIAERFIEMLKGAMASLKVGDPW-DLSTDVGPLIDKPAGKLLRAHTELMRGEAWL--IAPAPLDDGNGYFVAPGIIE--I 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 432 PKDRIMKEEIFGPVLAVYVYPEKQYKDILQLVDTTSpYGLTGAVFAQDKNVIQEARKLLRnaAGNFYINDKSTGAVVAQQ 511
Cdd:cd07125 399 VGIFDLTTEVFGPILHVIRFKAEDLDEAIEDINATG-YGLTLGIHSRDEREIEYWRERVE--AGNLYINRNITGAIVGRQ 475
|
490 500
....*....|....*....|..
gi 1121863746 512 PFGGARASGTNDKPGGRHYILR 533
Cdd:cd07125 476 PFGGWGLSGTGPKAGGPNYLLR 497
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
60-545 |
2.49e-76 |
|
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: 249.09 E-value: 2.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 60 VVGGQEVWTADVRYQLSPYNHAHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAK 139
Cdd:cd07097 4 YIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELE--ARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 140 TMI-GQGKTVIQA--EIDAAaelIDFFRFNAKYAMELEEEQLISVPVSTNSMVYRGLEGFVAAVSPFNF-TAIGGNLAgA 215
Cdd:cd07097 82 LLTrEEGKTLPEArgEVTRA---GQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFpIAIPAWKI-A 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 216 PALM-GNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSEN 294
Cdd:cd07097 158 PALAyGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 295 LDRYRTfprlagECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDpA 374
Cdd:cd07097 238 GARVQL------EMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGD-A 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 375 GDFETFFSAVIDDKSFARIKKWIQHAeTSPNLTILAGG---KCDDKvGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVY 451
Cdd:cd07097 311 LDEGVDIGPVVSERQLEKDLRYIEIA-RSEGAKLVYGGerlKRPDE-GYYLAPALFAGVTNDMRIAREEIFGPVAAVIRV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 452 peKQYKDILQLVDTTsPYGLTGAVFAQDknvIQEARKLLRNA-AGNFYINDKSTGaVVAQQPFGGARASGTNDKPGGRHY 530
Cdd:cd07097 389 --RDYDEALAIANDT-EFGLSAGIVTTS---LKHATHFKRRVeAGVVMVNLPTAG-VDYHVPFGGRKGSSYGPREQGEAA 461
|
490
....*....|....*
gi 1121863746 531 ILRWTspqAIKETHV 545
Cdd:cd07097 462 LEFYT---TIKTVYV 473
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
37-540 |
3.06e-75 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 257.82 E-value: 3.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 37 SLERAALQKALNDLKGKTEAIPCVVGGqevwTADVRYQLSPYNHAHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQD 116
Cdd:PRK11904 533 RSELEPLAAAIAAFLEKQWQAGPIING----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEE 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 117 RAQIFFKAADLLSGpRRAEVLAKTMIGQGKTVIQAeIDAAAELIDFFRFnakYAMEleEEQLISVPVS-------TNSMV 189
Cdd:PRK11904 609 RAAILERAADLLEA-NRAELIALCVREAGKTLQDA-IAEVREAVDFCRY---YAAQ--ARRLFGAPEKlpgptgeSNELR 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 190 YRGLEGFVAaVSPFNFT-AIggnLAG--APALM-GNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDT 265
Cdd:PRK11904 682 LHGRGVFVC-ISPWNFPlAI---FLGqvAAALAaGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAA 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 266 VTSSEHFAGLNFTGSVPTFKRLWKQVSEnldryRTFP--RLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSA 343
Cdd:PRK11904 758 LTADPRIAGVAFTGSTETARIINRTLAA-----RDGPivPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSA 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 344 CSRLYVPDLLWPQIKAKL---LEEhgkIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSPNLtiLAGGKCDD--KV 418
Cdd:PRK11904 833 LRVLFVQEDIADRVIEMLkgaMAE---LKVGDPR-LLSTDVGPVIDAEAKANLDAHIERMKREARL--LAQLPLPAgtEN 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 419 GYFIEPCIVETKDPKDriMKEEIFGPVLAVYVYPEKQYKDILQLVDTTSpYGLTGAVFAQDKNVIQEARKLLRnaAGNFY 498
Cdd:PRK11904 907 GHFVAPTAFEIDSISQ--LEREVFGPILHVIRYKASDLDKVIDAINATG-YGLTLGIHSRIEETADRIADRVR--VGNVY 981
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1121863746 499 INDKSTGAVVAQQPFGGARASGTNDKPGGRHYILRWTSPQAI 540
Cdd:PRK11904 982 VNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
38-533 |
1.82e-73 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 254.09 E-value: 1.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 38 LERAALQKALNDLKGKT-EAIPCVVGgqEVWTADVRYQLSPYNHAHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQD 116
Cdd:COG4230 539 AVLAALSAALAAAAEKQwQAAPLIAG--EAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEE 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 117 RAQIFFKAADLLSGpRRAEVLAKTMIGQGKTvIQaeiDAAAEL---IDFFRFnakYAMELEEEQlisvpvsTNSMVYRGL 193
Cdd:COG4230 617 RAAILERAADLLEA-HRAELMALLVREAGKT-LP---DAIAEVreaVDFCRY---YAAQARRLF-------AAPTVLRGR 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 194 eGFVAAVSPFNFTaiggnLAG-----APALM-GNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVT 267
Cdd:COG4230 682 -GVFVCISPWNFP-----LAIftgqvAAALAaGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALV 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 268 SSEHFAGLNFTGSVPTFKRLWKQVSENLDRYRTFprLAgECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRL 347
Cdd:COG4230 756 ADPRIAGVAFTGSTETARLINRTLAARDGPIVPL--IA-ETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVL 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 348 YVPDllwpQIKAKLLE-------EhgkIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSPNLtiLAGGKCDDKV-- 418
Cdd:COG4230 833 CVQE----DIADRVLEmlkgamaE---LRVGDPA-DLSTDVGPVIDAEARANLEAHIERMRAEGRL--VHQLPLPEECan 902
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 419 GYFIEPCIVETKDPKDriMKEEIFGPVLAVYVYpekQYKDILQLVDT--TSPYGLTGAVFAQDKNVIQEARKLLRnaAGN 496
Cdd:COG4230 903 GTFVAPTLIEIDSISD--LEREVFGPVLHVVRY---KADELDKVIDAinATGYGLTLGVHSRIDETIDRVAARAR--VGN 975
|
490 500 510
....*....|....*....|....*....|....*..
gi 1121863746 497 FYINDKSTGAVVAQQPFGGARASGTNDKPGGRHYILR 533
Cdd:COG4230 976 VYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLR 1012
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
76-521 |
4.89e-68 |
|
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: 226.71 E-value: 4.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 76 SPYnHAHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIGQ-GKTVIQA--E 152
Cdd:cd07149 5 SPY-DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLE--ERREEFARTIALEaGKPIKDArkE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 153 IDAAaelIDFFRFNAKYAMELEEEQ--LISVPVSTNSM--VYRGLEGFVAAVSPFNFTAiggNLAG---APALM-GNVVL 224
Cdd:cd07149 82 VDRA---IETLRLSAEEAKRLAGETipFDASPGGEGRIgfTIREPIGVVAAITPFNFPL---NLVAhkvGPAIAaGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 225 WKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVptfkrlwkQVSENLDRYRTFPRL 304
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSP--------AVGEAIARKAGLKKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 305 AGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAV 384
Cdd:cd07149 228 TLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPL-DEDTDVGPM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 385 IDDKSFARIKKWIQHAETSpNLTILAGGKCDdkvGYFIEPCIVETKDPKDRIMKEEIFGPVlaVYVYPEKQYKDILQLVD 464
Cdd:cd07149 307 ISEAEAERIEEWVEEAVEG-GARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPV--VSLNPFDTLDEAIAMAN 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1121863746 465 tTSPYGLTGAVFAQDKNVIQEARKLLRnaAGNFYINDKSTgAVVAQQPFGGARASGT 521
Cdd:cd07149 381 -DSPYGLQAGVFTNDLQKALKAARELE--VGGVMINDSST-FRVDHMPYGGVKESGT 433
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
79-540 |
1.09e-65 |
|
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: 221.45 E-value: 1.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 79 NHAHK---VAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIGQ-GKTVIQAEID 154
Cdd:cd07131 20 NPADLeevVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLK--KRKEELARLVTREmGKPLAEGRGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 155 AAaELIDFFRFNAKYAMELEEEQLISVPVSTNSMVYRGLEGFVAAVSPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAVL 233
Cdd:cd07131 98 VQ-EAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFpVAIPSWKIFPALVCGNTVVFKPAEDTPA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 234 SSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSenldryRTFPRLAGECGGKNF 313
Cdd:cd07131 177 CALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA------RPNKRVALEMGGKNP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 314 HLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARI 393
Cdd:cd07131 251 IIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGL-DEETDMGPLINEAQLEKV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 394 KKWIQHAEtSPNLTILAGGKCDDK----VGYFIEPCIVETKDPKDRIMKEEIFGPVLAvyVYPEKQYKDILQLVDTTsPY 469
Cdd:cd07131 330 LNYNEIGK-EEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVA--LIEVSSLEEAIEIANDT-EY 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1121863746 470 GLTGAVFAQDKNVIQEARKLLRnaAGNFYINDKSTGAVVaQQPFGGARASGTNDKPGGRHYILRWTSPQAI 540
Cdd:cd07131 406 GLSSAIYTEDVNKAFRARRDLE--AGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGTTALDAFTEWKAV 473
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
96-536 |
9.31e-64 |
|
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: 215.27 E-value: 9.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 96 NKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIGQGKTVIQAEIDAAAELIDFFRFNAKYAMELEE 175
Cdd:cd07150 24 ERAIAAAYDAFPAWAATTPSERERILLKAAEIME--RRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVRG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 176 EQLISVPVSTNSMVYRGLEGFVAAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQF 254
Cdd:cd07150 102 ETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 255 VPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYrtfprlAGECGGKNFHLVHSSADVPTVVNGTLRSAF 334
Cdd:cd07150 182 VTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKI------TLELGGKNPLIVLADADLDYAVRAAAFGAF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 335 EYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAeTSPNLTILAGGKC 414
Cdd:cd07150 256 MHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPR-DPDTVIGPLISPRQVERIKRQVEDA-VAKGAKLLTGGKY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 415 DdkvGYFIEPCIVETKDPKDRIMKEEIFGPVlaVYVYPEKQYKDILQLVDTTSpYGLTGAVFAQDknvIQEARKLLRNA- 493
Cdd:cd07150 334 D---GNFYQPTVLTDVTPDMRIFREETFGPV--TSVIPAKDAEEALELANDTE-YGLSAAILTND---LQRAFKLAERLe 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1121863746 494 AGNFYINDkSTGAVVAQQPFGGARASGTNdKPGGRHYI-----LRWTS 536
Cdd:cd07150 405 SGMVHIND-PTILDEAHVPFGGVKASGFG-REGGEWSMeefteLKWIT 450
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
95-529 |
2.19e-63 |
|
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: 213.93 E-value: 2.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 95 INKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIGQ-GKTVIQAEIDAAAElIDFFRFNAKYAMEL 173
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILE--ERRDEIADWLIREsGSTRPKAAFEVGAA-IAILREAAGLPRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 174 EEEQLISVPVSTNSMVYRGLEGFVAAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPS-DTAVLSSYAVYKILLEAGLPPNV 251
Cdd:cd07104 79 EGEILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDsRTPVTGGLLIAEIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 252 IQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYrtfprlAGECGGKNFHLVHSSADVPTVVNGTLR 331
Cdd:cd07104 159 LNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKV------ALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 332 SAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAeTSPNLTILAG 411
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPR-DPDTVIGPLINERQVDRVHAIVEDA-VAAGARLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 412 GKCDdkvGYFIEPCIVETKDPKDRIMKEEIFGPVlaVYVYPEKQYKDILQLVDTTsPYGLTGAVFAQDknvIQEARKLLR 491
Cdd:cd07104 311 GTYE---GLFYQPTVLSDVTPDMPIFREEIFGPV--APVIPFDDDEEAVELANDT-EYGLSAAVFTRD---LERAMAFAE 381
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1121863746 492 NA-AGNFYINDKST--GAVVaqqPFGGARASGtndkpGGRH 529
Cdd:cd07104 382 RLeTGMVHINDQTVndEPHV---PFGGVKASG-----GGRF 414
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
41-548 |
6.86e-63 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 223.59 E-value: 6.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 41 AALQKALNDLKGKT-EAIPCVVGGQEvwTADVRYQLSPYNHAHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQ 119
Cdd:PRK11905 539 AALDEALNAFAAKTwHAAPLLAGGDV--DGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAA 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 120 IFFKAADLLSGpRRAEVLAKTMIGQGKTVIqaeiDAAAEL---IDFFRFNAKYAMELEEEQlISVPVstnsmvyrgleGF 196
Cdd:PRK11905 617 ILERAADLMEA-HMPELFALAVREAGKTLA----NAIAEVreaVDFLRYYAAQARRLLNGP-GHKPL-----------GP 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 197 VAAVSPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAVLSSYAVyKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFA 273
Cdd:PRK11905 680 VVCISPWNFPlAIfTGQIAAALV-AGNTVLAKPAEqTPLIAARAV-RLLHEAGVPKDALQLLPGDGRTVGAALVADPRIA 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 274 GLNFTGSVPTFKRLWKQVSENLDRYrtfPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLL 353
Cdd:PRK11905 758 GVMFTGSTEVARLIQRTLAKRSGPP---VPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDV 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 354 WPQIKAKL---LEEhgkIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSPNL--TILAGGKCDDkvGYFIEPCIVE 428
Cdd:PRK11905 835 ADRVLTMLkgaMDE---LRIGDPW-RLSTDVGPVIDAEAQANIEAHIEAMRAAGRLvhQLPLPAETEK--GTFVAPTLIE 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 429 TKDPKDriMKEEIFGPVLAVYVYpekQYKDILQLVD--TTSPYGLTGAVFAQDKNVIQEARKLLRnaAGNFYINDKSTGA 506
Cdd:PRK11905 909 IDSISD--LEREVFGPVLHVVRF---KADELDRVIDdiNATGYGLTFGLHSRIDETIAHVTSRIR--AGNIYVNRNIIGA 981
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1121863746 507 VVAQQPFGGARASGTNDKPGGRHYILR------WTSPQAIKETHVPLE 548
Cdd:PRK11905 982 VVGVQPFGGEGLSGTGPKAGGPLYLGRlvreapTPIPPAHESVDTDAA 1029
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
24-538 |
1.85e-62 |
|
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: 213.23 E-value: 1.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 24 EVANEPILEFKPGSLERAALQKalndlkgkTEAIPcVVGGQEVWTADVRYQLSPYNHAHKVAKYCYADKDLINKAINAAV 103
Cdd:TIGR01238 14 DLDNESELKPLEAQIHAWADKT--------WQAAP-IIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 104 AVRREWDLRPIQDRAQIFFKAADLLSgPRRAEVLAKTMIGQGKTVIQAeIDAAAELIDFFRFNAKYAME-LEEEQLISVp 182
Cdd:TIGR01238 85 QAFPTWNATPAKERAAKLDRLADLLE-LHMPELMALCVREAGKTIHNA-IAEVREAVDFCRYYAKQVRDvLGEFSVESR- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 183 vstnsmvyrgleGFVAAVSPFNFT-AI-GGNLAGAPAlMGNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGP 260
Cdd:TIGR01238 162 ------------GVFVCISPWNFPlAIfTGQISAALA-AGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 261 VFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDryRTFPRLAgECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQK 340
Cdd:TIGR01238 229 DVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRED--APVPLIA-ETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 341 CSA----CSRLYVPDLLWPQIKAKLLEehgkIKVGDPaGDFETFFSAVIDDKSFARIKKWIQH----AETSPNLTILAGG 412
Cdd:TIGR01238 306 CSAlrvlCVQEDVADRVLTMIQGAMQE----LKVGVP-HLLTTDVGPVIDAEAKQNLLAHIEHmsqtQKKIAQLTLDDSR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 413 KCDDkvGYFIEPCIVETKDPKDriMKEEIFGPVLAVYVYPEKQYKDILQLVDTTSpYGLTGAVFAQDKNVIQEARKLLRn 492
Cdd:TIGR01238 381 ACQH--GTFVAPTLFELDDIAE--LSEEVFGPVLHVVRYKARELDQIVDQINQTG-YGLTMGVHSRIETTYRWIEKHAR- 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1121863746 493 aAGNFYINDKSTGAVVAQQPFGGARASGTNDKPGGRHYILRWTSPQ 538
Cdd:TIGR01238 455 -VGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
76-520 |
2.39e-62 |
|
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: 211.91 E-value: 2.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 76 SPYNHAHkVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTM-IGQGKTVIQA--E 152
Cdd:cd07094 5 NPYDGEV-IGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLK--KRAEEFAKIIaCEGGKPIKDArvE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 153 IDAAaelIDFFRFNAKYAMELEEEQlISVPVSTNSMVYRGLE-----GFVAAVSPFNFTAiggNLAG---APAL-MGNVV 223
Cdd:cd07094 82 VDRA---IDTLRLAAEEAERIRGEE-IPLDATQGSDNRLAWTirepvGVVLAITPFNFPL---NLVAhklAPAIaTGCPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 224 LWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPtfkrlwkqVSENLDRYRTFPR 303
Cdd:cd07094 155 VLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAA--------VGEALRANAGGKR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 304 LAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDfETFFSA 383
Cdd:cd07094 227 IALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDE-DTDVGP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 384 VIDDKSFARIKKWIQHAETSpNLTILAGGKCDDKVgyfIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLV 463
Cdd:cd07094 306 LISEEAAERVERWVEEAVEA-GARLLCGGERDGAL---FKPTVLEDVPRDTKLSTEETFGPVVPIIRY--DDFEEAIRIA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1121863746 464 DTTsPYGLTGAVFAQDKNVIQEARKLLRnaAGNFYINDkSTGAVVAQQPFGGARASG 520
Cdd:cd07094 380 NST-DYGLQAGIFTRDLNVAFKAAEKLE--VGGVMVND-SSAFRTDWMPFGGVKESG 432
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
75-500 |
6.62e-62 |
|
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: 210.97 E-value: 6.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 75 LSPYNHAhKVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKT-MIGQGKTVIQA-- 151
Cdd:cd07088 18 LNPATGE-VVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIR--ENADELAKLiVEEQGKTLSLArv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 152 EIDAAAeliDFFRFNAKYAMELEEEQLISVPVSTNSMVYRGLEGFVAAVSPFNFTAIggnLAG---APALM-GNVVLWKP 227
Cdd:cd07088 95 EVEFTA---DYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFF---LIArklAPALVtGNTIVIKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 228 SDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLdryrTFPRLagE 307
Cdd:cd07088 169 SEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI----TKVSL--E 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 308 CGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDfETFFSAVIDD 387
Cdd:cd07088 243 LGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDA-ATDMGPLVNE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 388 KSFARIKKWIQHAETSpNLTILAGGKCDD-KVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVyvypeKQYKDILQLVDTT 466
Cdd:cd07088 322 AALDKVEEMVERAVEA-GATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPV-----VKFSSLDEAIELA 395
|
410 420 430
....*....|....*....|....*....|....*.
gi 1121863746 467 --SPYGLTGAVFAQDKNVIQEARKLLRnaAGNFYIN 500
Cdd:cd07088 396 ndSEYGLTSYIYTENLNTAMRATNELE--FGETYIN 429
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
90-521 |
9.64e-62 |
|
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: 210.28 E-value: 9.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 90 ADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTM-IGQGKTVIQA--EIDAAAELidfFRFN 166
Cdd:cd07145 18 LSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIE--RRKEELAKLLtIEVGKPIKQSrvEVERTIRL---FKLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 167 AKYAMELEEEQLIS--VPVSTNSMVYRGLE--GFVAAVSPFNFTAiggNLAG---APAL-MGNVVLWKPSDTAVLSSYAV 238
Cdd:cd07145 93 AEEAKVLRGETIPVdaYEYNERRIAFTVREpiGVVGAITPFNFPA---NLFAhkiAPAIaVGNSVVVKPSSNTPLTAIEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 239 YKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSenldryRTFPRLAGECGGKNFHLVHS 318
Cdd:cd07145 170 AKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG------GTGKKVALELGGSDPMIVLK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 319 SADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQ 398
Cdd:cd07145 244 DADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPL-DESTDLGPLISPEAVERMENLVN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 399 HAETSPNlTILAGGKCDDkvGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYvypekQYKDILQLVD--TTSPYGLTGAVF 476
Cdd:cd07145 323 DAVEKGG-KILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIA-----KVKDDEEAVEiaNSTEYGLQASVF 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1121863746 477 AQDknvIQEARKLLRN-AAGNFYINDkSTGAVVAQQPFGGARASGT 521
Cdd:cd07145 395 TND---INRALKVARElEAGGVVIND-STRFRWDNLPFGGFKKSGI 436
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
75-520 |
8.04e-61 |
|
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: 208.32 E-value: 8.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 75 LSPYNhAHKVAKYCYADKDLINKAINAAvavRR-----EWDLRPIQDRAQIFFKAADLLSgpRRAEVLAK-TMIGQGKTV 148
Cdd:cd07119 18 INPAN-GEVIATVPEGTAEDAKRAIAAA---RRafdsgEWPHLPAQERAALLFRIADKIR--EDAEELARlETLNTGKTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 149 IQAEIDAAaELIDFFRFNAKYAmELEEEQLISVPVSTNSMVYRGLEGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKP 227
Cdd:cd07119 92 RESEIDID-DVANCFRYYAGLA-TKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAaGNTVVIKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 228 SDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENldryrtFPRLAGE 307
Cdd:cd07119 170 SEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN------VKKVALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 308 CGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDD 387
Cdd:cd07119 244 LGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGL-DADTEMGPLVSA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 388 KSFARIKKWIQHAEtSPNLTILAGGK------CDDkvGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYPEKQykDILQ 461
Cdd:cd07119 323 EHREKVLSYIQLGK-EEGARLVCGGKrptgdeLAK--GYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE--EAIR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1121863746 462 LVDTTsPYGLTGAVFAQDKNVIQEARKLLRnaAGNFYINDksTGAVVAQQPFGGARASG 520
Cdd:cd07119 398 LANDT-PYGLAGAVWTKDIARANRVARRLR--AGTVWIND--YHPYFAEAPWGGYKQSG 451
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
90-529 |
3.25e-60 |
|
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: 206.26 E-value: 3.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 90 ADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKT-MIGQGKTVIQA---EIDAAAElidFFRF 165
Cdd:cd07093 16 GGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIE--ARADELALLeSLDTGKPITLArtrDIPRAAA---NFRF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 166 NAKYAMELEEEqliSVPVSTNSMVY--RGLEGFVAAVSPFNFTAIggnLAG---APAL-MGNVVLWKPSDTAVLSSYAVY 239
Cdd:cd07093 91 FADYILQLDGE---SYPQDGGALNYvlRQPVGVAGLITPWNLPLM---LLTwkiAPALaFGNTVVLKPSEWTPLTAWLLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 240 KILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRyrtfprLAGECGGKNFHLVHSS 319
Cdd:cd07093 165 ELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKP------VSLELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 320 ADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPaGDFETFFSAVIDDKSFARIKKWIQH 399
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDP-LDPDTEVGPLISKEHLEKVLGYVEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 400 AEtSPNLTILAGGKCDD----KVGYFIEPCIVETKDPKDRIMKEEIFGPVLAvyVYPEKQYKDILQLVDTTsPYGLTGAV 475
Cdd:cd07093 318 AR-AEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVT--VIPFDDEEEAIELANDT-PYGLAAYV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 476 FAQD-KNVIQEARKLlrnAAGNFYIN-----DKSTgavvaqqPFGGARASGTNdKPGGRH 529
Cdd:cd07093 394 WTRDlGRAHRVARRL---EAGTVWVNcwlvrDLRT-------PFGGVKASGIG-REGGDY 442
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
59-528 |
3.70e-60 |
|
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: 206.65 E-value: 3.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 59 CVVGGQevWTADVRYQLSPYNHAH--KVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEV 136
Cdd:cd07086 1 GVIGGE--WVGSGGETFTSRNPANgePIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALR--KKKEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 137 LAKTM-------IGQGKTVIQAEIDAAaeliDFF-----RFNAK-YAMELEEEQLISV--PVstnsmvyrgleGFVAAVS 201
Cdd:cd07086 77 LGRLVslemgkiLPEGLGEVQEMIDIC----DYAvglsrMLYGLtIPSERPGHRLMEQwnPL-----------GVVGVIT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 202 PFNF-TAIGG-NLAgaPALM-GNVVLWKPSDTAVLSSYAVYKILLEA----GLPPNVIQFVPASGPVfGDTVTSSEHFAG 274
Cdd:cd07086 142 AFNFpVAVPGwNAA--IALVcGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 275 LNFTGSVPTFKRLWKQVSenldryRTFPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLW 354
Cdd:cd07086 219 VSFTGSTEVGRRVGETVA------RRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 355 PQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAEtSPNLTILAGGKCDDKV--GYFIEPCIVETKDP 432
Cdd:cd07086 293 DEFLERLVKAYKQVRIGDPL-DEGTLVGPLINQAAVEKYLNAIEIAK-SQGGTVLTGGKRIDGGepGNYVEPTIVTGVTD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 433 KDRIMKEEIFGPVLavYVYPEKQYKDILQLVDTTsPYGLTGAVFAQDknvIQEARKLLRNA---AGNFYINDKSTGAVVa 509
Cdd:cd07086 371 DARIVQEETFAPIL--YVIKFDSLEEAIAINNDV-PQGLSSSIFTED---LREAFRWLGPKgsdCGIVNVNIPTSGAEI- 443
|
490
....*....|....*....
gi 1121863746 510 QQPFGGARASGtndkpGGR 528
Cdd:cd07086 444 GGAFGGEKETG-----GGR 457
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
84-540 |
7.88e-60 |
|
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: 204.98 E-value: 7.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 84 VAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSGpRRAEVLAKTMIGQGKTVIQAEIDAAAELIDFF 163
Cdd:cd07115 10 IARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILA-NADELARLESLDTGKPIRAARRLDVPRAADTF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 164 RFNAKYAMELEEEqliSVPVSTNSMVYRGLE--GFVAAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLSSYAVYK 240
Cdd:cd07115 89 RYYAGWADKIEGE---VIPVRGPFLNYTVREpvGVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELTPLSALRIAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 241 ILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDryrtfpRLAGECGGKNFHLVHSSA 320
Cdd:cd07115 166 LMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLK------RVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 321 DVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHA 400
Cdd:cd07115 240 DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPL-DPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 401 ETSpNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDTTSpYGLTGAVFAQDk 480
Cdd:cd07115 319 REE-GARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRF--RDEEEALRIANGTE-YGLAAGVWTRD- 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1121863746 481 nvIQEARKLLRNA-AGNFYINdkSTGAVVAQQPFGGARASGTNdKPGGRHYILRWTSPQAI 540
Cdd:cd07115 394 --LGRAHRVAAALkAGTVWIN--TYNRFDPGSPFGGYKQSGFG-REMGREALDEYTEVKSV 449
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
84-520 |
3.97e-59 |
|
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: 203.05 E-value: 3.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 84 VAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTM-IGQGKTVIQA--EIDAAAeli 160
Cdd:cd07103 10 IGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIR--ERAEDLARLLtLEQGKPLAEArgEVDYAA--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 161 DFFRFNAkyameleEE------QLISVPVSTNS-MVYRGLEGFVAAVSPFNFTAigGNLA--GAPAL-MGNVVLWKPSDT 230
Cdd:cd07103 85 SFLEWFA-------EEarriygRTIPSPAPGKRiLVIKQPVGVVAAITPWNFPA--AMITrkIAPALaAGCTVVLKPAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 231 AVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDryrtfpRLAGECGG 310
Cdd:cd07103 156 TPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVK------RVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 311 knfH---LVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDfETFFSAVIDD 387
Cdd:cd07103 230 ---NapfIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDE-GTDMGPLINE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 388 KSFARIKKWIQHAEtSPNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDTTs 467
Cdd:cd07103 306 RAVEKVEALVEDAV-AKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPF--DTEDEVIARANDT- 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1121863746 468 PYGLTGAVFAQD-KNVIQEARKLlrnAAGNFYINdksTGAV-VAQQPFGGARASG 520
Cdd:cd07103 382 PYGLAAYVFTRDlARAWRVAEAL---EAGMVGIN---TGLIsDAEAPFGGVKESG 430
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
84-520 |
6.04e-58 |
|
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: 200.22 E-value: 6.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 84 VAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgPRRAEVLAKTMIGQGKTV--IQAEIDAAAELID 161
Cdd:cd07090 10 LATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLR-ERNDEIARLETIDNGKPIeeARVDIDSSADCLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 162 FFrfnAKYAMELEEEQlisVPVSTNSMVYRGLE--GFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYAV 238
Cdd:cd07090 89 YY---AGLAPTLSGEH---VPLPGGSFAYTRREplGVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSPFTPLTALLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 239 YKILLEAGLPPNVIQFVPASGPVfGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLdRYRTFprlagECGGKNFHLVHS 318
Cdd:cd07090 163 AEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI-KHVTL-----ELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 319 SADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQ 398
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPL-DEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 399 HAETSpNLTILAGG---KCDDKV--GYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYPEKQykDILQLVDTTsPYGLTG 473
Cdd:cd07090 315 SAKQE-GAKVLCGGervVPEDGLenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEE--EVIRRANDT-TYGLAA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1121863746 474 AVFAQDknvIQEA-RKLLRNAAGNFYINdkSTGAVVAQQPFGGARASG 520
Cdd:cd07090 391 GVFTRD---LQRAhRVIAQLQAGTCWIN--TYNISPVEVPFGGYKQSG 433
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
76-520 |
6.76e-58 |
|
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: 199.78 E-value: 6.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 76 SPYNHaHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIGQ-GKTVIQAEID 154
Cdd:cd07147 5 NPYTG-EVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLE--ERFEELAETIVLEaGKPIKDARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 155 AAaELIDFFRFNAKYAMELEEEQLisvPVSTNSMV--YRGL-----EGFVAAVSPFNFTAiggNLAG---APAL-MGNVV 223
Cdd:cd07147 82 VA-RAIDTFRIAAEEATRIYGEVL---PLDISARGegRQGLvrrfpIGPVSAITPFNFPL---NLVAhkvAPAIaAGCPF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 224 LWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVfGDTVTSSEHFAGLNFTGSVPTFkrlWKQVSEnldryrtfpr 303
Cdd:cd07147 155 VLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVG---WDLKAR---------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 304 lAG------ECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPaGDF 377
Cdd:cd07147 221 -AGkkkvvlELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDP-KDD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 378 ETFFSAVIDDKSFARIKKWIQHAeTSPNLTILAGGKCDdkvGYFIEPCIVETKDPKDRIMKEEIFGPVlaVYVYPEKQYK 457
Cdd:cd07147 299 ATDVGPMISESEAERVEGWVNEA-VDAGAKLLTGGKRD---GALLEPTILEDVPPDMEVNCEEVFGPV--VTVEPYDDFD 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1121863746 458 DILQLVDtTSPYGLTGAVFAQDKNVIQEARKLLRnaAGNFYINDKSTGAvVAQQPFGGARASG 520
Cdd:cd07147 373 EALAAVN-DSKFGLQAGVFTRDLEKALRAWDELE--VGGVVINDVPTFR-VDHMPYGGVKDSG 431
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
90-520 |
8.00e-58 |
|
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: 199.29 E-value: 8.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 90 ADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAK--TMiGQGKTVIQA--EIDAAAeliDFFRF 165
Cdd:cd07106 16 ASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIE--ANAEELARllTL-EQGKPLAEAqfEVGGAV---AWLRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 166 NAKyaMELEEEQLISVPVSTNSMVYRGLeGFVAAVSPFNFTAIggnLAG---APALM-GNVVLWKPSDTAVLSSYAVYKI 241
Cdd:cd07106 90 TAS--LDLPDEVIEDDDTRRVELRRKPL-GVVAAIVPWNFPLL---LAAwkiAPALLaGNTVVLKPSPFTPLCTLKLGEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 242 LLEAgLPPNVIQFVPASGPVfGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRyrtfprLAGECGGKNFHLVHSSAD 321
Cdd:cd07106 164 AQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTLKR------VTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 322 VPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDfETFFSAVIDDKSFARIKKWIQHAE 401
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDP-GTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 402 TSpNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLavyvyPEKQYKDILQLVD--TTSPYGLTGAVFAQD 479
Cdd:cd07106 315 AK-GAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVL-----PVLKYSDEDEVIAraNDSEYGLGASVWSSD 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1121863746 480 knvIQEARKL-LRNAAGNFYINdkSTGAVVAQQPFGGARASG 520
Cdd:cd07106 389 ---LERAEAVaRRLEAGTVWIN--THGALDPDAPFGGHKQSG 425
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
95-539 |
1.06e-55 |
|
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: 193.26 E-value: 1.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 95 INKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTmIGQ--GK--TVIQAEIDAAAELIDFfrfNAKYA 170
Cdd:cd07095 2 VDAAVAAARAAFPGWAALSLEERAAILRRFAELLK--ANKEELARL-ISRetGKplWEAQTEVAAMAGKIDI---SIKAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 171 MELEEEQLISVPVSTNSMVYRGLeGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYAVYKILLEAGLPP 249
Cdd:cd07095 76 HERTGERATPMAQGRAVLRHRPH-GVMAVFGPFNFPGHLPNGHIVPALLaGNTVVFKPSELTPAVAELMVELWEEAGLPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 250 NVIQFVPASGPVfGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYrtfprLAGECGGKNFHLVHSSADVPTVVNGT 329
Cdd:cd07095 155 GVLNLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI-----LALEMGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 330 LRSAFEYGGQKCSACSRLYVPDLLWPQ-IKAKLLEEHGKIKVGDPAGDfETFFSAVIDDKSFARIKKWIQHAETSPNLTI 408
Cdd:cd07095 229 VQSAFLTAGQRCTCARRLIVPDGAVGDaFLERLVEAAKRLRIGAPDAE-PPFMGPLIIAAAAARYLLAQQDLLALGGEPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 409 LAGGKCDDKvGYFIEPCIVETKDPKDRiMKEEIFGPVLAVYVYpeKQYKDILQLVDTTsPYGLTGAVFAQDKNVIQEARK 488
Cdd:cd07095 308 LAMERLVAG-TAFLSPGIIDVTDAADV-PDEEIFGPLLQVYRY--DDFDEAIALANAT-RFGLSAGLLSDDEALFERFLA 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1121863746 489 LLRnaAGNFYINDKSTGAVVAqQPFGGARASGtNDKPGGRHYILRWTSPQA 539
Cdd:cd07095 383 RIR--AGIVNWNRPTTGASST-APFGGVGLSG-NHRPSAYYAADYCAYPVA 429
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
98-521 |
1.41e-55 |
|
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: 193.75 E-value: 1.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 98 AINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAktMI-----GQGKTVIQAEIDAAAELIDFFrfnAKYAME 172
Cdd:cd07107 24 AVAAARAAFPEWRATTPLERARMLRELATRLR--EHAEELA--LIdaldcGNPVSAMLGDVMVAAALLDYF---AGLVTE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 173 LEEEqliSVPVSTNSMVYRGLE--GFVAAVSPFN----FTAigGNLAgAPALMGNVVLWKPSDTAVLSSYAVYKILLEAg 246
Cdd:cd07107 97 LKGE---TIPVGGRNLHYTLREpyGVVARIVAFNhplmFAA--AKIA-APLAAGNTVVVKPPEQAPLSALRLAELAREV- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 247 LPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSEnldryrTFPRLAGECGGKNFHLVHSSADVPTVV 326
Cdd:cd07107 170 LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAE------GIKHVTLELGGKNALIVFPDADPEAAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 327 NGTLRSA-FEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSPN 405
Cdd:cd07107 244 DAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPT-DPATTMGPLVSRQQYDRVMHYIDSAKREGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 406 LTILAGGKCDDKV---GYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYPEKQykDILQLVDTTsPYGLTGAVFAQDknV 482
Cdd:cd07107 323 RLVTGGGRPEGPAlegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEA--EMVAQANGV-EYGLTAAIWTND--I 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 1121863746 483 IQEARKLLRNAAGNFYINDKSTGAVVAqqPFGGARASGT 521
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGA--PFGGVKNSGI 434
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
80-520 |
1.60e-55 |
|
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: 193.73 E-value: 1.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 80 HAHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSGprRAEVLAKTM-IGQGKTV-IQAEIDAAA 157
Cdd:cd07108 6 TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEA--RSEELARLLaLETGNALrTQARPEAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 158 eLIDFFRFNAKYAMELEEEqliSVPVSTNSMVYRGLE--GFVAAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLS 234
Cdd:cd07108 84 -LADLFRYFGGLAGELKGE---TLPFGPDVLTYTVREplGVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 235 SYAVYKILLEAgLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSEnldryrtfpRLAG---ECGGK 311
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD---------RLIPvslELGGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 312 NFHLVHSSADVPTVVNGTLRSA-FEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSF 390
Cdd:cd07108 230 SPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPL-DEATDIGAIISEKQF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 391 ARIKKWIQHAETSPNLTILAGGK----CDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAvyVYPEKQYKDILQLVDtT 466
Cdd:cd07108 309 AKVCGYIDLGLSTSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLC--AIPWKDEDEVIAMAN-D 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1121863746 467 SPYGLTGAVFAQD-KNVIQEARKLlrnAAGNFYINdkSTGAVVAQQPFGGARASG 520
Cdd:cd07108 386 SHYGLAAYVWTRDlGRALRAAHAL---EAGWVQVN--QGGGQQPGQSYGGFKQSG 435
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
90-520 |
1.68e-55 |
|
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: 193.96 E-value: 1.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 90 ADKDLINKAINAAVAVRREWDLRPI--QDRAQIFFKAADLLSgpRRAEVLAK-TMIGQGKTV-IQAEIDAAaELIDFFRF 165
Cdd:cd07091 38 ADEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIE--RDRDELAAlESLDNGKPLeESAKGDVA-LSIKCLRY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 166 NAKYAMELEEEqliSVPVSTNSMVYRGLE--GFVAAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLSSYAVYKIL 242
Cdd:cd07091 115 YAGWADKIQGK---TIPIDGNFLAYTRREpiGVCGQIIPWNFPLLMLAWKLAPALaAGNTVVLKPAEQTPLSALYLAELI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 243 LEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSE-NLDRYrTFprlagECGGKNFHLVHSSAD 321
Cdd:cd07091 192 KEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNLKKV-TL-----ELGGKSPNIVFDDAD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 322 VPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAe 401
Cdd:cd07091 266 LDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF-DPDTFQGPQVSKAQFDKILSYIESG- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 402 TSPNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDTTSpYGLTGAVFAQDKN 481
Cdd:cd07091 344 KKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKF--KTEDEVIERANDTE-YGLAAGVFTKDIN 420
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1121863746 482 -VIQEARKLlrnAAGNFYINdkSTGAVVAQQPFGGARASG 520
Cdd:cd07091 421 kALRVSRAL---KAGTVWVN--TYNVFDAAVPFGGFKQSG 455
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
84-540 |
1.79e-55 |
|
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: 194.20 E-value: 1.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 84 VAKYCYADKDLINKAINAA-VAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAK-TMIGQGKTVIQAEIDAAAELID 161
Cdd:cd07113 28 IASVASATEADVDAAVASAwRAFVSAWAKTTPAERGRILLRLADLIE--QHGEELAQlETLCSGKSIHLSRAFEVGQSAN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 162 FFRFNAKYAMELEEEQL-ISVPvSTNSMVYRGLE-----GFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLS 234
Cdd:cd07113 106 FLRYFAGWATKINGETLaPSIP-SMQGERYTAFTrrepvGVVAGIVPWNFSVMIAVWKIGAALAtGCTIVIKPSEFTPLT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 235 SYAVYKILLEAGLPPNVIQFVPASGPVfGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYRTfprlagECGGKNFH 314
Cdd:cd07113 185 LLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTL------ELGGKNAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 315 LVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIK 394
Cdd:cd07113 258 AFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPM-DESVMFGPLANQPHFDKVC 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 395 KWIQHAETSpNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYPEKqyKDILQLVDTTsPYGLTGA 474
Cdd:cd07113 337 SYLDDARAE-GDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDE--EELIQLINDT-PFGLTAS 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1121863746 475 VFAQdkNVIQEARKLLRNAAGNFYINDKSTgaVVAQQPFGGARASGTNdKPGGRHYILRWTSPQAI 540
Cdd:cd07113 413 VWTN--NLSKALRYIPRIEAGTVWVNMHTF--LDPAVPFGGMKQSGIG-REFGSAFIDDYTELKSV 473
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
99-528 |
3.48e-55 |
|
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: 192.82 E-value: 3.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 99 INAAVAVRRE------WDLRPIQDRAQIFFKAADLLSgpRRAEVLAKT-MIGQGKTVIQAEIDAAAELIDFFRFNAKYAM 171
Cdd:cd07112 26 VDRAVAAARRafesgvWSRLSPAERKAVLLRLADLIE--AHRDELALLeTLDMGKPISDALAVDVPSAANTFRWYAEAID 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 172 ELEEEqliSVPVSTN--SMVYRGLEGFVAAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLSSYAVYKILLEAGLP 248
Cdd:cd07112 104 KVYGE---VAPTGPDalALITREPLGVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAEQSPLTALRLAELALEAGLP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 249 PNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSE-NLDRyrtfprLAGECGGKNFHLV-HSSADVPTVV 326
Cdd:cd07112 181 AGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKR------VWLECGGKSPNIVfADAPDLDAAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 327 NGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSpNL 406
Cdd:cd07112 255 EAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPL-DPATRMGALVSEAHFDKVLGYIESGKAE-GA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 407 TILAGGKCDDKV--GYFIEPCIVETKDPKDRIMKEEIFGPVLAvyVYPEKQYKDILQLVDTTsPYGLTGAVFAQDKN-VI 483
Cdd:cd07112 333 RLVAGGKRVLTEtgGFFVEPTVFDGVTPDMRIAREEIFGPVLS--VITFDSEEEAVALANDS-VYGLAASVWTSDLSrAH 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1121863746 484 QEARKLLrnaAGNFYINdkSTGAVVAQQPFGGARASGtndkpGGR 528
Cdd:cd07112 410 RVARRLR---AGTVWVN--CFDEGDITTPFGGFKQSG-----NGR 444
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
75-545 |
1.22e-54 |
|
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: 191.01 E-value: 1.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 75 LSPyNHAHKVAKYCYADKDLINKAINAAvavRRE-----WDLRPIQDRAQIFFKAADLLSgpRRAEVLAKT-MIGQGKTV 148
Cdd:cd07118 2 RSP-AHGVVVARYAEGTVEDVDAAVAAA---RKAfdkgpWPRMSGAERAAVLLKVADLIR--ARRERLALIeTLESGKPI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 149 IQA--EIDAAAELidfFRFNAKYAMELEEEQLISVPVSTNSMVYRGLEGFVAAVSPFNFTA--IGGNLAGAPAlMGNVVL 224
Cdd:cd07118 76 SQArgEIEGAADL---WRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFliLSQKLPFALA-AGCTVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 225 WKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRyrtfprL 304
Cdd:cd07118 152 VKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKK------V 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 305 AGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAV 384
Cdd:cd07118 226 SLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPL-DPETKVGAI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 385 IDDKSFARIKKWIQHAETSPNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVD 464
Cdd:cd07118 305 INEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTF--DTVDEAIALAN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 465 TTsPYGLTGAVFAQD-KNVIQEARKLlrnAAGNFYINDKSTGAvvAQQPFGGARASGtNDKPGGRHYILRWTSpqaIKET 543
Cdd:cd07118 383 DT-VYGLSAGVWSKDiDTALTVARRI---RAGTVWVNTFLDGS--PELPFGGFKQSG-IGRELGRYGVEEYTE---LKTV 452
|
..
gi 1121863746 544 HV 545
Cdd:cd07118 453 HL 454
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
76-520 |
2.97e-54 |
|
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: 190.47 E-value: 2.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 76 SPYNHAhKVAKYCYADKDLINKAI-NAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTM---IGQGKTVIQA 151
Cdd:cd07082 22 SPIDGE-VIGSVPALSALEILEAAeTAYDAGRGWWPTMPLEERIDCLHKFADLLK--ENKEEVANLLmweIGKTLKDALK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 152 EIDAAAELIDFFRFNAKyamELEEEQLISVPVSTNS----MVYRGLEGFVAAVSPFNFTAiggNLAG---APAL-MGNVV 223
Cdd:cd07082 99 EVDRTIDYIRDTIEELK---RLDGDSLPGDWFPGTKgkiaQVRREPLGVVLAIGPFNYPL---NLTVsklIPALiMGNTV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 224 LWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENldryrtfpR 303
Cdd:cd07082 173 VFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMK--------R 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 304 LAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDfETFFSA 383
Cdd:cd07082 245 LVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDN-GVDITP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 384 VIDDKSFARIKKWIQHAEtSPNLTILAGGKcdDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLavyvyPEKQYKDILQLV 463
Cdd:cd07082 324 LIDPKSADFVEGLIDDAV-AKGATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVL-----PIIRVNDIEEAI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1121863746 464 D--TTSPYGLTGAVFAQDKNVIQE-ARKLLrnaAGNFYINDKStgavvaQQ-----PFGGARASG 520
Cdd:cd07082 396 ElaNKSNYGLQASIFTKDINKARKlADALE---VGTVNINSKC------QRgpdhfPFLGRKDSG 451
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
95-542 |
9.18e-54 |
|
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: 188.67 E-value: 9.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 95 INKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgPRRAEVLAKTMIGQGKTVIQA--EIDAAAELIDFFRFNAKYAME 172
Cdd:cd07101 20 VEAAFARARAAQRAWAARPFAERAAVFLRFHDLVL-ERRDELLDLIQLETGKARRHAfeEVLDVAIVARYYARRAERLLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 173 LEEEQLiSVPVSTNSMVYRGLEGFVAAVSPFNF---TAIGGNLagaPALM-GNVVLWKPSDTAVLSSYAVYKILLEAGLP 248
Cdd:cd07101 99 PRRRRG-AIPVLTRTTVNRRPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPDSQTALTALWAVELLIEAGLP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 249 PNVIQFVPASGPVFGDTVTssEHFAGLNFTGSVPTFKRLWKQVSEnldryrtfpRLAG---ECGGKNFHLVHSSADVPTV 325
Cdd:cd07101 175 RDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGR---------RLIGcslELGGKNPMIVLEDADLDKA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 326 VNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGdPAGDFETFFSAVIDDKSFARIKKWIQHAeTSPN 405
Cdd:cd07101 244 AAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLG-AALDYGPDMGSLISQAQLDRVTAHVDDA-VAKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 406 LTILAGGKCDDKVG-YFIEPCIVETKDPKDRIMKEEIFGPVlaVYVYPEKQYKDILQLVDTTsPYGLTGAVFAQDknvIQ 484
Cdd:cd07101 322 ATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPV--VSIYRVADDDEAIELANDT-DYGLNASVWTRD---GA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1121863746 485 EARKLLRN-AAGNFYIND---KSTGAVVAqqPFGGARASGTndkpGGRH---YILRWTSPQAIKE 542
Cdd:cd07101 396 RGRRIAARlRAGTVNVNEgyaAAWASIDA--PMGGMKDSGL----GRRHgaeGLLKYTETQTVAV 454
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
90-520 |
1.95e-53 |
|
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: 188.14 E-value: 1.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 90 ADKDLINKAINAAVAVRR--EWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKT-MIGQGKTViqAEIDA-AAELIDFFRF 165
Cdd:cd07114 16 ASAADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIE--ANAEELAELeTRDNGKLI--RETRAqVRYLAEWYRY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 166 NAKYAMELEEEqliSVPVSTNSM-VYRGLE--GFVAAVSPFN----FTAiggnLAGAPAL-MGNVVLWKPSDTAVLSSYA 237
Cdd:cd07114 92 YAGLADKIEGA---VIPVDKGDYlNFTRREplGVVAAITPWNspllLLA----KKLAPALaAGNTVVLKPSEHTPASTLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 238 VYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYrtfprlAGECGGKNFHLVH 317
Cdd:cd07114 165 LAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPV------TLELGGKSPNIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 318 SSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWI 397
Cdd:cd07114 239 DDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPL-DPETQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 398 QHAEtSPNLTILAGGK----CDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYPEKQykDILQLVDTTsPYGLTG 473
Cdd:cd07114 318 ARAR-EEGARVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEE--EAIALANDS-EYGLAA 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1121863746 474 AVFAQDknviqeARKLLRNA----AGNFYINDKStgAVVAQQPFGGARASG 520
Cdd:cd07114 394 GIWTRD------LARAHRVAraieAGTVWVNTYR--ALSPSSPFGGFKDSG 436
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
61-520 |
1.13e-52 |
|
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: 185.97 E-value: 1.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 61 VGGQEVWTADVryqLSPYNhAHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgPRRAEVLAKT 140
Cdd:cd07151 4 RDGTSERTIDV---LNPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILE-ERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 141 MIGQGKTVIQAEIDAAAElIDFFRFNAKYAMELEEEQLISVPVSTNSMVYRGLEGFVAAVSPFNFTAiggNLAG---APA 217
Cdd:cd07151 79 IRESGSTRIKANIEWGAA-MAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPL---HLSMrsvAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 218 L-MGNVVLWKP-SDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENL 295
Cdd:cd07151 155 LaLGNAVVLKPaSDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 296 DryrtfpRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAg 375
Cdd:cd07151 235 K------KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPS- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 376 DFETFFSAVIDDKSFARIKKWIQHAeTSPNLTILAGGKCDDKVgyfIEPCIVETKDPKDRIMKEEIFGPVlaVYVYPEKQ 455
Cdd:cd07151 308 DPDTVVGPLINESQVDGLLDKIEQA-VEEGATLLVGGEAEGNV---LEPTVLSDVTNDMEIAREEIFGPV--APIIKADD 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1121863746 456 YKDILQLVDTTsPYGLTGAVFAQDknvIQEARKL-LRNAAGNFYINDKStgavVAQQP---FGGARASG 520
Cdd:cd07151 382 EEEALELANDT-EYGLSGAVFTSD---LERGVQFaRRIDAGMTHINDQP----VNDEPhvpFGGEKNSG 442
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
21-533 |
1.46e-50 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 187.49 E-value: 1.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 21 STFEVANEPILefkpGSLERAALQKALNDLKgkteAIPCVvgGQEVWTADVRYQLSPYNHAHKVAKYCYADKDLINKAIN 100
Cdd:PRK11809 620 AGLDLANEHRL----ASLSSALLASAHQKWQ----AAPML--EDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALE 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 101 AAVAVRREWDLRPIQDRAQIFFKAADLLsgprraEVLAKTMIG-----QGKTVIQAeIDAAAELIDFFRFnakYAMELEE 175
Cdd:PRK11809 690 SAVNAAPIWFATPPAERAAILERAADLM------EAQMQTLMGllvreAGKTFSNA-IAEVREAVDFLRY---YAGQVRD 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 176 EqlisvpvSTNSMvYRGLeGFVAAVSPFNFT-AI-GGNLAGAPAlMGNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQ 253
Cdd:PRK11809 760 D-------FDNDT-HRPL-GPVVCISPWNFPlAIfTGQVAAALA-AGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQ 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 254 FVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLD-RYRTFPRLAgECGGKNFHLVHSSADVPTVVNGTLRS 332
Cdd:PRK11809 830 LLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDpQGRPIPLIA-ETGGQNAMIVDSSALTEQVVADVLAS 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 333 AFEYGGQKCSA----CSRLYVPDLLWPQIKAKLLEehgkIKVGDPaGDFETFFSAVIDDKSFARIKKWIQhAETSPNLTI 408
Cdd:PRK11809 909 AFDSAGQRCSAlrvlCLQDDVADRTLKMLRGAMAE----CRMGNP-DRLSTDIGPVIDAEAKANIERHIQ-AMRAKGRPV 982
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 409 L---AGGKCDDKVGYFIEPCIVETkDPKDRiMKEEIFGPVLAVYVYPEKQYKDILQLVDTTSpYGLTGAVFAQ-DKN--- 481
Cdd:PRK11809 983 FqaaRENSEDWQSGTFVPPTLIEL-DSFDE-LKREVFGPVLHVVRYNRNQLDELIEQINASG-YGLTLGVHTRiDETiaq 1059
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1121863746 482 VIQEARkllrnaAGNFYINDKSTGAVVAQQPFGGARASGTNDKPGGRHYILR 533
Cdd:PRK11809 1060 VTGSAH------VGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYR 1105
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
97-545 |
2.28e-50 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 181.23 E-value: 2.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 97 KAINAAVAVRREWDLRPIQDRAQIFFKAADLLSGpRRAEVLaktmigqgkTVIQAEI-----DAAAELIDFF---RFNAK 168
Cdd:PRK09407 58 AAFARARAAQRAWAATPVRERAAVLLRFHDLVLE-NREELL---------DLVQLETgkarrHAFEEVLDVAltaRYYAR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 169 YAMELEEEQLIS--VPVSTNSMVYRGLEGFVAAVSPFNF---TAIGGNLagaPALM-GNVVLWKP-SDTAvLSSYAVYKI 241
Cdd:PRK09407 128 RAPKLLAPRRRAgaLPVLTKTTELRQPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPdSQTP-LTALAAVEL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 242 LLEAGLPPNVIQFVPASGPVFGDTVTssEHFAGLNFTGSVPTFKRLWKQVSEnldryrtfpRLAG---ECGGKNFHLVHS 318
Cdd:PRK09407 204 LYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGR---------RLIGfslELGGKNPMIVLD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 319 SADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGdPAGDFETFFSAVIDDKSFARIKKWIQ 398
Cdd:PRK09407 273 DADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLG-AGYDYSADMGSLISEAQLETVSAHVD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 399 HAeTSPNLTILAGGKCDDKVG-YFIEPCIVETKDPKDRIMKEEIFGPVlaVYVYPEKQYKDILQLVDTTsPYGLTGAVFA 477
Cdd:PRK09407 352 DA-VAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPV--VSVYPVADVDEAVERANDT-PYGLNASVWT 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1121863746 478 QDKnviQEARKL-LRNAAGNFYIND------KSTGAvvaqqPFGGARASGTndkpGGRH---YILRWTSPQAIKETHV 545
Cdd:PRK09407 428 GDT---ARGRAIaARIRAGTVNVNEgyaaawGSVDA-----PMGGMKDSGL----GRRHgaeGLLKYTESQTIATQRV 493
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
90-520 |
3.12e-50 |
|
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: 179.36 E-value: 3.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 90 ADKDLINKAINAAvavRR---EWD-LRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIGQ-GKTVIQAEIDAAAELIDFFR 164
Cdd:cd07089 16 AGAADVDAAIAAA---RRafdTGDwSTDAEERARCLRQLHEALE--ARKEELRALLVAEvGAPVMTARAMQVDGPIGHLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 165 FNAKYAMELEEEQLISVPVS----TNSMVYRGLEGFVAAVSPFNFtAIGGNLAG-APAL-MGNVVLWKPSDTAVLSSYAV 238
Cdd:cd07089 91 YFADLADSFPWEFDLPVPALrggpGRRVVRREPVGVVAAITPWNF-PFFLNLAKlAPALaAGNTVVLKPAPDTPLSALLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 239 YKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRyrtfprLAGECGGKNFHLVHS 318
Cdd:cd07089 170 GEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKR------VLLELGGKSANIVLD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 319 SADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQ 398
Cdd:cd07089 244 DADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPA-DPGTVMGPLISAAQRDRVEGYIA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 399 HAETSpNLTILAGGKCDDK--VGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYvypekQYKDILQLVD--TTSPYGLTGA 474
Cdd:cd07089 323 RGRDE-GARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVI-----PYDDDDEAVRiaNDSDYGLSGG 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1121863746 475 VFAQDKN-VIQEARKlLRnaAGNFYINdkSTGAVVAQQPFGGARASG 520
Cdd:cd07089 397 VWSADVDrAYRVARR-IR--TGSVGIN--GGGGYGPDAPFGGYKQSG 438
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
96-529 |
4.75e-48 |
|
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: 173.46 E-value: 4.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 96 NKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIGQGKTVIQAEIDAAAEL-IDFFRFNAKYAMELE 174
Cdd:cd07138 39 DRAVAAARRAFPAWSATSVEERAALLERIAEAYE--ARADELAQAITLEMGAPITLARAAQVGLgIGHLRAAADALKDFE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 175 EEQLISvpvstNSMVYRGLEGFVAAVSPFNFTA--IGGNLAgaPALM-GNVVLWKPSDTAVLSSYAVYKILLEAGLPPNV 251
Cdd:cd07138 117 FEERRG-----NSLVVREPIGVCGLITPWNWPLnqIVLKVA--PALAaGCTVVLKPSEVAPLSAIILAEILDEAGLPAGV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 252 IQFVPASGPVFGDTVTSSEHFAGLNFTGSVptfkRLWKQVSENLDRyrTFPRLAGECGGKNFHLVHSSADVPTVVNGTLR 331
Cdd:cd07138 190 FNLVNGDGPVVGEALSAHPDVDMVSFTGST----RAGKRVAEAAAD--TVKRVALELGGKSANIILDDADLEKAVPRGVA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 332 SAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSpNLTILAG 411
Cdd:cd07138 264 ACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPR-DPATTLGPLASAAQFDRVQGYIQKGIEE-GARLVAG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 412 GkcDDK-----VGYFIEPCIVETKDPKDRIMKEEIFGPVLAvyVYPekqYKDILQLV----DTtsPYGLTGAVFAQDKNV 482
Cdd:cd07138 342 G--PGRpegleRGYFVKPTVFADVTPDMTIAREEIFGPVLS--IIP---YDDEDEAIaianDT--PYGLAGYVWSADPER 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1121863746 483 IQEARKLLRnaAGNFYINDkstGAVVAQQPFGGARASGtNDKPGGRH 529
Cdd:cd07138 413 ARAVARRLR--AGQVHING---AAFNPGAPFGGYKQSG-NGREWGRY 453
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
95-520 |
2.97e-47 |
|
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: 171.26 E-value: 2.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 95 INKAINAAVAV--RREWDLRPIQdRAQIFFKAADLLSgpRRAEVLAKTM-IGQGKTVIQAEIDAAAeLIDFFRFNAKYAM 171
Cdd:cd07109 21 VDRAVQAARRAfeSGWLRLSPAE-RGRLLLRIARLIR--EHADELARLEsLDTGKPLTQARADVEA-AARYFEYYGGAAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 172 ELEEEqliSVPVSTNSMVYRGLE--GFVAAVSPFNFTA-IGGNLAgAPAL-MGNVVLWKPSDTAVLSSYAVYKILLEAGL 247
Cdd:cd07109 97 KLHGE---TIPLGPGYFVYTVREphGVTGHIIPWNYPLqITGRSV-APALaAGNAVVVKPAEDAPLTALRLAELAEEAGL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 248 PPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENldryrtFPRLAGECGGKNFHLVHSSADVPTVVN 327
Cdd:cd07109 173 PAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEN------VVPVTLELGGKSPQIVFADADLEAALP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 328 GTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDFEtfFSAVIDDKSFARIKKWIQHAETSpNLT 407
Cdd:cd07109 247 VVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPD--LGPLISAKQLDRVEGFVARARAR-GAR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 408 ILAGG---KCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYPEKQykDILQLVDTTSpYGLTGAVFAQDKNV-I 483
Cdd:cd07109 324 IVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEA--EAIALANGTD-YGLVAGVWTRDGDRaL 400
|
410 420 430
....*....|....*....|....*....|....*..
gi 1121863746 484 QEARKLLrnaAGNFYINDKSTGAVVaQQPFGGARASG 520
Cdd:cd07109 401 RVARRLR---AGQVFVNNYGAGGGI-ELPFGGVKKSG 433
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
89-528 |
7.20e-47 |
|
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: 169.78 E-value: 7.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 89 YADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIGQGKTVI---QAEIDAAAElidFFRF 165
Cdd:cd07152 9 VADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLE--EHADEIADWIVRESGSIRpkaGFEVGAAIG---ELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 166 NAKYAMELEEEQLISVPVSTnSMVYRGLEGFVAAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPS-DTAVLSSYAVYKILL 243
Cdd:cd07152 84 AAGLPTQPQGEILPSAPGRL-SLARRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDpRTPVSGGVVIARLFE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 244 EAGLPPNVIQFVPAsGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRyrtfprLAGECGGKNFHLVHSSADVP 323
Cdd:cd07152 163 EAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKK------VSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 324 TVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDfETFFSAVIDDKSFARIKKWIQhAETS 403
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATG-QVALGPLINARQLDRVHAIVD-DSVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 404 PNLTILAGGKCDdkvGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDTTsPYGLTGAVFAQDknvI 483
Cdd:cd07152 314 AGARLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVF--DSDEEAVALANDT-EYGLSAGIISRD---V 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1121863746 484 QEARKL---LRnaAGNFYINDKsTGAVVAQQPFGGARASGTNDKPGGR 528
Cdd:cd07152 385 GRAMALadrLR--TGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
89-500 |
8.20e-45 |
|
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: 164.34 E-value: 8.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 89 YADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIGQ-GKTVIQA--EIDAAAELIDFFrf 165
Cdd:cd07102 14 LASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLA--ANTDEIAEELTWQmGRPIAQAggEIRGMLERARYM-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 166 nakyaMELEEEQLISVPVS-----TNSMVYRGLeGFVAAVSPFN---FTAIGgnlAGAPALM-GNVVLWKPSDTAVLSSY 236
Cdd:cd07102 90 -----ISIAEEALADIRVPekdgfERYIRREPL-GVVLIIAPWNypyLTAVN---AVIPALLaGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 237 AVYKILLEAGLPPNVIQFVPASGPVfGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENldryrtFPRLAGECGGKNFHLV 316
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGR------FIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 317 HSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKW 396
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPL-DPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 397 IQHAetspnltILAGGK---------CDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYvypeKQYKD---ILQLVD 464
Cdd:cd07102 313 IADA-------IAKGARalidgalfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIM----KVKSDaeaIALMND 381
|
410 420 430
....*....|....*....|....*....|....*..
gi 1121863746 465 ttSPYGLTGAVFAQDknvIQEARKLLRN-AAGNFYIN 500
Cdd:cd07102 382 --SEYGLTASVWTKD---IARAEALGEQlETGTVFMN 413
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
84-540 |
2.19e-44 |
|
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: 163.16 E-value: 2.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 84 VAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIG-QGKTVIQA--EIDAAAELI 160
Cdd:cd07099 9 LGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALA--DHADELAELLHAeTGKPRADAglEVLLALEAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 161 DFFRFNAKYAMELEEEQLISV-PVSTNSMVYRGLeGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYAV 238
Cdd:cd07099 87 DWAARNAPRVLAPRKVPTGLLmPNKKATVEYRPY-GVVGVISPWNYPLLTPMGDIIPALAaGNAVVLKPSEVTPLVGELL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 239 YKILLEAGLPPNVIQFVPASGPVfGDTVTSSEHfAGLNFTGSVPTFKRLWKQVSENLdryrtFPRLAgECGGKNFHLVHS 318
Cdd:cd07099 166 AEAWAAAGPPQGVLQVVTGDGAT-GAALIDAGV-DKVAFTGSVATGRKVMAAAAERL-----IPVVL-ELGGKDPMIVLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 319 SADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGdFETFFSAVIDDKSFARIKKWIQ 398
Cdd:cd07099 238 DADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDI-GDADIGPMTTARQLDIVRRHVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 399 HAeTSPNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYPekqykDILQLVDTT--SPYGLTGAVF 476
Cdd:cd07099 317 DA-VAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVA-----DEDEAIALAndSRYGLSASVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1121863746 477 AQDKNVIQE-ARKLlrnAAGNFYINDKSTGAVVAQQPFGGARASGtndkpGGRHY----ILRWTSPQAI 540
Cdd:cd07099 391 SRDLARAEAiARRL---EAGAVSINDVLLTAGIPALPFGGVKDSG-----GGRRHgaegLREFCRPKAI 451
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
90-520 |
3.31e-44 |
|
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: 163.47 E-value: 3.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 90 ADKDLINKAINAA-VAVRREWDLR-PIQDRAQIFFKAADLLSgpRRAEVLAKT-MIGQGKTVIQAEIDAAAELIDFFRFN 166
Cdd:cd07143 41 ATEADVDIAVEVAhAAFETDWGLKvSGSKRGRCLSKLADLME--RNLDYLASIeALDNGKTFGTAKRVDVQASADTFRYY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 167 AKYAmELEEEQLISVPVSTNSMVYRGLEGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYAVYKILLEA 245
Cdd:cd07143 119 GGWA-DKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAaGNTIVLKPSELTPLSALYMTKLIPEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 246 GLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENldryrTFPRLAGECGGKNFHLVHSSADVPTV 325
Cdd:cd07143 198 GFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS-----NLKKVTLELGGKSPNIVFDDADLESA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 326 VNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDfETFFSAVIDDKSFARIKKWIQHAETSPN 405
Cdd:cd07143 273 VVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAE-DTFQGPQVSQIQYERIMSYIESGKAEGA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 406 LTILAGGKCDDKvGYFIEPCIVETKDPKDRIMKEEIFGPVLAVyvypeKQYKDILQLVD--TTSPYGLTGAVFAQD-KNV 482
Cdd:cd07143 352 TVETGGKRHGNE-GYFIEPTIFTDVTEDMKIVKEEIFGPVVAV-----IKFKTEEEAIKraNDSTYGLAAAVFTNNiNNA 425
|
410 420 430
....*....|....*....|....*....|....*...
gi 1121863746 483 IQEARKLlrnAAGNFYINDKSTgaVVAQQPFGGARASG 520
Cdd:cd07143 426 IRVANAL---KAGTVWVNCYNL--LHHQVPFGGYKQSG 458
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
88-520 |
7.07e-44 |
|
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: 161.74 E-value: 7.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 88 CYAD--KDLINKAINAAVAVRRE--WDLRPiQDRAQIFFKAADLLSgpRRAEVLAKTM-IGQGKTVIQA--EIDAAAELI 160
Cdd:cd07120 12 TYADggVAEAEAAIAAARRAFDEtdWAHDP-RLRARVLLELADAFE--ANAERLARLLaLENGKILGEArfEISGAISEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 161 DFF----RFNAKYAMELEEEQLisvpvstnSMVYRGLEGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSS 235
Cdd:cd07120 89 RYYaglaRTEAGRMIEPEPGSF--------SLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAaGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 236 YAVYKILLEA-GLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLwkqvseNLDRYRTFPRLAGECGGKNFH 314
Cdd:cd07120 161 AAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAI------MAAAAPTLKRLGLELGGKTPC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 315 LVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGdPAGDFETFFSAVIDDKSFARIK 394
Cdd:cd07120 235 IVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVG-PGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 395 KWIQHAETSPNLTILAGGKCDDKV--GYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYPEKqyKDILQLVDTTSpYGLT 472
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEGLakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDE--AEAVALANDTD-YGLA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1121863746 473 GAVFAQDKN-VIQEARKLlrnAAGNFYINDKstGAVVAQQPFGGARASG 520
Cdd:cd07120 391 ASVWTRDLArAMRVARAI---RAGTVWINDW--NKLFAEAEEGGYRQSG 434
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
61-520 |
1.23e-43 |
|
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: 161.74 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 61 VGGQevWTADVRYQ----LSPYNhAHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEV 136
Cdd:cd07559 5 INGE--WVAPSKGEyfdnYNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIE--ENLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 137 LAKT-MIGQGKTV---IQAEIDAAaelIDFFRFNAKyAMELEEEQLISVPVSTNSMVYRGLEGFVAAVSPFNFTAIGGNL 212
Cdd:cd07559 80 LAVAeTLDNGKPIretLAADIPLA---IDHFRYFAG-VIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 213 AGAPALM-GNVVLWKPSDTAVLSSYAVYKILLEAgLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQV 291
Cdd:cd07559 156 KLAPALAaGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 292 SENLdryrtFPrLAGECGGKNFHLVHSSADVPT------VVNGTLRSAFEYGgQKCSACSRLYVPDLLWPQIKAKLLEEH 365
Cdd:cd07559 235 AENL-----IP-VTLELGGKSPNIFFDDAMDADddfddkAEEGQLGFAFNQG-EVCTCPSRALVQESIYDEFIERAVERF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 366 GKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSpNLTILAGGK----CDDKVGYFIEPCIVETKDPKDRIMKEEI 441
Cdd:cd07559 308 EAIKVGNPL-DPETMMGAQVSKDQLEKILSYVDIGKEE-GAEVLTGGErltlGGLDKGYFYEPTLIKGGNNDMRIFQEEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 442 FGPVLAVYVYpeKQYKDILQLVDTTsPYGLTGAVFAQDknvIQEARKLLRN-AAGNFYINdkSTGAVVAQQPFGGARASG 520
Cdd:cd07559 386 FGPVLAVITF--KDEEEAIAIANDT-EYGLGGGVWTRD---INRALRVARGiQTGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
95-521 |
4.02e-43 |
|
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: 159.80 E-value: 4.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 95 INKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIGQ-GKTVIQAEIDAAAELIDFFRFNAKYAMEL 173
Cdd:cd07092 21 VDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIE--ENAEELAALESRNtGKPLHLVRDDELPGAVDNFRFFAGAARTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 174 EEEQLISVPVSTNSMVYRGLEGFVAAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLSSYAVYKILLEaGLPPNVI 252
Cdd:cd07092 99 EGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPLTTLLLAELAAE-VLPPGVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 253 QFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRyrtfprLAGECGGKNFHLVHSSADVPTVVNGTLRS 332
Cdd:cd07092 178 NVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKR------VHLELGGKAPVIVFDDADLDAAVAGIATA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 333 AFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDfETFFSAVIDDKSFARIKKWIqhAETSPNLTILAGG 412
Cdd:cd07092 252 GYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDE-DTEMGPLNSAAQRERVAGFV--ERAPAHARVLTGG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 413 KCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVyvypeKQYKDILQLVD--TTSPYGLTGAVFAQDKNVIQEARKLL 490
Cdd:cd07092 329 RRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTV-----QPFDDEDEAIElaNDVEYGLASSVWTRDVGRAMRLSARL 403
|
410 420 430
....*....|....*....|....*....|.
gi 1121863746 491 RnaAGNFYINDKstGAVVAQQPFGGARASGT 521
Cdd:cd07092 404 D--FGTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
84-520 |
4.40e-43 |
|
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: 160.27 E-value: 4.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 84 VAKYCYADKDLINKAINAA-VAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLA--KTMiGQGKTVIQAEIDAAAELI 160
Cdd:cd07144 36 IASVYAAGEEDVDKAVKAArKAFESWWSKVTGEERGELLDKLADLVE--KNRDLLAaiEAL-DSGKPYHSNALGDLDEII 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 161 DFFRFNAKYAMELEEEqliSVPVSTNSMVYRGLE--GFVAAVSPFNFTAiggNLAG---APALM-GNVVLWKPSDTAVLS 234
Cdd:cd07144 113 AVIRYYAGWADKIQGK---TIPTSPNKLAYTLHEpyGVCGQIIPWNYPL---AMAAwklAPALAaGNTVVIKPAENTPLS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 235 SYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDryrtfpRLAGECGGKNFH 314
Cdd:cd07144 187 LLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLK------AVTLECGGKSPA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 315 LVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDllwpQIKAKLLE---EHGK--IKVGDPAGDfETFFSAVIDDKS 389
Cdd:cd07144 261 LVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQE----SIYDKFVEkfvEHVKqnYKVGSPFDD-DTVVGPQVSKTQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 390 FARIKKWIQHAETSpNLTILAGG---KCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDTT 466
Cdd:cd07144 336 YDRVLSYIEKGKKE-GAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKF--KTYEEAIKKANDT 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1121863746 467 sPYGLTGAVFAQDknvIQEARKLLRN-AAGNFYINdkSTGAVVAQQPFGGARASG 520
Cdd:cd07144 413 -TYGLAAAVFTKD---IRRAHRVARElEAGMVWIN--SSNDSDVGVPFGGFKMSG 461
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
95-520 |
1.35e-42 |
|
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: 157.62 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 95 INKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIGQ-GKTVIQA--EIDAAAELIDFFrfnAKYAM 171
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLR--ERKDELARLITLEmGKPIAEAraEVEKCAWICRYY---AENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 172 ELEEEQLISVPVSTNSMVYRGLeGFVAAVSPFNFT-------AiggnlagAPALM-GNVVLWKPSDTAVLSSYAVYKILL 243
Cdd:cd07100 76 AFLADEPIETDAGKAYVRYEPL-GVVLGIMPWNFPfwqvfrfA-------APNLMaGNTVLLKHASNVPGCALAIEELFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 244 EAGLPPNVIQFVPASGPVFgDTVTSSEHFAGLNFTGSVptfkRLWKQVSEnldryrtfprLAG--------ECGGKNFHL 315
Cdd:cd07100 148 EAGFPEGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSE----RAGRAVAA----------EAGknlkksvlELGGSDPFI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 316 VHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFF----SAVIDDKSFA 391
Cdd:cd07100 213 VLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPM-DEDTDLgplaRKDLRDELHE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 392 RIKKWIQH-AetspnlTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVypekqYKDILQLVD--TTSP 468
Cdd:cd07100 292 QVEEAVAAgA------TLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIK-----VKDEEEAIAlaNDSP 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1121863746 469 YGLTGAVFAQDKNVIQE-ARKLlrnAAGNFYINDKSTGAvvAQQPFGGARASG 520
Cdd:cd07100 361 FGLGGSVFTTDLERAERvARRL---EAGMVFINGMVKSD--PRLPFGGVKRSG 408
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
92-531 |
1.76e-42 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 159.09 E-value: 1.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 92 KDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTM-IGQGKTVIQA--EIDAAAELIDFFRFNAK 168
Cdd:PLN02278 61 RAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLII--ANKEDLAQLMtLEQGKPLKEAigEVAYGASFLEYFAEEAK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 169 YAMEleeeQLISVPVSTNSM-VYRGLEGFVAAVSPFNFTaiggnLA-----GAPALM-GNVVLWKPSDTAVLSSYAVYKI 241
Cdd:PLN02278 139 RVYG----DIIPSPFPDRRLlVLKQPVGVVGAITPWNFP-----LAmitrkVGPALAaGCTVVVKPSELTPLTALAAAEL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 242 LLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSEnldryrTFPRLAGECGGKNFHLVHSSAD 321
Cdd:PLN02278 210 ALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAA------TVKRVSLELGGNAPFIVFDDAD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 322 VPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDFETfFSAVIDDKSFARIKKWIQHAe 401
Cdd:PLN02278 284 LDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVT-QGPLINEAAVQKVESHVQDA- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 402 TSPNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDTTSpYGLTGAVFAQD-K 480
Cdd:PLN02278 362 VSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRF--KTEEEAIAIANDTE-AGLAAYIFTRDlQ 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1121863746 481 NVIQEARKLLRNAAGnfyINDKSTGAVVAqqPFGGARASGTNdKPGGRHYI 531
Cdd:PLN02278 439 RAWRVSEALEYGIVG---VNEGLISTEVA--PFGGVKQSGLG-REGSKYGI 483
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
83-521 |
2.11e-42 |
|
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: 158.28 E-value: 2.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 83 KVAKYCYADKDLINKAINAAVAVRR---EWDLRPIQDRAQIFFKAADLLSGPRRAEVLAKTMIGqGKTVIQAEIDAAAEL 159
Cdd:cd07141 34 KICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDN-GKPFSKSYLVDLPGA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 160 IDFFRFNAKYAMELEEEqliSVPVSTNSMVYRGLE--GFVAAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLSSY 236
Cdd:cd07141 113 IKVLRYYAGWADKIHGK---TIPMDGDFFTYTRHEpvGVCGQIIPWNFPLLMAAWKLAPALaCGNTVVLKPAEQTPLTAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 237 AVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTfKRLWKQVS--ENLDryrtfpRLAGECGGKNFH 314
Cdd:cd07141 190 YLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV-GKLIQQAAgkSNLK------RVTLELGGKSPN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 315 LVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIK 394
Cdd:cd07141 263 IVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPF-DPKTEQGPQIDEEQFKKIL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 395 KWIQHAETSpNLTILAGGKCDDKVGYFIEPCIVetKDPKD--RIMKEEIFGPVLAVYvypekQYKDILQLVD--TTSPYG 470
Cdd:cd07141 342 ELIESGKKE-GAKLECGGKRHGDKGYFIQPTVF--SDVTDdmRIAKEEIFGPVQQIF-----KFKTIDEVIEraNNTTYG 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1121863746 471 LTGAVFAQDKNVIQEARKLLRnaAGNFYINdkSTGAVVAQQPFGGARASGT 521
Cdd:cd07141 414 LAAAVFTKDIDKAITFSNALR--AGTVWVN--CYNVVSPQAPFGGYKMSGN 460
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
95-520 |
3.55e-42 |
|
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: 157.13 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 95 INKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSGpRRAEVLAKTMIGQGKTVIQAEIDAAaELIDFFRFNAKYAMELE 174
Cdd:cd07110 21 VDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRE-RREELAELEARDNGKPLDEAAWDVD-DVAGCFEYYADLAEQLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 175 EEQLISVPVSTNSM---VYRGLEGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYAVYKILLEAGLPPN 250
Cdd:cd07110 99 AKAERAVPLPSEDFkarVRREPVGVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSELTSLTELELAEIAAEAGLPPG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 251 VIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRyrtfprLAGECGGKNFHLVHSSADVPTVVNGTL 330
Cdd:cd07110 179 VLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKP------VSLELGGKSPIIVFDDADLEKAVEWAM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 331 RSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDfETFFSAVIDDKSFARIKKWIQHAEtSPNLTILA 410
Cdd:cd07110 253 FGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEE-GVRLGPLVSQAQYEKVLSFIARGK-EEGARLLC 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 411 GGKCDD--KVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDtTSPYGLTGAVFAQDKNVIQEARK 488
Cdd:cd07110 331 GGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSF--ATEDEAIALAN-DSEYGLAAAVISRDAERCDRVAE 407
|
410 420 430
....*....|....*....|....*....|..
gi 1121863746 489 LLRnaAGNFYINdkSTGAVVAQQPFGGARASG 520
Cdd:cd07110 408 ALE--AGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
84-520 |
4.58e-42 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 157.38 E-value: 4.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 84 VAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIGQ-GK---TVIQAEIDAAAEL 159
Cdd:PRK13473 30 LAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIE--ENADEFARLESLNcGKplhLALNDEIPAIVDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 160 IDFF-----RFNAKYAMELEEEQlisvpvstNSMVYRGLEGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVL 233
Cdd:PRK13473 108 FRFFagaarCLEGKAAGEYLEGH--------TSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAaGNTVVLKPSEITPL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 234 SSYAVYKILLEAgLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYRTfprlagECGGKNF 313
Cdd:PRK13473 180 TALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHL------ELGGKAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 314 HLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARI 393
Cdd:PRK13473 253 VIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD-DEDTELGPLISAAHRDRV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 394 KKWIQHAETSPNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYPEKQykDILQLVDtTSPYGLTG 473
Cdd:PRK13473 332 AGFVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED--QAVRWAN-DSDYGLAS 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1121863746 474 AVFAQDknvIQEARKLLRN-AAGNFYINDKSTgaVVAQQPFGGARASG 520
Cdd:PRK13473 409 SVWTRD---VGRAHRVSARlQYGCTWVNTHFM--LVSEMPHGGQKQSG 451
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
90-526 |
4.70e-42 |
|
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: 157.27 E-value: 4.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 90 ADKDLINKAINAAVAVRRE--WDLRPIQDRAQIFFKAADLLSgpRRAEVLAK-TMIGQGKTVIQAEIDAAAELIDFFRFN 166
Cdd:cd07142 38 GDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLE--KHADELAAlETWDNGKPYEQARYAEVPLAARLFRYY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 167 AKYAMELEEEqliSVPVSTNSMVYRGLE--GFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYAVYKILL 243
Cdd:cd07142 116 AGWADKIHGM---TLPADGPHHVYTLHEpiGVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEQTPLSALLAAKLAA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 244 EAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYRTFprlagECGGKNFHLVHSSADVP 323
Cdd:cd07142 193 EAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSNLKPVTL-----ELGGKSPFIVCEDADVD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 324 TVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPagdfetFFSAV-----IDDKSFARIKKWIQ 398
Cdd:cd07142 268 KAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDP------FRKGVeqgpqVDKEQFEKILSYIE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 399 HAETSpNLTILAGGKCDDKVGYFIEPCIVetKDPKD--RIMKEEIFGPVLAVYVYpeKQYKDILQLVDTTSpYGLTGAVF 476
Cdd:cd07142 342 HGKEE-GATLITGGDRIGSKGYYIQPTIF--SDVKDdmKIARDEIFGPVQSILKF--KTVDEVIKRANNSK-YGLAAGVF 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1121863746 477 AQDKNVIQEARKLLRnaAGNFYINdkSTGAVVAQQPFGGARASGTNDKPG 526
Cdd:cd07142 416 SKNIDTANTLSRALK--AGTVWVN--CYDVFDASIPFGGYKMSGIGREKG 461
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
133-520 |
6.38e-42 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 155.66 E-value: 6.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 133 RAEVLAKTMIG-QGKTVIQAEIDAAAElIDFFRFNAKYAMELEEEQLISVPVSTNSMVYRGLEGFVAAVSPFNFT--AIG 209
Cdd:PRK10090 11 RASEISALIVEeGGKIQQLAEVEVAFT-ADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPffLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 210 GNLAgaPALM-GNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLW 288
Cdd:PRK10090 90 RKMA--PALLtGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 289 KQVSENLdryrtfPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKI 368
Cdd:PRK10090 168 AAAAKNI------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 369 KVGDPAGDFETFFSAVIDDKSFARIKKWIQHAeTSPNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAV 448
Cdd:PRK10090 242 QFGNPAERNDIAMGPLINAAALERVEQKVARA-VEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1121863746 449 YVYpeKQYKDILQLVDtTSPYGLTGAVFAQDKNVIQEARKLLRnaAGNFYINDKSTGAVvaqQPF-GGARASG 520
Cdd:PRK10090 321 VAF--DTLEEAIAMAN-DSDYGLTSSIYTQNLNVAMKAIKGLK--FGETYINRENFEAM---QGFhAGWRKSG 385
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
95-520 |
6.99e-42 |
|
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: 155.81 E-value: 6.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 95 INKAINAAVAVRREWDLRPIQDRAQIFFKAADLLsgPRRAEVLAKTM---IGQGKTVIQAEIDAAAELidfFRFNAKYAM 171
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLL--ESRRDEFIEAMmeeTGATAAWAGFNVDLAAGM---LREAASLIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 172 ELEEEQLISVPVSTNSMVYRGLEGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYAVYKILLEAGLPPN 250
Cdd:cd07105 77 QIIGGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRVFHEAGLPKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 251 VIQFV---PASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYRTfprlagECGGKNFHLVHSSADVPTVVN 327
Cdd:cd07105 157 VLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLL------ELGGKAPAIVLEDADLDAAAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 328 GTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGdfetffSAVIDDKSFARIKKWIQHAeTSPNLT 407
Cdd:cd07105 231 AALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL------GSLVSAAAADRVKELVDDA-LSKGAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 408 ILAGGKCDD-KVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDTTSpYGLTGAVFAQDKNVIQE- 485
Cdd:cd07105 304 LVVGGLADEsPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRV--KDEEEAVRIANDSE-YGLSAAVFTRDLARALAv 380
|
410 420 430
....*....|....*....|....*....|....*...
gi 1121863746 486 ARKLlrnAAGNFYINdkstGAVV---AQQPFGGARASG 520
Cdd:cd07105 381 AKRI---ESGAVHIN----GMTVhdePTLPHGGVKSSG 411
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
98-531 |
1.93e-41 |
|
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: 155.21 E-value: 1.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 98 AINAAVAVRREWDLRpiQDRAQIFFKAADLLSgpRRAEVLAkTMIGQ--GKTVIQA--EIDAAaelIDFFRFNAKYAMEl 173
Cdd:cd07146 25 EALALAASYRSTLTR--YQRSAILNKAAALLE--ARREEFA-RLITLesGLCLKDTryEVGRA---ADVLRFAAAEALR- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 174 EEEQLISVPVSTNSMVYRGLE-----GFVAAVSPFNFTAiggNLAG---APALM-GNVVLWKPSDTAVLSSYAVYKILLE 244
Cdd:cd07146 96 DDGESFSCDLTANGKARKIFTlreplGVVLAITPFNHPL---NQVAhkiAPAIAaNNRIVLKPSEKTPLSAIYLADLLYE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 245 AGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSenldrYRtfpRLAGECGGKNFHLVHSSADVPT 324
Cdd:cd07146 173 AGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG-----YK---RQLLELGGNDPLIVMDDADLER 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 325 VVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPaGDFETFFSAVIDDKSFARIKKWIQHAETSp 404
Cdd:cd07146 245 AATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDP-MDPATDMGTVIDEEAAIQIENRVEEAIAQ- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 405 NLTILAGGKcddKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAvyVYPEKQYKDILQLVDTTSpYGLTGAVFAQDKNVIQ 484
Cdd:cd07146 323 GARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAP--VIRVKDLDEAIAISNSTA-YGLSSGVCTNDLDTIK 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1121863746 485 EARKLLRNAAGNfyINDkSTGAVVAQQPFGGARASGTNDKPGGRHYI 531
Cdd:cd07146 397 RLVERLDVGTVN--VNE-VPGFRSELSPFGGVKDSGLGGKEGVREAM 440
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
99-520 |
2.99e-41 |
|
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: 155.04 E-value: 2.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 99 INAAVAVRRE------WDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIGQ-GKTVIQAEIDAAAELIDFFRFNAKYAM 171
Cdd:cd07139 38 VDAAVAAARRafdngpWPRLSPAERAAVLRRLADALE--ARADELARLWTAEnGMPISWSRRAQGPGPAALLRYYAALAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 172 ELEEEQLISVPVSTNSMVYRGLEGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYAVYKILLEAGLPPN 250
Cdd:cd07139 116 DFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAaGCTVVLKPSPETPLDAYLLAEAAEEAGLPPG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 251 VIQFVPASGPVfGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYRTfprlagECGGKNFHLVHSSADVPTVVNGTL 330
Cdd:cd07139 196 VVNVVPADREV-GEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTL------ELGGKSAAIVLDDADLDAAVPGLV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 331 RSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSpNLTILA 410
Cdd:cd07139 269 PASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPL-DPATQIGPLASARQRERVEGYIAKGRAE-GARLVT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 411 GGKCDDKV--GYFIEPCIVETKDPKDRIMKEEIFGPVLAVYvypekQYKDILQLVDTT--SPYGLTGAVFAQDknviqEA 486
Cdd:cd07139 347 GGGRPAGLdrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVI-----PYDDEDDAVRIAndSDYGLSGSVWTAD-----VE 416
|
410 420 430
....*....|....*....|....*....|....*....
gi 1121863746 487 RKL-----LRnaAGNFYINDKSTGAVVaqqPFGGARASG 520
Cdd:cd07139 417 RGLavarrIR--TGTVGVNGFRLDFGA---PFGGFKQSG 450
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
93-520 |
3.44e-41 |
|
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: 154.92 E-value: 3.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 93 DLINKAINAAVAVRRE----WDLRPIQDRAQIFFKAADLLSgpRRAEVLAK--TMiGQGKTVIQ---AEIDAAAeliDFF 163
Cdd:cd07117 34 DATDADVDRAVKAAQEafktWRKTTVAERANILNKIADIID--ENKELLAMveTL-DNGKPIREtraVDIPLAA---DHF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 164 RFNAKyAMELEEEQLISVPVSTNSMVYRGLEGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYAVYKIL 242
Cdd:cd07117 108 RYFAG-VIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAaGNTVVIKPSSTTSLSLLELAKII 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 243 LEAgLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLdryrtFPRLAgECGGKNFHLVHSSADV 322
Cdd:cd07117 187 QDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL-----IPATL-ELGGKSANIIFDDANW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 323 PTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAET 402
Cdd:cd07117 260 DKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPL-DPDTQMGAQVNKDQLDKILSYVDIAKE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 403 SpNLTILAGGK----CDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYvypekQYKDILQLVDTT--SPYGLTGAVF 476
Cdd:cd07117 339 E-GAKILTGGHrlteNGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVI-----KFKTEDEVIDMAndSEYGLGGGVF 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1121863746 477 AQDknvIQEARKLLRNA-AGNFYINdkSTGAVVAQQPFGGARASG 520
Cdd:cd07117 413 TKD---INRALRVARAVeTGRVWVN--TYNQIPAGAPFGGYKKSG 452
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
90-520 |
1.59e-39 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 150.42 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 90 ADKDLINKAINAAVAVRREWD-LRPIQdRAQIFFKAADLLSgpRRAEVLAKT-MIGQGKTvIQ----AEIDAAAELIDFF 163
Cdd:PRK13252 41 ATPADVEAAVASAKQGQKIWAaMTAME-RSRILRRAVDILR--ERNDELAALeTLDTGKP-IQetsvVDIVTGADVLEYY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 164 rfnAKYAMELEEEQlisVPVSTNSMVYRGLE--GFVAAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLSSYAVYK 240
Cdd:PRK13252 117 ---AGLAPALEGEQ---IPLRGGSFVYTRREplGVCAGIGAWNYPIQIACWKSAPALaAGNAMIFKPSEVTPLTALKLAE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 241 ILLEAGLPPNVIQFVPASGPVfGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLdRYRTFprlagECGGKNFHLVHSSA 320
Cdd:PRK13252 191 IYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASL-KEVTM-----ELGGKSPLIVFDDA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 321 DVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHA 400
Cdd:PRK13252 264 DLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPM-DPATNFGPLVSFAHRDKVLGYIEKG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 401 ETSpNLTILAGGK------CDDkvGYFIEPCIVEtkDPKD--RIMKEEIFGPVLAVYVYPEKQykDILQLVDTTsPYGLT 472
Cdd:PRK13252 343 KAE-GARLLCGGErlteggFAN--GAFVAPTVFT--DCTDdmTIVREEIFGPVMSVLTFDDED--EVIARANDT-EYGLA 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1121863746 473 GAVFAQDknvIQEA-RKLLRNAAGNFYINdkSTGAVVAQQPFGGARASG 520
Cdd:PRK13252 415 AGVFTAD---LSRAhRVIHQLEAGICWIN--TWGESPAEMPVGGYKQSG 458
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
75-522 |
1.64e-38 |
|
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: 147.18 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 75 LSPYNHAHkVAKYCYADKDLINKAINAAVAVRREWDLR-PIQDRAQIFFKAADLLSGprRAEVLAKTMIGQG-KTVIQA- 151
Cdd:cd07148 4 VNPFDLKP-IGEVPTVDWAAIDKALDTAHALFLDRNNWlPAHERIAILERLADLMEE--RADELALLIAREGgKPLVDAk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 152 -EIDAAaelIDFFRFNAKYAMELEEEQLIS--VPVSTNSMVYRGLE--GFVAAVSPFNFTAiggNLA---GAPAL-MGNV 222
Cdd:cd07148 81 vEVTRA---IDGVELAADELGQLGGREIPMglTPASAGRIAFTTREpiGVVVAISAFNHPL---NLIvhqVAPAIaAGCP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 223 VLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEhFAGLNFTGSVPTFKRLWKQVSENldryrtfP 302
Cdd:cd07148 155 VIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPR-VAFFSFIGSARVGWMLRSKLAPG-------T 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 303 RLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFS 382
Cdd:cd07148 227 RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPT-DPDTEVG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 383 AVIDDKSFARIKKWIQHAETSpNLTILAGGKCDDKVGYfiEPCIVETKDPKDRIMKEEIFGPVLAVYvypekQYKDILQL 462
Cdd:cd07148 306 PLIRPREVDRVEEWVNEAVAA-GARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVY-----SYDDLDEA 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1121863746 463 VDTTS--PYGLTGAVFAQDKNV-IQEARKLlrnAAGNFYINDKsTGAVVAQQPFGGARASGTN 522
Cdd:cd07148 378 IAQANslPVAFQAAVFTKDLDVaLKAVRRL---DATAVMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
90-520 |
2.06e-38 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 147.57 E-value: 2.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 90 ADKDLINKAINAAVAV-----RREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKT-MIGQGKTVIQAE--IDAAAELID 161
Cdd:PLN02467 42 ATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKIT--ERKSELAKLeTLDCGKPLDEAAwdMDDVAGCFE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 162 FFrfnAKYAMELEEEQL--ISVPVST-NSMVYRGLEGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYA 237
Cdd:PLN02467 120 YY---ADLAEALDAKQKapVSLPMETfKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAaGCTAVLKPSELASVTCLE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 238 VYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDryrtfPrLAGECGGKNFHLVH 317
Cdd:PLN02467 197 LADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVK-----P-VSLELGGKSPIIVF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 318 SSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPagdFET--FFSAVIDDKSFARIKK 395
Cdd:PLN02467 271 DDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDP---LEEgcRLGPVVSEGQYEKVLK 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 396 WIQHAEtSPNLTILAGGKCDD--KVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYPEKQykDILQLVDTTSpYGLTG 473
Cdd:PLN02467 348 FISTAK-SEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTED--EAIELANDSH-YGLAG 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1121863746 474 AVFAQDKNVIQEARKLLRnaAGNFYINdkSTGAVVAQQPFGGARASG 520
Cdd:PLN02467 424 AVISNDLERCERVSEAFQ--AGIVWIN--CSQPCFCQAPWGGIKRSG 466
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
95-542 |
2.52e-37 |
|
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: 143.98 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 95 INKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAK-TMIGQGKTVIQA---EIDAAAELIDFFRFNAKYA 170
Cdd:cd07098 20 VDEAIAAARAAQREWAKTSFAERRKVLRSLLKYIL--ENQEEICRvACRDTGKTMVDAslgEILVTCEKIRWTLKHGEKA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 171 MELEeeqliSVPVSTNsMVYRGLE------GFVAAVSPFNF---TAIGGNLAgapALM-GNVVLWKPSDTAVLSSY---- 236
Cdd:cd07098 98 LRPE-----SRPGGLL-MFYKRARveyeplGVVGAIVSWNYpfhNLLGPIIA---ALFaGNAIVVKVSEQVAWSSGffls 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 237 AVYKILLEAGLPPNVIQFVPASGPVfGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDryrtfPRLAgECGGKNFHLV 316
Cdd:cd07098 169 IIRECLAACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLT-----PVVL-ELGGKDPAIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 317 HSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPA-GDFEtfFSAVIDDKSFARIKK 395
Cdd:cd07098 242 LDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLdGDVD--VGAMISPARFDRLEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 396 WIQHAeTSPNLTILAGGK----CDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDTTsPYGL 471
Cdd:cd07098 320 LVADA-VEKGARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKA--SDDEEAVEIANST-EYGL 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1121863746 472 TGAVFAQDKnviQEARKLLRN-AAGNFYINDKSTGAVVAQQPFGGARASGTnDKPGGRHYILRWTSPQAIKE 542
Cdd:cd07098 396 GASVFGKDI---KRARRIASQlETGMVAINDFGVNYYVQQLPFGGVKGSGF-GRFAGEEGLRGLCNPKSVTE 463
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
84-519 |
3.45e-37 |
|
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: 143.81 E-value: 3.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 84 VAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTM-IGQGKTVIQA--EIDAAAELI 160
Cdd:cd07085 29 IARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLE--ENLDELARLItLEHGKTLADArgDVLRGLEVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 161 DFfRFNAKYAMELEeeqliSVPVSTNSM---VYRGLEGFVAAVSPFNFTAIggnlagAPALM-------GNVVLWKPSDT 230
Cdd:cd07085 107 EF-ACSIPHLLKGE-----YLENVARGIdtySYRQPLGVVAGITPFNFPAM------IPLWMfpmaiacGNTFVLKPSER 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 231 AVLSSYAVYKILLEAGLPPNVIQFVPASGPVfGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYRTFprlageCGG 310
Cdd:cd07085 175 VPGAAMRLAELLQEAGLPDGVLNVVHGGKEA-VNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQAL------GGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 311 KNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGdPAGDFETFFSAVIDDKSF 390
Cdd:cd07085 248 KNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVG-AGDDPGADMGPVISPAAK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 391 ARIKKWIQHAETspnltilAGGKC-----DDKV-----GYFIEPCIVETKDPKDRIMKEEIFGPVLA-VYVypeKQYKDI 459
Cdd:cd07085 327 ERIEGLIESGVE-------EGAKLvldgrGVKVpgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSiVRV---DTLDEA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1121863746 460 LQLVDtTSPYGLTGAVFAQDKNViqeARKLLRNA-AGNFYINdkstgaV-----VAQQPFGGARAS 519
Cdd:cd07085 397 IAIIN-ANPYGNGAAIFTRSGAA---ARKFQREVdAGMVGIN------VpipvpLAFFSFGGWKGS 452
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
84-520 |
3.72e-36 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 141.11 E-value: 3.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 84 VAKYCYADKDLINKAINAAvavRREWDLRPIQ-----DRAQIFFKAADLLSgpRRAEVLAK-------TMIGQGKTViqa 151
Cdd:PLN02766 49 IARIAEGDKEDVDLAVKAA---REAFDHGPWPrmsgfERGRIMMKFADLIE--EHIEELAAldtidagKLFALGKAV--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 152 EIDAAAELidfFRFNAKYAMELEEEQLisvPVSTNSMVYRGLE--GFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPS 228
Cdd:PLN02766 121 DIPAAAGL---LRYYAGAADKIHGETL---KMSRQLQGYTLKEpiGVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 229 DTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSE-NLDRyrtfprLAGE 307
Cdd:PLN02766 195 EQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNLKQ------VSLE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 308 CGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDD 387
Cdd:PLN02766 269 LGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF-DPRARQGPQVDK 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 388 KSFARIKKWIQHAEtSPNLTILAGGK-CDDKvGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDTT 466
Cdd:PLN02766 348 QQFEKILSYIEHGK-REGATLLTGGKpCGDK-GYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKF--KTVEEAIKKANNT 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1121863746 467 SpYGLTGAVFAQDKNVIQEARKLLRnaAGNFYINdkSTGAVVAQQPFGGARASG 520
Cdd:PLN02766 424 K-YGLAAGIVTKDLDVANTVSRSIR--AGTIWVN--CYFAFDPDCPFGGYKMSG 472
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
90-525 |
3.91e-36 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 140.86 E-value: 3.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 90 ADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAkTMIGQ--GKTVIQAEIDAAAELidffrfnA 167
Cdd:PRK09457 34 ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLE--ENKEELA-EVIARetGKPLWEAATEVTAMI-------N 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 168 KYAMELEE------EQLISVPVSTNSMVYRGLeGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYAVYK 240
Cdd:PRK09457 104 KIAISIQAyhertgEKRSEMADGAAVLRHRPH-GVVAVFGPYNFPGHLPNGHIVPALLaGNTVVFKPSELTPWVAELTVK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 241 ILLEAGLPPNVIQFVPAsGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYrtfprLAGECGGKNFHLVHSSA 320
Cdd:PRK09457 183 LWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKI-----LALEMGGNNPLVIDEVA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 321 DVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQ-IKAKLLEEHGKIKVGDPAGDFETFFSAVIDDKSFARIKKWIQH 399
Cdd:PRK09457 257 DIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWDAEPQPFMGAVISEQAAQGLVAAQAQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 400 AETSPNLTILAGGKCDDKVGyFIEPCIVETKDPKDRImKEEIFGPVLAVYVYPEkqYKDILQLVDTTSpYGLTGAVFAQD 479
Cdd:PRK09457 337 LLALGGKSLLEMTQLQAGTG-LLTPGIIDVTGVAELP-DEEYFGPLLQVVRYDD--FDEAIRLANNTR-FGLSAGLLSDD 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1121863746 480 KNVIQEARKLLRnaAGNFYINDKSTGAVVAqQPFGGARASGtNDKP 525
Cdd:PRK09457 412 REDYDQFLLEIR--AGIVNWNKPLTGASSA-APFGGVGASG-NHRP 453
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
195-528 |
4.52e-35 |
|
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: 137.72 E-value: 4.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 195 GFVAAVSPFNF-TAIGG-NLAGApALMGNVVLWKPSDTAVLSSYAVYKILLEA----GLPPNVIQFVPASGPVfGDTVTS 268
Cdd:cd07130 134 GVVGVITAFNFpVAVWGwNAAIA-LVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGADV-GEALVK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 269 SEHFAGLNFTGSVPTfkrlWKQVSENLDRYrtFPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLY 348
Cdd:cd07130 212 DPRVPLVSFTGSTAV----GRQVGQAVAAR--FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 349 VPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSPNlTILAGGKCDDKVGYFIEPCIVE 428
Cdd:cd07130 286 VHESIYDEVLERLKKAYKQVRIGDPL-DDGTLVGPLHTKAAVDNYLAAIEEAKSQGG-TVLFGGKVIDGPGNYVEPTIVE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 429 TKdPKDRIMKEEIFGPVLavYVYPekqYKDILQLVDTTS--PYGLTGAVFAQDknvIQEARKLLrNAAG------NfyIN 500
Cdd:cd07130 364 GL-SDAPIVKEETFAPIL--YVLK---FDTLEEAIAWNNevPQGLSSSIFTTD---LRNAFRWL-GPKGsdcgivN--VN 431
|
330 340 350
....*....|....*....|....*....|
gi 1121863746 501 DKSTGAVV--AqqpFGGARASGtndkpGGR 528
Cdd:cd07130 432 IGTSGAEIggA---FGGEKETG-----GGR 453
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
84-526 |
4.60e-35 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 138.79 E-value: 4.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 84 VAKYCYADKDLINKAINAAVAVRRE--WDLRPIQDRAQIFFKAADLLSgPRRAEVLAKTMIGQGKTVIQAeidAAAELID 161
Cdd:PLN02466 86 IAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLE-KHNDELAALETWDNGKPYEQS---AKAELPM 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 162 FFRFNAKYAMELEEEQLISVPVSTNSMVYRGLE--GFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYAV 238
Cdd:PLN02466 162 FARLFRYYAGWADKIHGLTVPADGPHHVQTLHEpiGVAGQIIPWNFPLLMFAWKVGPALAcGNTIVLKTAEQTPLSALYA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 239 YKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYRTFprlagECGGKNFHLVHS 318
Cdd:PLN02466 242 AKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVTL-----ELGGKSPFIVCE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 319 SADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPagdfetFFSAV-----IDDKSFARI 393
Cdd:PLN02466 317 DADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDP------FKKGVeqgpqIDSEQFEKI 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 394 KKWIQHAETSpNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYvypekQYKDILQLVD--TTSPYGL 471
Cdd:PLN02466 391 LRYIKSGVES-GATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSIL-----KFKDLDEVIRraNNTRYGL 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1121863746 472 TGAVFAQDKNVIQEARKLLRnaAGNFYIN--DKSTGAVvaqqPFGGARASGTNDKPG 526
Cdd:PLN02466 465 AAGVFTQNLDTANTLSRALR--VGTVWVNcfDVFDAAI----PFGGYKMSGIGREKG 515
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
90-529 |
2.41e-34 |
|
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: 135.60 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 90 ADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSGPRRAEVLAKTMIGqGKTVIQ---AEIDAAAELidfFRFN 166
Cdd:cd07111 56 AEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDN-GKPIREsrdCDIPLVARH---FYHH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 167 AKYAMELEEEqlisvpvstnsMVYRGLEGFVAAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLSSYAVYKILLEA 245
Cdd:cd07111 132 AGWAQLLDTE-----------LAGWKPVGVVGQIVPWNFPLLMLAWKICPALaMGNTVVLKPAEYTPLTALLFAEICAEA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 246 GLPPNVIQFVPASGPvFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSEnldryrTFPRLAGECGGKNFHLVHSSADVPTV 325
Cdd:cd07111 201 GLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAG------TGKKLSLELGGKSPFIVFDDADLDSA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 326 VNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSPN 405
Cdd:cd07111 274 VEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPL-DKAIDMGAIVDPAQLKRIRELVEEGRAEGA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 406 LTILAGGKCDDKvGYFIEPCIVETKDPKDRIMKEEIFGPVLAvyVYPEKQYKDILQLVDTTsPYGLTGAVFAQDKNVIQE 485
Cdd:cd07111 353 DVFQPGADLPSK-GPFYPPTLFTNVPPASRIAQEEIFGPVLV--VLTFRTAKEAVALANNT-PYGLAASVWSENLSLALE 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1121863746 486 ARKLLRnaAGNFYINdkSTGAVVAQQPFGGARASGTNdKPGGRH 529
Cdd:cd07111 429 VALSLK--AGVVWIN--GHNLFDAAAGFGGYRESGFG-REGGKE 467
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
97-520 |
2.96e-34 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 135.42 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 97 KAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTM-IGQGKTVIQA--EIDAAAELIDFFRFNAK--YAM 171
Cdd:PRK11241 52 AAIDAANRALPAWRALTAKERANILRRWFNLMM--EHQDDLARLMtLEQGKPLAEAkgEISYAASFIEWFAEEGKriYGD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 172 ELEEEQ------LISVPVstnsmvyrgleGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYAVYKILLE 244
Cdd:PRK11241 130 TIPGHQadkrliVIKQPI-----------GVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 245 AGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRyrtfprLAGECGGKNFHLVHSSADVPT 324
Cdd:PRK11241 199 AGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK------VSLELGGNAPFIVFDDADLDK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 325 VVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDFETfFSAVIDDKSFARIKKWIQHAeTSP 404
Cdd:PRK11241 273 AVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVT-IGPLIDEKAVAKVEEHIADA-LEK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 405 NLTILAGGKCDDKVGYFIEPCIVeTKDPKD-RIMKEEIFGPVLAVYVYpeKQYKDILQLVDTTSpYGLTGAVFAQD-KNV 482
Cdd:PRK11241 351 GARVVCGGKAHELGGNFFQPTIL-VDVPANaKVAKEETFGPLAPLFRF--KDEADVIAQANDTE-FGLAAYFYARDlSRV 426
|
410 420 430
....*....|....*....|....*....|....*...
gi 1121863746 483 IQEARKLLRNAAGnfyINDKSTGAVVAqqPFGGARASG 520
Cdd:PRK11241 427 FRVGEALEYGIVG---INTGIISNEVA--PFGGIKASG 459
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
84-520 |
5.64e-34 |
|
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: 134.55 E-value: 5.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 84 VAKYCYADKDLINKAINAAVAV--RREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAKT-MIGQGKTVIQAEIDAAAELI 160
Cdd:cd07140 34 ICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLME--EHQEELATIeSLDSGAVYTLALKTHVGMSI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 161 DFFRFNAKYAMELeeeQLISVPVS----TNSMVYRGLE--GFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVL 233
Cdd:cd07140 112 QTFRYFAGWCDKI---QGKTIPINqarpNRNLTLTKREpiGVCGIVIPWNYPLMMLAWKMAACLAaGNTVVLKPAQVTPL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 234 SSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENldryrTFPRLAGECGGKNF 313
Cdd:cd07140 189 TALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVS-----NLKKVSLELGGKSP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 314 HLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARI 393
Cdd:cd07140 264 LIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL-DRSTDHGPQNHKAHLDKL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 394 KKWIQHAeTSPNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYPEKQYKDILQLVDTTSpYGLTG 473
Cdd:cd07140 343 VEYCERG-VKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDVDGVLQRANDTE-YGLAS 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1121863746 474 AVFAQDKNviqearKLLRNA----AGNFYINDKSTGAVVAqqPFGGARASG 520
Cdd:cd07140 421 GVFTKDIN------KALYVSdkleAGTVFVNTYNKTDVAA--PFGGFKQSG 463
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
95-548 |
2.62e-33 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 133.10 E-value: 2.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 95 INKAINAAVAV--RREWDLRPIQDRAQIFFKAADLLSgpRRAEVLAK-TMIGQGKTV---IQAEIDAAAELIDFfrfnak 168
Cdd:PRK09847 59 IDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLME--AHAEELALlETLDTGKPIrhsLRDDIPGAARAIRW------ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 169 YAMELEEEQLISVPVSTNS--MVYRGLEGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYAVYKILLEA 245
Cdd:PRK09847 131 YAEAIDKVYGEVATTSSHElaMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLAKEA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 246 GLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENldryrTFPRLAGECGGKNFHLVHSSA-DVPT 324
Cdd:PRK09847 211 GLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS-----NMKRVWLEAGGKSANIVFADCpDLQQ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 325 VVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSP 404
Cdd:PRK09847 286 AASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL-DPATTMGTLIDCAHADSVHSFIREGESKG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 405 nlTILAGGKCDDKVGYfIEPCIVETKDPKDRIMKEEIFGPVLAVYVYPEKQykDILQLVDtTSPYGLTGAVFAQDknvIQ 484
Cdd:PRK09847 365 --QLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEE--QALQLAN-DSQYGLGAAVWTRD---LS 435
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1121863746 485 EARKLLRN-AAGNFYINDKSTGAVVAqqPFGGARASGtNDKPGGRHYILRWTSpqaIKETHVPLE 548
Cdd:PRK09847 436 RAHRMSRRlKAGSVFVNNYNDGDMTV--PFGGYKQSG-NGRDKSLHALEKFTE---LKTIWISLE 494
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
61-520 |
6.00e-29 |
|
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: 119.86 E-value: 6.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 61 VGGQevWTADVRYQ----LSPYNhAHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSGPRRAEV 136
Cdd:cd07116 5 IGGE--WVAPVKGEyfdnITPVT-GKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 137 LAKTmIGQGKTV---IQAEIDAAaelIDFFRFNAKyAMELEEEQLISVPVSTNSMVYRGLEGFVAAVSPFNFTAIGGNLA 213
Cdd:cd07116 82 VAET-WDNGKPVretLAADIPLA---IDHFRYFAG-CIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 214 GAPALM-GNVVLWKPSDTAVLSSYAVYKILLEAgLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVS 292
Cdd:cd07116 157 LAPALAaGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 293 ENLdryrtFPrLAGECGGKN----FHLVHSSAD--VPTVVNGTLRSAFEYgGQKCSACSRLYVPDLLWPQIKAKLLEEHG 366
Cdd:cd07116 236 ENI-----IP-VTLELGGKSpnifFADVMDADDafFDKALEGFVMFALNQ-GEVCTCPSRALIQESIYDRFMERALERVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 367 KIKVGDPAgDFETFFSAVIDDKSFARIKKWIQHAETSpNLTILAGGK----CDDKVGYFIEPCIVETKDpKDRIMKEEIF 442
Cdd:cd07116 309 AIKQGNPL-DTETMIGAQASLEQLEKILSYIDIGKEE-GAEVLTGGErnelGGLLGGGYYVPTTFKGGN-KMRIFQEEIF 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1121863746 443 GPVLAVYVYpeKQYKDILQLVDTTsPYGLTGAVFAQDKNviqEARKLLRN-AAGNFYINdkSTGAVVAQQPFGGARASG 520
Cdd:cd07116 386 GPVLAVTTF--KDEEEALEIANDT-LYGLGAGVWTRDGN---TAYRMGRGiQAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
90-520 |
4.56e-27 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 114.06 E-value: 4.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 90 ADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSGPRR--AEVLAKTMigqGKTVIQAEIDAAaELIDFFRFNA 167
Cdd:PRK09406 20 LTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADqvAALMTLEM---GKTLASAKAEAL-KCAKGFRYYA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 168 KYAMEL---EEEQLISVPVSTNSMVYRGLeGFVAAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSSYAVYKILL 243
Cdd:PRK09406 96 EHAEALladEPADAAAVGASRAYVRYQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGNVGLLKHASNVPQTALYLADLFR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 244 EAGLPPNVIQ-FVPASGPVfgDTVTSSEHFAGLNFTGSVPTfkrlwkqvsenldrYRTFPRLAG--------ECGGKNFH 314
Cdd:PRK09406 175 RAGFPDGCFQtLLVGSGAV--EAILRDPRVAAATLTGSEPA--------------GRAVAAIAGdeikktvlELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 315 LVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIK 394
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPT-DPDTDVGPLATEQGRDEVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 395 KWIQHAeTSPNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYPEkqYKDILQLVDTTsPYGLTGA 474
Cdd:PRK09406 318 KQVDDA-VAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVAD--IDEAIEIANAT-TFGLGSN 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1121863746 475 VFAQDKnviQEARKLLRN-AAGNFYINdkstGAVVA--QQPFGGARASG 520
Cdd:PRK09406 394 AWTRDE---AEQERFIDDlEAGQVFIN----GMTVSypELPFGGVKRSG 435
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
195-520 |
3.54e-25 |
|
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: 108.00 E-value: 3.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 195 GFVAAVSPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAVLSSyAVYKILLEAGLPPNVIQFVPASGPVFgdTVTSSEH 271
Cdd:cd07087 102 GVVLIIGPWNYplqLALA-PLIGAIA-AGNTVVLKPSELAPATS-ALLAKLIPKYFDPEAVAVVEGGVEVA--TALLAEP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 272 FAGLNFTGSVPTFKRLWKQVSENLdryrTFPRLagECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPd 351
Cdd:cd07087 177 FDHIFFTGSPAVGKIVMEAAAKHL----TPVTL--ELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVH- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 352 llwPQIKAKLLEEHGK-IK--VGDPAGDFETFfSAVIDDKSFARIKKWIQHAetspnlTILAGGKCDDKvGYFIEPCIVE 428
Cdd:cd07087 250 ---ESIKDELIEELKKaIKefYGEDPKESPDY-GRIINERHFDRLASLLDDG------KVVIGGQVDKE-ERYIAPTILD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 429 TKDPKDRIMKEEIFGPVLAVYVYPEKQykDILQLVDTTsPYGLTGAVFAQDKNVIQearKLLRN-AAGNFYINDKSTGAV 507
Cdd:cd07087 319 DVSPDSPLMQEEIFGPILPILTYDDLD--EAIEFINSR-PKPLALYLFSEDKAVQE---RVLAEtSSGGVCVNDVLLHAA 392
|
330
....*....|...
gi 1121863746 508 VAQQPFGGARASG 520
Cdd:cd07087 393 IPNLPFGGVGNSG 405
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
96-540 |
6.14e-25 |
|
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: 107.71 E-value: 6.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 96 NKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSgPRRAEVLAKTMIGQGKTVIQAEIDAAAELIDFFRFNAKYAMELEE 175
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLA-AKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 176 EQLISVP--VSTNSMVYRGLEGFVAAVSPFNF--TAIGGNLAGAPAlMGNVVLWKPSDTAVLSSYAVYKILLEAG-LPPN 250
Cdd:cd07084 81 EPGNHLGqgLKQQSHGYRWPYGPVLVIGAFNFplWIPLLQLAGALA-MGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 251 VIQFVPASGPVfGDTVTSSEHFAGLNFTGSVptfkrlwkQVSENLDRYRTFPRLAGECGGKNFHLVHSSAD-VPTVVNGT 329
Cdd:cd07084 160 DVTLINGDGKT-MQALLLHPNPKMVLFTGSS--------RVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 330 LRSAFEYGGQKCSACSRLYVP--DLLWPQIKaKLLEEHGKIKVGDpagdfeTFFSAVIDDKSFARikkwIQHAETSPNLT 407
Cdd:cd07084 231 VQDMTACSGQKCTAQSMLFVPenWSKTPLVE-KLKALLARRKLED------LLLGPVQTFTTLAM----IAHMENLLGSV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 408 ILAGGK------CDDKVGYFIEPCIVETKDPKDRIMK---EEIFGPVLAVYVYPEKQYKDILQLVDTTSPYgLTGAVFAQ 478
Cdd:cd07084 300 LLFSGKelknhsIPSIYGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKKDQLALVLELLERMHGS-LTAAIYSN 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1121863746 479 DKNVIQEARKLLRNAAGNFYINDKSTGAVVAQQPFGGARASGTNDKPGGRHYILRWTSPQAI 540
Cdd:cd07084 379 DPIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
47-528 |
9.16e-25 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 108.00 E-value: 9.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 47 LNDLKGKTEAIPCVVGGqeVWTAD--VRYQLSPYNHaHKVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQIFFKA 124
Cdd:PLN02315 11 LSEIGLSSRNLGCYVGG--EWRANgpLVSSVNPANN-QPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 125 ADLLSgpRRAEVLAKTMIGQGKTVIQAEIDAAAELIDFfrfnAKYAMELEEEQLISVPVST--NSM---VYRGLeGFVAA 199
Cdd:PLN02315 88 GDALR--AKLDYLGRLVSLEMGKILAEGIGEVQEIIDM----CDFAVGLSRQLNGSIIPSErpNHMmmeVWNPL-GIVGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 200 VSPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAVLSSYAVYKILLEA----GLPPNVIQFVpASGPVFGDTVTSSEHFAG 274
Cdd:PLN02315 161 ITAFNFpCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSF-CGGAEIGEAIAKDTRIPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 275 LNFTGSVPTFKRLWKQVSENldryrtFPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLW 354
Cdd:PLN02315 240 VSFTGSSKVGLMVQQTVNAR------FGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 355 PQIKAKLLEEHGKIKVGDPAgDFETFFSAVIDDKSFARIKKWIQhAETSPNLTILAGGKCDDKVGYFIEPCIVETKdPKD 434
Cdd:PLN02315 314 DDVLEQLLTVYKQVKIGDPL-EKGTLLGPLHTPESKKNFEKGIE-IIKSQGGKILTGGSAIESEGNFVQPTIVEIS-PDA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 435 RIMKEEIFGPVLavYVYPEKQYKDILQLvDTTSPYGLTGAVFAQDKNVIQEARKLLRNAAGNFYINDKSTGAVVAqQPFG 514
Cdd:PLN02315 391 DVVKEELFGPVL--YVMKFKTLEEAIEI-NNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIG-GAFG 466
|
490
....*....|....
gi 1121863746 515 GARASGtndkpGGR 528
Cdd:PLN02315 467 GEKATG-----GGR 475
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
195-521 |
3.61e-23 |
|
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: 102.30 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 195 GFVAAVSPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAVLSSyAVYKILLEAGLPPNVIQFVPASGPVFGDTVTssEH 271
Cdd:cd07135 110 GVVLIIGPWNYpvlLALS-PLVGAIA-AGCTVVLKPSELTPHTA-ALLAELVPKYLDPDAFQVVQGGVPETTALLE--QK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 272 FAGLNFTGSVptfkRLWKQVSENLDRYRTfPrLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPd 351
Cdd:cd07135 185 FDKIFYTGSG----RVGRIIAEAAAKHLT-P-VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 352 llwPQIKAKLLEEHGK-IKVGDPAGDFE-TFFSAVIDDKSFARIKKWIQHAETspnlTILAGGKCDDKVgYFIEPCIVET 429
Cdd:cd07135 258 ---PSVYDEFVEELKKvLDEFYPGGANAsPDYTRIVNPRHFNRLKSLLDTTKG----KVVIGGEMDEAT-RFIPPTIVSD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 430 KDPKDRIMKEEIFGPVLAVYVY-PEKQYKDILQLVDTTspygLTGAVFAQDKNVIQeaRKLLRNAAGNFYINDKSTGAVV 508
Cdd:cd07135 330 VSWDDSLMSEELFGPVLPIIKVdDLDEAIKVINSRDTP----LALYIFTDDKSEID--HILTRTRSGGVVINDTLIHVGV 403
|
330
....*....|...
gi 1121863746 509 AQQPFGGARASGT 521
Cdd:cd07135 404 DNAPFGGVGDSGY 416
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
75-520 |
7.59e-23 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 101.48 E-value: 7.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 75 LSPYNHA--------HKVAKYCYADKDLINKAINAAVAVRREWDLRPIQDRAQiffKAADLLSGPR-RAEVLAKTMIGQ- 144
Cdd:PRK13968 3 ITPATHAisvnpatgEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQ---KLRDIGKALRaRSEEMAQMITREm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 145 GKTVIQA--EIDAAAELIDFFrfnAKY--AMELEEEQLisvpVSTNSMV--YRGLeGFVAAVSPFNFtAIGGNLAGA-PA 217
Cdd:PRK13968 80 GKPINQAraEVAKSANLCDWY---AEHgpAMLKAEPTL----VENQQAVieYRPL-GTILAIMPWNF-PLWQVMRGAvPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 218 LM-GNVVLWKPSDTAVLSSYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEhFAGLNFTGSVPTFKRLWKQVSENLD 296
Cdd:PRK13968 151 LLaGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIGAQAGAALK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 297 RyrtfprLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAgD 376
Cdd:PRK13968 230 K------CVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPR-D 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 377 FETFFSAV----IDDKSFARIKkwiqhAETSPNLTILAGGKCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYP 452
Cdd:PRK13968 303 EENALGPMarfdLRDELHHQVE-----ATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAK 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1121863746 453 EKQYKdiLQLVDtTSPYGLTGAVFAQDKNVIQE-ARKLlrnAAGNFYINDKStgAVVAQQPFGGARASG 520
Cdd:PRK13968 378 DAEHA--LELAN-DSEFGLSATIFTTDETQARQmAARL---ECGGVFINGYC--ASDARVAFGGVKKSG 438
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
195-520 |
9.85e-23 |
|
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: 101.04 E-value: 9.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 195 GFVAAVSPFN--FTAIGGNLAGAPAlMGNVVLWKPSDTAVLSSYAVYKILLEAgLPPNVIQFVPasgpvfGDTVTS---- 268
Cdd:cd07136 102 GVVLIIAPWNypFQLALAPLIGAIA-AGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVE------GGVEENqell 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 269 SEHFAGLNFTGSVPTFKRLWKQVSENLdryrTFPRLagECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSAcsrly 348
Cdd:cd07136 174 DQKFDYIFFTGSVRVGKIVMEAAAKHL----TPVTL--ELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVA----- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 349 vPDLLWPQ--IKAKLLEE--------HGKIKVGDPAgdfetfFSAVIDDKSFARIKKWIQHAEtspnltILAGGKCDDKV 418
Cdd:cd07136 243 -PDYVLVHesVKEKFIKElkeeikkfYGEDPLESPD------YGRIINEKHFDRLAGLLDNGK------IVFGGNTDRET 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 419 GYfIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVdTTSPYGLTGAVFAQDKNViqeARKLLRNAA-GNF 497
Cdd:cd07136 310 LY-IEPTILDNVTWDDPVMQEEIFGPILPVLTY--DTLDEAIEII-KSRPKPLALYLFSEDKKV---EKKVLENLSfGGG 382
|
330 340
....*....|....*....|...
gi 1121863746 498 YINDKSTGAVVAQQPFGGARASG 520
Cdd:cd07136 383 CINDTIMHLANPYLPFGGVGNSG 405
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
195-520 |
1.62e-22 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 100.87 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 195 GFVAAVSPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAVLSSYAVYKiLLEAGLPPNVIQFVPASGPVfgDTVTSSEH 271
Cdd:PTZ00381 111 GVVLVIGAWNYplnLTLI-PLAGAIA-AGNTVVLKPSELSPHTSKLMAK-LLTKYLDPSYVRVIEGGVEV--TTELLKEP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 272 FAGLNFTGSVPTFKRLWKQVSENLdryrTFPRLagECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPD 351
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAENL----TPCTL--ELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 352 llwpQIKAKLLEEHgKIKVGDPAG-DFETF--FSAVIDDKSFARIKKWIQHAETspnlTILAGGKCDDKVGYfIEPCIVE 428
Cdd:PTZ00381 260 ----SIKDKFIEAL-KEAIKEFFGeDPKKSedYSRIVNEFHTKRLAELIKDHGG----KVVYGGEVDIENKY-VAPTIIV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 429 TKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDtTSPYGLTGAVFAQDKNVIQeaRKLLRNAAGNFYINDKSTGAVV 508
Cdd:PTZ00381 330 NPDLDSPLMQEEIFGPILPILTY--ENIDEVLEFIN-SRPKPLALYYFGEDKRHKE--LVLENTSSGAVVINDCVFHLLN 404
|
330
....*....|..
gi 1121863746 509 AQQPFGGARASG 520
Cdd:PTZ00381 405 PNLPFGGVGNSG 416
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
92-481 |
1.13e-21 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 98.29 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 92 KDLINKAINAAVAVRREWDLRPIQDRAQIFFKAADLLSGPRR--AEVLAKTMIGQGKTVIqAEIDAAAELIDffrfnakY 169
Cdd:PLN00412 52 QEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKApiAECLVKEIAKPAKDAV-TEVVRSGDLIS-------Y 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 170 AME-----LEEEQLI---SVPVSTNS---MVYRGLEGFVAAVSPFNFTAiggNLAG---APALM-GNVVLWKPSDTAVLS 234
Cdd:PLN00412 124 TAEegvriLGEGKFLvsdSFPGNERNkycLTSKIPLGVVLAIPPFNYPV---NLAVskiAPALIaGNAVVLKPPTQGAVA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 235 SYAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEHFAGLNFTGSvPTFKRLWKQVsenldryRTFPrLAGECGGKNFH 314
Cdd:PLN00412 201 ALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISKKA-------GMVP-LQMELGGKDAC 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 315 LVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDFEtfFSAVIDDKSFARIK 394
Cdd:PLN00412 272 IVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCD--ITPVVSESSANFIE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 395 KWIQHAETSpnltilaGGK-CDD--KVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDtTSPYGL 471
Cdd:PLN00412 350 GLVMDAKEK-------GATfCQEwkREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRI--NSVEEGIHHCN-ASNFGL 419
|
410
....*....|
gi 1121863746 472 TGAVFAQDKN 481
Cdd:PLN00412 420 QGCVFTRDIN 429
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
202-520 |
7.99e-20 |
|
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: 91.90 E-value: 7.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 202 PFNFTAigGNLAGAPAlMGNVVLWKPSDTAVLSSYAVYKILLEAglppnviqFVPASGPVF-GDTVTSSE----HFAGLN 276
Cdd:cd07134 113 PFNLAF--GPLVSAIA-AGNTAILKPSELTPHTSAVIAKIIREA--------FDEDEVAVFeGDAEVAQAllelPFDHIF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 277 FTGSVPTFKRLWKQVSENLdryrTFPRLagECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPdllwPQ 356
Cdd:cd07134 182 FTGSPAVGKIVMAAAAKHL----ASVTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVH----ES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 357 IKAKLLEeHGKIKVGDPAGDFETF-----FSAVIDDKSFARIKKWIQHAeTSPNLTILAGGKCDDKvGYFIEPCIVETKD 431
Cdd:cd07134 252 VKDAFVE-HLKAEIEKFYGKDAARkaspdLARIVNDRHFDRLKGLLDDA-VAKGAKVEFGGQFDAA-QRYIAPTVLTNVT 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 432 PKDRIMKEEIFGPVLAVYVypekqYKDILQLVDTT--SPYGLTGAVFAQDKNVIQearKLLRN-AAGNFYINDKSTGAVV 508
Cdd:cd07134 329 PDMKIMQEEIFGPVLPIIT-----YEDLDEVIEYInaKPKPLALYVFSKDKANVN---KVLARtSSGGVVVNDVVLHFLN 400
|
330
....*....|..
gi 1121863746 509 AQQPFGGARASG 520
Cdd:cd07134 401 PNLPFGGVNNSG 412
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
184-520 |
5.33e-18 |
|
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: 86.38 E-value: 5.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 184 STNSMVYRGLeGFVAAVSPFNF---TAIGGnLAGAPAlMGNVVLWKPSD----TAvlssyAVYKILLEAGLPPNVIQFV- 255
Cdd:cd07133 93 AKAEVEYQPL-GVVGIIVPWNYplyLALGP-LIAALA-AGNRVMIKPSEftprTS-----ALLAELLAEYFDEDEVAVVt 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 256 --PASGPVFgdtvtSSEHFAGLNFTGSVPTFKRLWKQVSENLdryrTFPRLagECGGKNFHLVHSSADVPTVVNGTLRSA 333
Cdd:cd07133 165 ggADVAAAF-----SSLPFDHLLFTGSTAVGRHVMRAAAENL----TPVTL--ELGGKSPAIIAPDADLAKAAERIAFGK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 334 FEYGGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIkVGDPAGDFEtfFSAVIDDKSFARIKKWIQHAETS-PNLTILAGG 412
Cdd:cd07133 234 LLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-YPTLADNPD--YTSIINERHYARLQGLLEDARAKgARVIELNPA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 413 KCDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVyvypeKQYKDILQLVD--TTSPYGLTGAVFAQDKnviQEARKLL 490
Cdd:cd07133 311 GEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPI-----LTYDSLDEAIDyiNARPRPLALYYFGEDK---AEQDRVL 382
|
330 340 350
....*....|....*....|....*....|...
gi 1121863746 491 RN-AAGNFYINDksTGAVVAQ--QPFGGARASG 520
Cdd:cd07133 383 RRtHSGGVTIND--TLLHVAQddLPFGGVGASG 413
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
96-500 |
4.04e-17 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 84.80 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 96 NKAINAAVAVRRE----WDLRPIQDRAQIFFKAADLLSgpRRAEVLAKTMIG-QGKTV--IQAEIDAAAELIDFFRFNAK 168
Cdd:PLN02419 150 NEEFKAAVSAAKQafplWRNTPITTRQRVMLKFQELIR--KNMDKLAMNITTeQGKTLkdSHGDIFRGLEVVEHACGMAT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 169 YAMEleeEQLISVPVSTNSMVYRGLEGFVAAVSPFNFTAIggnlagAPALM-------GNVVLWKPSDTAVLSSYAVYKI 241
Cdd:PLN02419 228 LQMG---EYLPNVSNGVDTYSIREPLGVCAGICPFNFPAM------IPLWMfpvavtcGNTFILKPSEKDPGASVILAEL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 242 LLEAGLPPNVIQFVPASGPVFgDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRYRTfprlagECGGKNFHLVHSSAD 321
Cdd:PLN02419 299 AMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQS------NMGAKNHGLVLPDAN 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 322 VPTVVNGTLRSAFEYGGQKCSACSR-LYVPDL-LWpqiKAKLLEEHGKIKV---GDPAGDfetfFSAVIDDKSFARIKKW 396
Cdd:PLN02419 372 IDATLNALLAAGFGAAGQRCMALSTvVFVGDAkSW---EDKLVERAKALKVtcgSEPDAD----LGPVISKQAKERICRL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 397 IQHAeTSPNLTILAGGKCDDKVGY----FIEPCIVETKDPKDRIMKEEIFGPVLAvyVYPEKQYKDILQLVDTTSpYGLT 472
Cdd:PLN02419 445 IQSG-VDDGAKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLV--CMQANSFDEAISIINKNK-YGNG 520
|
410 420
....*....|....*....|....*....
gi 1121863746 473 GAVFAQDKnviQEARKLLRN-AAGNFYIN 500
Cdd:PLN02419 521 AAIFTSSG---AAARKFQMDiEAGQIGIN 546
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
212-520 |
5.93e-17 |
|
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: 83.42 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 212 LAGAPAlMGNVVLWKPSDTAVLSSYAVYKiLLEAGLPPNVIQFVpaSGPVFGDTVTSSEHFAGLNFTGSvptfKRLWKQV 291
Cdd:cd07132 121 LVGAIA-AGNCVVIKPSEVSPATAKLLAE-LIPKYLDKECYPVV--LGGVEETTELLKQRFDYIFYTGS----TSVGKIV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 292 SENLDRYRTFPRLagECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSAcsrlyvPD--LLWPQIKAKLLEEHGKIK 369
Cdd:cd07132 193 MQAAAKHLTPVTL--ELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIA------PDyvLCTPEVQEKFVEALKKTL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 370 V---GDPAGDFETFfSAVIDDKSFARIKKWIqhaetsPNLTILAGGKCDDKVGYfIEPCIVETKDPKDRIMKEEIFGPVL 446
Cdd:cd07132 265 KefyGEDPKESPDY-GRIINDRHFQRLKKLL------SGGKVAIGGQTDEKERY-IAPTVLTDVKPSDPVMQEEIFGPIL 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1121863746 447 AvyVYPEKQYKDILQLV-DTTSPygLTGAVFAQDKNVIQearKLLRN-AAGNFYINDKSTGAVVAQQPFGGARASG 520
Cdd:cd07132 337 P--IVTVNNLDEAIEFInSREKP--LALYVFSNNKKVIN---KILSNtSSGGVCVNDTIMHYTLDSLPFGGVGNSG 405
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
203-533 |
8.04e-12 |
|
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: 67.68 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 203 FNFTAIGGNLAGAPALMGNV-VLWKP-SDTAVLSsYAVYKILLEAG-LPPNVIQFVPAS-GPVFgDTVTSSEHFAglnFT 278
Cdd:cd07128 154 FNFPVWGMLEKFAPALLAGVpVIVKPaTATAYLT-EAVVKDIVESGlLPEGALQLICGSvGDLL-DHLGEQDVVA---FT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 279 GSVPTFKRLwkqvsenldryRTFPRLAGEcgGKNFHL----VHSSADVPTVVNGT----------LRSAFEYGGQKCSAC 344
Cdd:cd07128 229 GSAATAAKL-----------RAHPNIVAR--SIRFNAeadsLNAAILGPDATPGTpefdlfvkevAREMTVKAGQKCTAI 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 345 SRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDfETFFSAVIDDKSF----ARIKKWIQHAET---SPNLTILAGGKCDDk 417
Cdd:cd07128 296 RRAFVPEARVDAVIEALKARLAKVVVGDPRLE-GVRMGPLVSREQRedvrAAVATLLAEAEVvfgGPDRFEVVGADAEK- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 418 vGYFIEPCIVETKDP--KDRIMKEEIFGPVlaVYVYPekqYKDILQLVDTTSPYG--LTGAVFAQDKnviQEARKLLRNA 493
Cdd:cd07128 374 -GAFFPPTLLLCDDPdaATAVHDVEAFGPV--ATLMP---YDSLAEAIELAARGRgsLVASVVTNDP---AFARELVLGA 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1121863746 494 A---GNFYINDKST-------GAVVAQQPFGG-ARASGtNDKPGG----RHYILR 533
Cdd:cd07128 445 ApyhGRLLVLNRDSakestghGSPLPQLVHGGpGRAGG-GEELGGlrgvKHYMQR 498
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
191-451 |
1.06e-11 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 67.42 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 191 RGLEGFVAAvspFNFTAIGGNLAGAPALMGNV-VLWKPSDTAVLSSYAVYKILLEAG-LPPNVIQFVPASGpvfGDTVTS 268
Cdd:PRK11903 149 RGVALFINA---FNFPAWGLWEKAAPALLAGVpVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSS---AGLLDH 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 269 SEHFAGLNFTGSVPTFKRLwkqvsenldryRTFPRLAGECGGKNFHL--VHSSADVPTVVNGTlrSAFEY---------- 336
Cdd:PRK11903 223 LQPFDVVSFTGSAETAAVL-----------RSHPAVVQRSVRVNVEAdsLNSALLGPDAAPGS--EAFDLfvkevvremt 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 337 --GGQKCSACSRLYVPDLLWPQIKAKLLEEHGKIKVGDPAGDFETFFSAVIDDK---SFARIKKWIQHAEtspnlTILAG 411
Cdd:PRK11903 290 vkSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQlaaVRAGLAALRAQAE-----VLFDG 364
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1121863746 412 GKC-----DDKVGYFIEPCIVETKDPK--DRIMKEEIFGPVLAVYVY 451
Cdd:PRK11903 365 GGFalvdaDPAVAACVGPTLLGASDPDaaTAVHDVEVFGPVATLLPY 411
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
195-521 |
5.14e-10 |
|
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: 61.66 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 195 GFVAAVSPFNFtAIGGNL---AGAPAlMGNVVLWKPSDTAVLSSYAVYKiLLEAGLPPNVIQFVPASGPVfgDTVTSSEH 271
Cdd:cd07137 103 GVVLVISAWNF-PFLLSLepvIGAIA-AGNAVVLKPSELAPATSALLAK-LIPEYLDTKAIKVIEGGVPE--TTALLEQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 272 FAGLNFTGSVPTFKRLWKQVSENLDryrtfPrLAGECGGKNFHLVHSSADVPTVVNGTLrsAFEYG---GQKCSACSRLY 348
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHLT-----P-VTLELGGKCPVIVDSTVDLKVAVRRIA--GGKWGcnnGQACIAPDYVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 349 VPDLLWP----QIKAKLLEEHGK--IKVGDpagdfetfFSAVIDDKSFARIKKWIQHAETSPnlTILAGGKCDDKvGYFI 422
Cdd:cd07137 250 VEESFAPtlidALKNTLEKFFGEnpKESKD--------LSRIVNSHHFQRLSRLLDDPSVAD--KIVHGGERDEK-NLYI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 423 EPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDtTSPYGLTGAVFAQDKNViqEARKLLRNAAGNFYINDK 502
Cdd:cd07137 319 EPTILLDPPLDSSIMTEEIFGPLLPIITV--KKIEESIEIIN-SRPKPLAAYVFTKNKEL--KRRIVAETSSGGVTFNDT 393
|
330
....*....|....*....
gi 1121863746 503 STGAVVAQQPFGGARASGT 521
Cdd:cd07137 394 VVQYAIDTLPFGGVGESGF 412
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
220-520 |
6.51e-08 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 55.05 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 220 GNVVLWKPSDTAVLSSYAVYKiLLEAGLPPNVIQFVpaSGPVFGDTVTSSEHFAGLNFTGSVPTFKRLWKQVSENLDRyr 299
Cdd:PLN02174 140 GNAVVLKPSELAPASSALLAK-LLEQYLDSSAVRVV--EGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTP-- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 300 tfprLAGECGGKNFHLVHSSADVPTVVNGTLrsAFEYGGQKCSAC--------SRLYVPDLLwPQIKAKLLEEHGKikvg 371
Cdd:PLN02174 215 ----VVLELGGKSPVVVDSDTDLKVTVRRII--AGKWGCNNGQACispdyiltTKEYAPKVI-DAMKKELETFYGK---- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 372 DPAGDFEtfFSAVIDDKSFARIKKWIQHAETSPNltILAGGKcDDKVGYFIEPCIVETKDPKDRIMKEEIFGPVLAVYVY 451
Cdd:PLN02174 284 NPMESKD--MSRIVNSTHFDRLSKLLDEKEVSDK--IVYGGE-KDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTL 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 452 PEKQYK-DILQlvdtTSPYGLTGAVFAQDKNViqEARKLLRNAAGNFYINDKSTGAVVAQQPFGGARASG 520
Cdd:PLN02174 359 NNLEESfDVIR----SRPKPLAAYLFTHNKKL--KERFAATVSAGGIVVNDIAVHLALHTLPFGGVGESG 422
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
91-543 |
3.41e-07 |
|
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: 52.88 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 91 DKDLINKAINAAVAVRREWDLRPIQ--DRAQ----IFFKAADLLSGPRRAEVLAKTMigqGKTVIQAEIDAAAELIDFFR 164
Cdd:cd07126 32 DEDEINEFVDSLRQCPKSGLHNPLKnpERYLlygdVSHRVAHELRKPEVEDFFARLI---QRVAPKSDAQALGEVVVTRK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 165 FNAKYAMELEEEQLISVPVSTN-----SMVYRGLEGFVAAVSPFNF----TAIggNLAGApALMGNVVLWKPSDTAVLSS 235
Cdd:cd07126 109 FLENFAGDQVRFLARSFNVPGDhqgqqSSGYRWPYGPVAIITPFNFpleiPAL--QLMGA-LFMGNKPLLKVDSKVSVVM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 236 YAVYKILLEAGLPPNVIQFVPASGPVFGDTVTSSEhFAGLNFTGSvptfkrlwKQVSENLDRyRTFPRLAGECGGKNFHL 315
Cdd:cd07126 186 EQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEAN-PRMTLFTGS--------SKVAERLAL-ELHGKVKLEDAGFDWKI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 316 VHSS-ADVPTVVNGTLRSAFEYGGQKCSACSRLYVPDlLWPQI----KAKLLEEHGKIK---VGdPAGDFETffsavidd 387
Cdd:cd07126 256 LGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHE-NWVQAgildKLKALAEQRKLEdltIG-PVLTWTT-------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 388 ksfARIKKWIQHAETSPNLTILAGGK------CDDKVGYfIEPC-----IVETKDPKD-RIMKEEIFGPVLAVYVYPEKQ 455
Cdd:cd07126 326 ---ERILDHVDKLLAIPGAKVLFGGKpltnhsIPSIYGA-YEPTavfvpLEEIAIEENfELVTTEVFGPFQVVTEYKDEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 456 YKDILQLVDTTsPYGLTGAVFAQDKNVIQEArkLLRNAAGNFY--INDKSTGAvvAQQ----PFGGARASGTNdkpggrh 529
Cdd:cd07126 402 LPLVLEALERM-HAHLTAAVVSNDIRFLQEV--LANTVNGTTYagIRARTTGA--PQNhwfgPAGDPRGAGIG------- 469
|
490
....*....|....
gi 1121863746 530 yilrwtSPQAIKET 543
Cdd:cd07126 470 ------TPEAIRLV 477
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
195-520 |
8.09e-07 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 51.65 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 195 GFVAAVSPFNFtAIGGNL---AGAPAlMGNVVLWKPSDTAVLSSYavykiLLEAGLP----PNVIQfVPASGPVFGDTVT 267
Cdd:PLN02203 110 GVVLIFSSWNF-PIGLSLeplIGAIA-AGNAVVLKPSELAPATSA-----FLAANIPkyldSKAVK-VIEGGPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 268 ssEH-FAGLNFTGSvptfKRLWKQVSENLDRYRTfPrLAGECGGKN---FHLVHSSADVPTVVNGTLRSAFEY-GGQKCS 342
Cdd:PLN02203 182 --QHkWDKIFFTGS----PRVGRIIMTAAAKHLT-P-VALELGGKCpciVDSLSSSRDTKVAVNRIVGGKWGScAGQACI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 343 ACSRLYVPDLLWPqIKAKLLEEHGKIKVGDPAGDFETFfSAVIDDKSFARIKKWIqhAETSPNLTILAGGKCDDKvGYFI 422
Cdd:PLN02203 254 AIDYVLVEERFAP-ILIELLKSTIKKFFGENPRESKSM-ARILNKKHFQRLSNLL--KDPRVAASIVHGGSIDEK-KLFI 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 423 EPCIVETKDPKDRIMKEEIFGPVLAVYVYpeKQYKDILQLVDtTSPYGLtgAVFAQDKNVIQEARKLLRNAAGNFYINDK 502
Cdd:PLN02203 329 EPTILLNPPLDSDIMTEEIFGPLLPIITV--KKIEDSIAFIN-SKPKPL--AIYAFTNNEKLKRRILSETSSGSVTFNDA 403
|
330
....*....|....*...
gi 1121863746 503 STGAVVAQQPFGGARASG 520
Cdd:PLN02203 404 IIQYACDSLPFGGVGESG 421
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
220-522 |
2.89e-05 |
|
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: 46.70 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 220 GNVVLWKPSDTAVLSSYAVYKI----LLEAGLPPNVIQFV--PASGPVFGDTVTSSEhFAGLNFTGSvPTFkrlwkqvSE 293
Cdd:cd07127 221 GNPVIVKPHPAAILPLAITVQVarevLAEAGFDPNLVTLAadTPEEPIAQTLATRPE-VRIIDFTGS-NAF-------GD 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 294 NLDRYRTFPRLAGECGGKNFHLVHSSADVPTVVNGTLRSAFEYGGQKCSACSRLYVPD---------LLWPQIKAKLLEE 364
Cdd:cd07127 292 WLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRdgiqtddgrKSFDEVAADLAAA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 365 HGKIkVGDPAGDFEtFFSAVIDDKSFARIKKWIQHAETSPNLTILAGGKCDDKVGYfiEPCIVETKDPKDRIMKEEIFGP 444
Cdd:cd07127 372 IDGL-LADPARAAA-LLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPDARVR--TPLLLKLDASDEAAYAEERFGP 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121863746 445 VLAVyVYPEKQYKDILQLVDTTSPYG-LTGAVFAQDKNVIQEARKLLRNAAGNFYINdkSTGAVVAQQP--FGGARASGT 521
Cdd:cd07127 448 IAFV-VATDSTDHSIELARESVREHGaMTVGVYSTDPEVVERVQEAALDAGVALSIN--LTGGVFVNQSaaFSDFHGTGA 524
|
.
gi 1121863746 522 N 522
Cdd:cd07127 525 N 525
|
|
| |
