|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
32-553 |
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: 1034.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 32 VANEPILAFTQGSPEREALQKALKDLKGQTEAIPCVVGDEEVWTLDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALA 111
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 112 ARKEWDLKPIADRAQIFLKAADMLSGPHRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEGQQPISVPPS 191
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 192 T-NSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFG 270
Cdd:cd07123 161 VwNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 271 DTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTFPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSA 350
Cdd:cd07123 241 DTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 351 CSRLYVPHSLWPQIKGRLLEEHGRIKVGDPaEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGKCDDSVGYFVE 430
Cdd:cd07123 321 ASRAYVPESLWPEVKERLLEELKEIKMGDP-DDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 431 PCIVESKDPQEPIMKEEIFGPVLTVYVYPDDKYKETLQLVDSTTSYGLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKS 510
Cdd:cd07123 400 PTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 795203903 511 TGSVVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKETHKP 553
Cdd:cd07123 480 TGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETFVP 522
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
33-563 |
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: 988.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 33 ANEPILAFTQGSPEREALQKALKDLKGQTEAIPCVVGDEEVWTLDV-QYQVSPFNHGHKVAKFCYADKSLLNKAIEAALA 111
Cdd:TIGR01236 1 ANEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEVYDSNErIPQVNPHNHQAVLAKATNATEEDAMKAVEAALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 112 ARKEWDLKPIADRAQIFLKAADMLSGPHRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEGQQPISVPPS 191
Cdd:TIGR01236 81 AKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPISAPGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 192 TNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGD 271
Cdd:TIGR01236 161 WNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 272 TVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTFPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSAC 351
Cdd:TIGR01236 241 QVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 352 SRLYVPHSLWPQIKGRLLEEHGRIKVGDPaEDFGTFFSAVIDAKSFARIKKWLEHARSSPS-LTILAGGKCDDSVGYFVE 430
Cdd:TIGR01236 321 SRLYVPHSKWPEFKSDLLAELQSVKVGDP-DDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEaLTILYGGKYDDSQGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 431 PCIVESKDPQEPIMKEEIFGPVLTVYVYPDDKYKETLQLVDSTTSYGLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKS 510
Cdd:TIGR01236 400 PTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYINDKC 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 795203903 511 TGSVVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKETHKPLGDWSYAYMQ 563
Cdd:TIGR01236 480 TGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
47-551 |
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: 806.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 47 REALQKALKDLKG-QTEAIPCVVGDEEVWTLDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRA 125
Cdd:cd07083 1 RRAMREALRRVKEeFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 126 QIFLKAADMLSGPHRAEILAKTMVGqGKTVIQaEIDAAAELIDFFRFNAKYAVELEGQQPI--SVPPSTNSTVYRGLeGF 203
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEV-GKNWVE-AIDDVAEAIDFIRYYARAALRLRYPAVEvvPYPGEDNESFYVGL-GA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 204 VAAISPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGI 282
Cdd:cd07083 158 GVVISPWNFPvAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 283 NFTGSVPTFKHLWKQVAQNLDRFRTFPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWP 362
Cdd:cd07083 238 NFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 363 QIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSspSLTILAGGKCDDSVGYFVEPCIVESKDPQEP 442
Cdd:cd07083 318 PVLERLLKRAERLSVGPPEEN-GTDLGPVIDAEQEAKVLSYIEHGKN--EGQLVLGGKRLEGEGYFVAPTVVEEVPPKAR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 443 IMKEEIFGPVLTVYVYPDDKYKETLQLVDSTTSYGLTGAVFSQdKDVVQEATKVLrnAAGNFYINDKSTGSVVGQQPFGG 522
Cdd:cd07083 395 IAQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRK-REHLEEARREF--HVGNLYINRKITGALVGVQPFGG 471
|
490 500
....*....|....*....|....*....
gi 795203903 523 ARASGTNDKPGGPHYILRWTSPQVIKETH 551
Cdd:cd07083 472 FKLSGTNAKTGGPHYLRRFLEMKAVAERF 500
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
103-547 |
7.14e-139 |
|
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: 409.29 E-value: 7.14e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPHRAEILAKTMVGqGKTVIQAEIDAAaELIDFFRFNAKYAVELEG 182
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLET-GKPIEEALGEVA-RAADTFRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 183 QQ-PISVPPSTNSTVYRGLeGFVAAISPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQ 260
Cdd:cd07078 79 EViPSPDPGELAIVRREPL-GVVGAITPWNFPlLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 261 FVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfrtfPRLAGECGGKNFHFVHCSADVDSVVSGTLRSA 340
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 341 FEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGK 420
Cdd:cd07078 232 FGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPL-DPDTDMGPLISAAQLDRVLAYIEDAKAEGA-KLLCGGK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 421 CDDS-VGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDKDVVQEATKVLRn 499
Cdd:cd07078 310 RLEGgKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDE--EEAIELANDTE-YGLAAGVFTRDLERALRVAERLE- 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 795203903 500 aAGNFYINDKSTGsVVGQQPFGGARASGTNdKPGGPHYILRWTSPQVI 547
Cdd:cd07078 386 -AGTVWINDYSVG-AEPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
61-551 |
5.32e-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: 408.75 E-value: 5.32e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 61 TEAIPCVVGDEEVW-----TLDVqyqVSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADML 135
Cdd:COG1012 3 TPEYPLFIGGEWVAaasgeTFDV---INPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 136 SGpHRAEILAKTMVGQGKTVIQAEIDAAaELIDFFRFNAKYAVELEGQQ-PISVPPSTNSTVYRGLeGFVAAISPFNFTA 214
Cdd:COG1012 79 EE-RREELAALLTLETGKPLAEARGEVD-RAADFLRYYAGEARRLYGETiPSDAPGTRAYVRREPL-GVVGAITPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 215 IGGNLAGAPAL-MGNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKH 293
Cdd:COG1012 156 ALAAWKLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 294 LWKQVAQNLdrfrtfPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHG 373
Cdd:COG1012 236 IAAAAAENL------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 374 RIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSpSLTILAGGKC-DDSVGYFVEPCIVESKDPQEPIMKEEIFGPV 452
Cdd:COG1012 310 ALKVGDPL-DPGTDMGPLISEAQLERVLAYIEDAVAE-GAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 453 LTVYVYPDdkYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGsVVGQQPFGGARASGTNDKp 532
Cdd:COG1012 388 LSVIPFDD--EEEAIALAND-TEYGLAASVFTRDLARARRVARRLE--AGMVWINDGTTG-AVPQAPFGGVKQSGIGRE- 460
|
490
....*....|....*....
gi 795203903 533 GGPHYILRWTSPQVIKETH 551
Cdd:COG1012 461 GGREGLEEYTETKTVTIRL 479
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
34-549 |
3.77e-132 |
|
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: 395.05 E-value: 3.77e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 34 NEPILAFTQGSpEREALQKALKDLK---GQTeaIPCVVGDEEVWTLDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAAL 110
Cdd:cd07124 3 NEPFTDFADEE-NRAAFRAALARVReelGRE--YPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 111 AARKEWDLKPIADRAQIFLKAADMLSgPHRAEiLAKTMVGQ-GKTVIQAEIDAAaELIDFFRFNAKYAVELEGQQPISVP 189
Cdd:cd07124 80 AAFPTWRRTPPEERARLLLRAAALLR-RRRFE-LAAWMVLEvGKNWAEADADVA-EAIDFLEYYAREMLRLRGFPVEMVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 190 PSTNSTVYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPL 268
Cdd:cd07124 157 GEDNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 269 FGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTFPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKC 348
Cdd:cd07124 236 VGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKC 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 349 SACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPaEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLtiLAGGKCDDSV--G 426
Cdd:cd07124 316 SACSRVIVHESVYDEFLERLVERTKALKVGDP-EDPEVYMGPVIDKGARDRIRRYIEIGKSEGRL--LLGGEVLELAaeG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 427 YFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDdkYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYI 506
Cdd:cd07124 393 YFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD--FDEALEIAND-TEYGLTGGVFSRSPEHLERARREFE--VGNLYA 467
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 795203903 507 NDKSTGSVVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKE 549
Cdd:cd07124 468 NRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTE 510
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
75-547 |
3.19e-122 |
|
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: 367.63 E-value: 3.19e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 75 TLDVqyqVSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGphRAEILAKTMV-GQGK 153
Cdd:pfam00171 8 TIEV---INPAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEE--RKDELAELETlENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 154 TVIQAEIDAAaELIDFFRFNAKYAVELEGQqPISVPPSTNSTVYRGLEGFVAAISPFNFTAiggNLAG---APALM-GNV 229
Cdd:pfam00171 82 PLAEARGEVD-RAIDVLRYYAGLARRLDGE-TLPSDPGRLAYTRREPLGVVGAITPWNFPL---LLPAwkiAPALAaGNT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 230 VLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfrtfP 309
Cdd:pfam00171 157 VVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------K 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 310 RLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPaEDFGTFFS 389
Cdd:pfam00171 231 RVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDP-LDPDTDMG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 390 AVIDAKSFARIKKWLEHARSSpSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQL 469
Cdd:pfam00171 310 PLISKAQLERVLKYVEDAKEE-GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDE--EEAIEI 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795203903 470 VDSTTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSVVGqQPFGGARASGTNDKpGGPHYILRWTSPQVI 547
Cdd:pfam00171 387 ANDTE-YGLAAGVFTSDLERALRVARRLE--AGMVWINDYTTGDADG-LPFGGFKQSGFGRE-GGPYGLEEYTEVKTV 459
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
34-550 |
1.51e-115 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 352.31 E-value: 1.51e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 34 NEPILAFTQgsPE-REALQKALKDLKGQT-EAIPCVVGDEEVWTLDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALA 111
Cdd:PRK03137 7 HEPFTDFSV--EEnVEAFEEALKKVEKELgQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 112 ARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMVGQ-GKTVIQAEIDAAaELIDFFRFNAKYAVEL-EGQQPISVP 189
Cdd:PRK03137 85 AFETWKKWSPEDRARILLRAAAIIR--RRKHEFSAWLVKEaGKPWAEADADTA-EAIDFLEYYARQMLKLaDGKPVESRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 190 PSTNSTVYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPL 268
Cdd:PRK03137 162 GEHNRYFYIPL-GVGVVISPWNFpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 269 FGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTFPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKC 348
Cdd:PRK03137 241 VGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 349 SACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfgTFFSAVIDAKSFARIKKWLEHARSSPSLtiLAGGKCDDSVGYF 428
Cdd:PRK03137 321 SACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN--AYMGPVINQASFDKIMSYIEIGKEEGRL--VLGGEGDDSKGYF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 429 VEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDdkYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIND 508
Cdd:PRK03137 397 IQPTIFADVDPKARIMQEEIFGPVVAFIKAKD--FDHALEIANN-TEYGLTGAVISNNREHLEKARREFH--VGNLYFNR 471
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 795203903 509 KSTGSVVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKET 550
Cdd:PRK03137 472 GCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEM 513
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
34-549 |
6.98e-102 |
|
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: 317.19 E-value: 6.98e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 34 NEPILAFTQgSPEREALQKAL---KDLKGQTeaIPCVVGDEEVWTLDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAAL 110
Cdd:TIGR01237 3 HEPFTDFAD-EENRQAFFKALatvKEQLGKT--YPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 111 AARKEWDLKPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGKTVIQAEIDAAaELIDFFRFNAKYAVELEGQQPI-SVP 189
Cdd:TIGR01237 80 KAFEAWKKTDPEERAAILFKAAAIVR-RRRHEFSALLVKEVGKPWNEADAEVA-EAIDFMEYYARQMIELAKGKPVnSRE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 190 PSTNSTVYRGLeGFVAAISPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPL 268
Cdd:TIGR01237 158 GETNQYVYTPT-GVTVVISPWNFPfAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 269 FGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTFPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKC 348
Cdd:TIGR01237 237 VGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 349 SACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPaEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTIlaGGKCDDSVGYF 428
Cdd:TIGR01237 317 SAGSRAVVHEKVYDEVVERFVEITESLKVGPP-DSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVS--GGCGDDSKGYF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 429 VEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDdkYKETLQLVDSTtSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIND 508
Cdd:TIGR01237 394 IGPTIFADVDRKARLAQEEIFGPVVAFIRASD--FDEALEIANNT-EYGLTGGVISNNRDHINRAKAEFE--VGNLYFNR 468
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 795203903 509 KSTGSVVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKE 549
Cdd:TIGR01237 469 NITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKTVTE 509
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
107-547 |
8.13e-102 |
|
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: 311.86 E-value: 8.13e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 107 EAALAARKEWDLKPIADRAQIFLKAADMLSGPHRAEILAKTMVGqGKTvIQAEIDAAAELIDFFRFNAKYAVELEGQQPI 186
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLET-GKP-IEEALGEVARAIDTFRYAAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 187 SVPPSTNSTVYRGLEGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPAD 265
Cdd:cd06534 79 SPDPGGEAYVRREPLGVVGVITPWNFpLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 266 GPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfrtfPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGG 345
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 346 QKCSACSRLYVPHSLWPQIKGRLLeehgrikvgdpaedfgtffsavidaksfarikkwleharsspsltilaggkcddsv 425
Cdd:cd06534 233 QICTAASRLLVHESIYDEFVEKLV-------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 426 gyfvepCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFY 505
Cdd:cd06534 257 ------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDE--EEAIALANDTE-YGLTAGVFTRDLNRALRVAERLR--AGTVY 325
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 795203903 506 INDKSTGsVVGQQPFGGARASGTNDKpGGPHYILRWTSPQVI 547
Cdd:cd06534 326 INDSSIG-VGPEAPFGGVKNSGIGRE-GGPYGLEEYTRTKTV 365
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
33-540 |
2.56e-96 |
|
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: 302.96 E-value: 2.56e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 33 ANEPIL-AFTQGSPEREALQKALKDLK-GQTEAIPCVVGDEEVW--TLDVqyqVSPFNHGHKVAKFCYADKSLLNKAIEA 108
Cdd:cd07125 1 ANSSFVnRIFDLEVPLEALADALKAFDeKEWEAIPIINGEETETgeGAPV---IDPADHERTIGEVSLADAEDVDAALAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 109 ALAARKEWDLKPIADRAQIFLKAADMLSGpHRAEILAKTMVGQGKTVIQAeIDAAAELIDFFRFNAKYAVELEGQQPISV 188
Cdd:cd07125 78 AAAAFAGWSATPVEERAEILEKAADLLEA-NRGELIALAAAEAGKTLADA-DAEVREAIDFCRYYAAQARELFSDPELPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 189 PPS-TNSTVYRGLeGFVAAISPFNF---TAIGGNLAgapALM-GNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVP 263
Cdd:cd07125 156 PTGeLNGLELHGR-GVFVCISPWNFplaIFTGQIAA---ALAaGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 264 ADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldRFRTFPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEY 343
Cdd:cd07125 232 GDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAE---RDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 344 GGQKCSACSRLYVPHSLWP----QIKGRLLEehgrIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSPSLtiLAGG 419
Cdd:cd07125 309 AGQRCSALRLLYLQEEIAErfieMLKGAMAS----LKVGDPW-DLSTDVGPLIDKPAGKLLRAHTELMRGEAWL--IAPA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 420 KCDDSVGYFVEPCIVESKDPQEpiMKEEIFGPVLTVYVYPDDKYKETLQLVDSTtSYGLTGAVFSQDKDvvqEATKVLRN 499
Cdd:cd07125 382 PLDDGNGYFVAPGIIEIVGIFD--LTTEVFGPILHVIRFKAEDLDEAIEDINAT-GYGLTLGIHSRDER---EIEYWRER 455
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 795203903 500 A-AGNFYINDKSTGSVVGQQPFGGARASGTNDKPGGPHYILR 540
Cdd:cd07125 456 VeAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLR 497
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
44-547 |
7.98e-79 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 267.83 E-value: 7.98e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 44 SPEREALQKALKDLKGQT-EAIPCVVGDEEVWTLdvqyqVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIA 122
Cdd:PRK11904 533 RSELEPLAAAIAAFLEKQwQAGPIINGEGEARPV-----VSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 123 DRAQIFLKAADMLSGpHRAEILAKTMVGQGKTVIQAeIDAAAELIDFFRFnakYAVELEGQ--QPISVPPSTNSTVYRGL 200
Cdd:PRK11904 608 ERAAILERAADLLEA-NRAELIALCVREAGKTLQDA-IAEVREAVDFCRY---YAAQARRLfgAPEKLPGPTGESNELRL 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 201 EG---FVAaISPFNFT-AIggnLAG--APALM-GNVVLWKPSD-TAMLASYAIyRVLREAGLPPNIIQFVPADGPLFGDT 272
Cdd:PRK11904 683 HGrgvFVC-ISPWNFPlAI---FLGqvAAALAaGNTVIAKPAEqTPLIAAEAV-KLLHEAGIPKDVLQLLPGDGATVGAA 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 273 VTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfRTFP--RLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSA 350
Cdd:PRK11904 758 LTADPRIAGVAFTGSTETARIINRTLAA-----RDGPivPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSA 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 351 CSRLYVPHSLWPQ----IKGRLLEehgrIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSPslTILAGGKCDDS-- 424
Cdd:PRK11904 833 LRVLFVQEDIADRviemLKGAMAE----LKVGDPR-LLSTDVGPVIDAEAKANLDAHIERMKREA--RLLAQLPLPAGte 905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 425 VGYFVEPCIVESKDPQEpiMKEEIFGPVLTVYVYpddKYKETLQLVDS--TTSYGLTGAVFSQDKDVVQEATKVLRnaAG 502
Cdd:PRK11904 906 NGHFVAPTAFEIDSISQ--LEREVFGPILHVIRY---KASDLDKVIDAinATGYGLTLGIHSRIEETADRIADRVR--VG 978
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 795203903 503 NFYINDKSTGSVVGQQPFGGARASGTNDKPGGPHYILRWTSPQVI 547
Cdd:PRK11904 979 NVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
46-547 |
5.38e-77 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 264.11 E-value: 5.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 46 EREALQKALKDLKGQT-EAIPCVVGDEEvwTLDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADR 124
Cdd:COG4230 540 VLAALSAALAAAAEKQwQAAPLIAGEAA--SGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEER 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 125 AQIFLKAADMLSGpHRAEILAKTMVGQGKTvIQaeiDAAAEL---IDFFRFnakYAVELEGQQpisvppsTNSTVYRGLe 201
Cdd:COG4230 618 AAILERAADLLEA-HRAELMALLVREAGKT-LP---DAIAEVreaVDFCRY---YAAQARRLF-------AAPTVLRGR- 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 202 GFVAAISPFNFTaiggnLAG-----APALM-GNVVLWKPSD-TAMLASYAIyRVLREAGLPPNIIQFVPADGPLFGDTVT 274
Cdd:COG4230 682 GVFVCISPWNFP-----LAIftgqvAAALAaGNTVLAKPAEqTPLIAARAV-RLLHEAGVPADVLQLLPGDGETVGAALV 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 275 SSEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTFprLAgECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRL 354
Cdd:COG4230 756 ADPRIAGVAFTGSTETARLINRTLAARDGPIVPL--IA-ETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVL 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 355 YVPHSLWPQ----IKGRLLEehgrIKVGDPAE---DFGtffsAVIDAKSFARIKKWLEHARSSPslTILAGGKCDDSV-- 425
Cdd:COG4230 833 CVQEDIADRvlemLKGAMAE----LRVGDPADlstDVG----PVIDAEARANLEAHIERMRAEG--RLVHQLPLPEECan 902
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 426 GYFVEPCIVESKDPQEpiMKEEIFGPVLTVYVYpddKYKETLQLVDS--TTSYGLTGAVFSQDKDVVQEATKVLRnaAGN 503
Cdd:COG4230 903 GTFVAPTLIEIDSISD--LEREVFGPVLHVVRY---KADELDKVIDAinATGYGLTLGVHSRIDETIDRVAARAR--VGN 975
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 795203903 504 FYINDKSTGSVVGQQPFGGARASGTNDKPGGPHYILRWTSPQVI 547
Cdd:COG4230 976 VYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTV 1019
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
77-536 |
1.55e-72 |
|
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: 239.46 E-value: 1.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 77 DVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGphRAEILAKTMV-GQGKTV 155
Cdd:cd07097 14 DGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEA--RKEELARLLTrEEGKTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 156 IQA--EIDAAaelIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNF-TAIGGNLAgAPALM-GNVVL 231
Cdd:cd07097 92 PEArgEVTRA---GQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFpIAIPAWKI-APALAyGNTVV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 232 WKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTfprl 311
Cdd:cd07097 168 FKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQL---- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 312 agECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAV 391
Cdd:cd07097 244 --EMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE-GVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 392 IDAKSFARIKKWLEHARSSPSlTILAGG---KCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDdkYKETLQ 468
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGA-KLVYGGerlKRPDE-GYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRD--YDEALA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795203903 469 LVDStTSYGLTGAVFSQDkdvVQEATKVLRNA-AGNFYINDKSTGsVVGQQPFGGARASGTNDKPGGPH 536
Cdd:cd07097 397 IAND-TEFGLSAGIVTTS---LKHATHFKRRVeAGVVMVNLPTAG-VDYHVPFGGRKGSSYGPREQGEA 460
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
33-544 |
3.06e-69 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 242.46 E-value: 3.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 33 ANEPILAftqgspereALQKALKDLKGQT-EAIPCVVGDEevwTLDVQYQV-SPFNHGHKVAKFCYADKSLLNKAIEAAL 110
Cdd:PRK11905 533 SDEATLA---------ALDEALNAFAAKTwHAAPLLAGGD---VDGGTRPVlNPADHDDVVGTVTEASAEDVERALAAAQ 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 111 AARKEWDLKPIADRAQIFLKAADMLSGpHRAEILAKTMVGQGKTVIqaeiDAAAEL---IDFFRFNAKYAVELEGQQPIs 187
Cdd:PRK11905 601 AAFPEWSATPAAERAAILERAADLMEA-HMPELFALAVREAGKTLA----NAIAEVreaVDFLRYYAAQARRLLNGPGH- 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 188 vppstnstvyRGLeGFVAAISPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAMLASYAIyRVLREAGLPPNIIQFVPA 264
Cdd:PRK11905 675 ----------KPL-GPVVCISPWNFPlAIfTGQIAAALV-AGNTVLAKPAEqTPLIAARAV-RLLHEAGVPKDALQLLPG 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 265 DGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFrtfPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYG 344
Cdd:PRK11905 742 DGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPP---VPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSA 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 345 GQKCSACSRLYVPHSLWPQI----KGRLLEehgrIKVGDPAE---DFGtffsAVIDAKSFARIKKWLEHARSSPSL--TI 415
Cdd:PRK11905 819 GQRCSALRVLCLQEDVADRVltmlKGAMDE----LRIGDPWRlstDVG----PVIDAEAQANIEAHIEAMRAAGRLvhQL 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 416 LAGGKCDDsvGYFVEPCIVESKDPQEpiMKEEIFGPVLTVYVYpddKYKETLQLVDS--TTSYGLTGAVFSQDKDVVQEA 493
Cdd:PRK11905 891 PLPAETEK--GTFVAPTLIEIDSISD--LEREVFGPVLHVVRF---KADELDRVIDDinATGYGLTFGLHSRIDETIAHV 963
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 795203903 494 TKvlRNAAGNFYINDKSTGSVVGQQPFGGARASGTNDKPGGPHYILRWTSP 544
Cdd:PRK11905 964 TS--RIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVRE 1012
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
102-543 |
2.52e-67 |
|
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: 224.33 E-value: 2.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 102 LNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGKTVIQAEIDAAAElIDFFRFNAKYAVELE 181
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILE-ERRDEIADWLIRESGSTRPKAAFEVGAA-IAILREAAGLPRRPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 182 GQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPS-DTAMLASYAIYRVLREAGLPPNII 259
Cdd:cd07104 80 GEILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDsRTPVTGGLLIAEIFEEAGLPKGVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 260 QFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfRTFPRLAGECGGKNFHFVHCSADVDSVVSGTLRS 339
Cdd:cd07104 160 NVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAG------RHLKKVALELGGNNPLIVLDDADLDLAVSAAAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 340 AFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSpSLTILAGG 419
Cdd:cd07104 234 AFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDP-DTVIGPLINERQVDRVHAIVEDAVAA-GARLLTGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 420 KCDdsvGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLRN 499
Cdd:cd07104 312 TYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDD--EEAVELAND-TEYGLSAAVFTRD---LERAMAFAER 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 795203903 500 A-AGNFYINDKST--GSVVgqqPFGGARASGTnDKPGGPHYI-----LRWTS 543
Cdd:cd07104 383 LeTGMVHINDQTVndEPHV---PFGGVKASGG-GRFGGPASLeefteWQWIT 430
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
83-528 |
6.92e-67 |
|
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: 224.01 E-value: 6.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 83 SPFnHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMVGQ-GKTVIQA--E 159
Cdd:cd07149 5 SPY-DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLE--ERREEFARTIALEaGKPIKDArkE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 160 IDAAaelIDFFRFNAKYAVELEGQQ-PISVPPSTNSTV---YRGLEGFVAAISPFNFTAiggNLAG---APALM-GNVVL 231
Cdd:cd07149 82 VDRA---IETLRLSAEEAKRLAGETiPFDASPGGEGRIgftIREPIGVVAAITPFNFPL---NLVAhkvGPAIAaGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 232 WKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfrtFPRL 311
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 312 AGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAV 391
Cdd:cd07149 228 TLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDE-DTDVGPM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 392 IDAKSFARIKKWLEHARSSPSlTILAGGKCDdsvGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYpdDKYKETLQLVD 471
Cdd:cd07149 307 ISEAEAERIEEWVEEAVEGGA-RLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPF--DTLDEAIAMAN 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 795203903 472 StTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSvVGQQPFGGARASGT 528
Cdd:cd07149 381 D-SPYGLQAGVFTNDLQKALKAARELE--VGGVMINDSSTFR-VDHMPYGGVKESGT 433
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
97-547 |
1.21e-64 |
|
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: 217.78 E-value: 1.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 97 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpHRAEILAKTMVGQGKTVIQA--EIDAAAeliDFFRFNA 174
Cdd:cd07106 16 ASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEA-NAEELARLLTLEQGKPLAEAqfEVGGAV---AWLRYTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 175 KYAVELEGQQpiSVPPSTNSTVYRGLeGFVAAISPFNFTAIggnLAG---APALM-GNVVLWKPSDTAMLASYAIYRVLR 250
Cdd:cd07106 92 SLDLPDEVIE--DDDTRRVELRRKPL-GVVAAIVPWNFPLL---LAAwkiAPALLaGNTVVLKPSPFTPLCTLKLGELAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 251 EAgLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfrtfprLAGECGGKNFHFVHCSADVD 330
Cdd:cd07106 166 EV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTLKR------VTLELGGNDAAIVLPDVDID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 331 SVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSS 410
Cdd:cd07106 238 AVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDP-GTTLGPVQNKMQYDKVKELVEDAKAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 411 pSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvV 490
Cdd:cd07106 317 -GAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDE--DEVIARAND-SEYGLGASVWSSD---L 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 795203903 491 QEATKV-LRNAAGNFYINdkSTGSVVGQQPFGGARASGTndkpG---GPHYILRWTSPQVI 547
Cdd:cd07106 390 ERAEAVaRRLEAGTVWIN--THGALDPDAPFGGHKQSGI----GvefGIEGLKEYTQTQVI 444
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
25-545 |
1.35e-64 |
|
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: 219.40 E-value: 1.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 25 KHTSSLKVANEPILAFTQGSPEREALQKalkdlkgqTEAIPcVVGDEEVWTLDVQYQVSPFNHGHKVAKFCYADKSLLNK 104
Cdd:TIGR01238 8 KNSLGIDLDNESELKPLEAQIHAWADKT--------WQAAP-IIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGKTVIQAeIDAAAELIDFFRFNAKYAVELEGQQ 184
Cdd:TIGR01238 79 AIDSAQQAFPTWNATPAKERAAKLDRLADLLE-LHMPELMALCVREAGKTIHNA-IAEVREAVDFCRYYAKQVRDVLGEF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 185 piSVPPstnstvyrglEGFVAAISPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAMLASYAIyRVLREAGLPPNIIQF 261
Cdd:TIGR01238 157 --SVES----------RGVFVCISPWNFPlAIfTGQISAALA-AGNTVIAKPAEqTSLIAYRAV-ELMQEAGFPAGTIQL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 262 VPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfRTFPRLAgECGGKNFHFVHCSADVDSVVSGTLRSAF 341
Cdd:TIGR01238 223 LPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRED--APVPLIA-ETGGQNAMIVDSTALPEQVVRDVLRSAF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 342 EYGGQKCSACSRLYVPHSLWPQ----IKGRLLEehgrIKVGDPAEdFGTFFSAVIDAKSFARIKKWLEH----ARSSPSL 413
Cdd:TIGR01238 300 DSAGQRCSALRVLCVQEDVADRvltmIQGAMQE----LKVGVPHL-LTTDVGPVIDAEAKQNLLAHIEHmsqtQKKIAQL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 414 TILAGGKCDDsvGYFVEPCIVESKDPQEpiMKEEIFGPVLTVYVYpddKYKETLQLVD--STTSYGLTGAVFSQDKDVVQ 491
Cdd:TIGR01238 375 TLDDSRACQH--GTFVAPTLFELDDIAE--LSEEVFGPVLHVVRY---KARELDQIVDqiNQTGYGLTMGVHSRIETTYR 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 795203903 492 EATKVLRnaAGNFYINDKSTGSVVGQQPFGGARASGTNDKPGGPHYILRWTSPQ 545
Cdd:TIGR01238 448 WIEKHAR--VGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
105-528 |
1.97e-64 |
|
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: 217.60 E-value: 1.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMVGQ-GKTVIQA--EIDAAAELidfFRFNAKYAVELE 181
Cdd:cd07145 26 AIEVAEKAKDVMSNLPAYKRYKILMKVAELIE--RRKEELAKLLTIEvGKPIKQSrvEVERTIRL---FKLAAEEAKVLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 182 GQqpisVPPSTNstvYRGLE-----------GFVAAISPFNFTAiggNLAG---APAL-MGNVVLWKPSDTAMLASYAIY 246
Cdd:cd07145 101 GE----TIPVDA---YEYNErriaftvrepiGVVGAITPFNFPA---NLFAhkiAPAIaVGNSVVVKPSSNTPLTAIELA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 247 RVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfRTFPRLAGECGGKNFHFVHCS 326
Cdd:cd07145 171 KILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG------GTGKKVALELGGSDPMIVLKD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 327 ADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEH 406
Cdd:cd07145 245 ADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDE-STDLGPLISPEAVERMENLVND 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 407 ARSSPSlTILAGGKCDDsvGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTGAVFSQD 486
Cdd:cd07145 324 AVEKGG-KILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDD--EEAVEIANS-TEYGLQASVFTND 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 795203903 487 kdvVQEATKVLRN-AAGNFYINDkSTGSVVGQQPFGGARASGT 528
Cdd:cd07145 398 ---INRALKVARElEAGGVVIND-STRFRWDNLPFGGFKKSGI 436
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
75-507 |
6.26e-64 |
|
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: 216.36 E-value: 6.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 75 TLDVqyqVSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMVG-QGK 153
Cdd:cd07088 14 TIDV---LNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIR--ENADELAKLIVEeQGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 154 TVIQA--EIDAAAeliDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIggnLAG---APALM-G 227
Cdd:cd07088 88 TLSLArvEVEFTA---DYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFF---LIArklAPALVtG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 228 NVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfrT 307
Cdd:cd07088 162 NTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI----T 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 308 FPRLagECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTF 387
Cdd:cd07088 238 KVSL--ELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDA-ATD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 388 FSAVIDAKSFARIKKWLEHARSSPSlTILAGGKCDDS-VGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYpdDKYKET 466
Cdd:cd07088 315 MGPLVNEAALDKVEEMVERAVEAGA-TLLTGGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKF--SSLDEA 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 795203903 467 LQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIN 507
Cdd:cd07088 392 IELAND-SEYGLTSYIYTENLNTAMRATNELE--FGETYIN 429
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
103-543 |
9.51e-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: 215.66 E-value: 9.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEG 182
Cdd:cd07150 24 ERAIAAAYDAFPAWAATTPSERERILLKAAEIME--RRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVRG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 183 QQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQF 261
Cdd:cd07150 102 ETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 262 VPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfRTFPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAF 341
Cdd:cd07150 182 VTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG------RHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 342 EYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGKC 421
Cdd:cd07150 256 MHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPR-DPDTVIGPLISPRQVERIKRQVEDAVAKGA-KLLTGGKY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 422 DdsvGYFVEPCIVESKDPQEPIMKEEIFGPVltVYVYPDDKYKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLRNA- 500
Cdd:cd07150 334 D---GNFYQPTVLTDVTPDMRIFREETFGPV--TSVIPAKDAEEALELAND-TEYGLSAAILTND---LQRAFKLAERLe 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 795203903 501 AGNFYINDkSTGSVVGQQPFGGARASGTNdKPGGPHYI-----LRWTS 543
Cdd:cd07150 405 SGMVHIND-PTILDEAHVPFGGVKASGFG-REGGEWSMeefteLKWIT 450
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
82-528 |
3.63e-63 |
|
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: 213.97 E-value: 3.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpHRAEILAKTMVGQGKTVIQA--- 158
Cdd:cd07093 2 FNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEA-RADELALLESLDTGKPITLArtr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 159 EIDAAAElidFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFTAIggnLAG---APAL-MGNVVLWKP 234
Cdd:cd07093 80 DIPRAAA---NFRFFADYILQLDGESYPQDGGALNYVLRQPV-GVAGLITPWNLPLM---LLTwkiAPALaFGNTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 235 SDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFrTFprlagE 314
Cdd:cd07093 153 SEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPV-SL-----E 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 315 CGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPaEDFGTFFSAVIDA 394
Cdd:cd07093 227 LGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDP-LDPDTEVGPLISK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 395 KSFARIKKWLEHARSSPSlTILAGGKCDDSV----GYFVEPCIVESKDPQEPIMKEEIFGPVLTvyVYPDDKYKETLQLV 470
Cdd:cd07093 306 EHLEKVLGYVELARAEGA-TILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVT--VIPFDDEEEAIELA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795203903 471 DSTTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIN-----DKSTgsvvgqqPFGGARASGT 528
Cdd:cd07093 383 NDTP-YGLAAYVWTRDLGRAHRVARRLE--AGTVWVNcwlvrDLRT-------PFGGVKASGI 435
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
91-542 |
5.55e-63 |
|
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: 214.13 E-value: 5.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 91 VAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMVGQ-GKTVIQAEIDAAaELIDF 169
Cdd:cd07131 28 VGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLK--KRKEELARLVTREmGKPLAEGRGDVQ-EAIDM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 170 FRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAIYRV 248
Cdd:cd07131 105 AQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFpVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVEL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 249 LREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfRTFPRLAGECGGKNFHFVHCSAD 328
Cdd:cd07131 185 FAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA------RPNKRVALEMGGKNPIIVMDDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 329 VDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHAR 408
Cdd:cd07131 259 LDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDE-ETDMGPLINEAQLEKVLNYNEIGK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 409 SSpSLTILAGG----KCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVltVYVYPDDKYKETLQLVDStTSYGLTGAVFS 484
Cdd:cd07131 338 EE-GATLLLGGerltGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPV--VALIEVSSLEEAIEIAND-TEYGLSSAIYT 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 795203903 485 QDkdvVQEATKVLRNA-AGNFYINDKSTGSVVgQQPFGGARASGTNDKPGGPHYILRWT 542
Cdd:cd07131 414 ED---VNKAFRARRDLeAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGTTALDAFT 468
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
88-527 |
2.44e-62 |
|
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: 211.91 E-value: 2.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMV-GQGKTVIQA--EIDAAA 164
Cdd:cd07103 7 GEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIR--ERAEDLARLLTlEQGKPLAEArgEVDYAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 165 eliDFFRFNAKYAVELEGQqpiSVPPSTNST---VYRGLEGFVAAISPFNFTAigGNLA--GAPAL-MGNVVLWKPSDTA 238
Cdd:cd07103 85 ---SFLEWFAEEARRIYGR---TIPSPAPGKrilVIKQPVGVVAAITPWNFPA--AMITrkIAPALaAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 239 MLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfrtfpRLAGECGGk 318
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVK------RVSLELGG- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 319 NFHFVHC-SADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSF 397
Cdd:cd07103 230 NAPFIVFdDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDE-GTDMGPLINERAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 398 ARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYG 477
Cdd:cd07103 309 EKVEALVEDAVAKGA-KVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTE--DEVIARAND-TPYG 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 795203903 478 LTGAVFSQDKDVVQEATKVLRnaAGNFYINdksTGSVVG-QQPFGGARASG 527
Cdd:cd07103 385 LAAYVFTRDLARAWRVAEALE--AGMVGIN---TGLISDaEAPFGGVKESG 430
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
82-527 |
2.46e-62 |
|
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: 212.42 E-value: 2.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTM---VGQGKTVIQA 158
Cdd:cd07086 18 RNPAN-GEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALR--KKKEALGRLVsleMGKILPEGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 159 EIDaaaELIDFfrfnAKYAVELEGQQPISVPPSTNS-----TVYRGLeGFVAAISPFNF-TAIGG-NLAgaPALM-GNVV 230
Cdd:cd07086 95 EVQ---EMIDI----CDYAVGLSRMLYGLTIPSERPghrlmEQWNPL-GVVGVITAFNFpVAVPGwNAA--IALVcGNTV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 231 LWKPSDTAMLASYAIY----RVLREAGLPPNIIQFVPADGPlFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfR 306
Cdd:cd07086 165 VWKPSETTPLTAIAVTkilaEVLEKNGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVA------R 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 307 TFPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGT 386
Cdd:cd07086 238 RFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE-GT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 387 FFSAVIDAKSFARIKKWLEHARSSpSLTILAGGKC--DDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLtvYVYPDDKYK 464
Cdd:cd07086 317 LVGPLINQAAVEKYLNAIEIAKSQ-GGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPIL--YVIKFDSLE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795203903 465 ETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLRNA---AGNFYINDKSTGSVVGqQPFGGARASG 527
Cdd:cd07086 394 EAIAINND-VPQGLSSSIFTED---LREAFRWLGPKgsdCGIVNVNIPTSGAEIG-GAFGGEKETG 454
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
82-527 |
3.44e-62 |
|
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: 212.17 E-value: 3.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGKTVIQAE 159
Cdd:cd07119 18 INPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIR-EDAEELARLETLNTGKTLRESE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 160 IDAAaELIDFFRFNAKYAVELEGQQpISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTA 238
Cdd:cd07119 96 IDID-DVANCFRYYAGLATKETGEV-YDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAaGNTVVIKPSEVT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 239 MLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfrtFPRLAGECGGK 318
Cdd:cd07119 174 PLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN------VKKVALELGGK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 319 NFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPaEDFGTFFSAVIDAKSFA 398
Cdd:cd07119 248 NPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNG-LDADTEMGPLVSAEHRE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 399 RIKKWLEHARSSPSlTILAGGK------CDDsvGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDS 472
Cdd:cd07119 327 KVLSYIQLGKEEGA-RLVCGGKrptgdeLAK--GYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE--EEAIRLAND 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 795203903 473 TTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDksTGSVVGQQPFGGARASG 527
Cdd:cd07119 402 TP-YGLAGAVWTKDIARANRVARRLR--AGTVWIND--YHPYFAEAPWGGYKQSG 451
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
74-527 |
1.69e-61 |
|
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: 209.85 E-value: 1.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 74 WTLDVQyqvSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGK 153
Cdd:cd07151 10 RTIDVL---NPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILE-ERRDEIVEWLIRESGS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 154 TVIQAEIDAAAElIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAiggNLAG---APAL-MGNV 229
Cdd:cd07151 85 TRIKANIEWGAA-MAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPL---HLSMrsvAPALaLGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 230 VLWKP-SDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfrtf 308
Cdd:cd07151 161 VVLKPaSDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 309 pRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFF 388
Cdd:cd07151 236 -KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDP-DTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 389 SAVIDAKSFARIKKWLEHARSSpSLTILAGGKCDDSVgyfVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQ 468
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEE-GATLLVGGEAEGNV---LEPTVLSDVTNDMEIAREEIFGPVAPIIKADDE--EEALE 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795203903 469 LVDStTSYGLTGAVFSQDkdvVQEATKV-LRNAAGNFYINDKStgsvVGQQP---FGGARASG 527
Cdd:cd07151 388 LAND-TEYGLSGAVFTSD---LERGVQFaRRIDAGMTHINDQP----VNDEPhvpFGGEKNSG 442
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
88-527 |
2.26e-61 |
|
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: 209.22 E-value: 2.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpHRAEILAKTMVGQGKTVIQAEIDAAAELI 167
Cdd:cd07115 7 GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILA-NADELARLESLDTGKPIRAARRLDVPRAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 168 DFFRFNAKYAVELEGQQ-PISvPPSTNSTVyRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAI 245
Cdd:cd07115 86 DTFRYYAGWADKIEGEViPVR-GPFLNYTV-REPVGVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELTPLSALRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 246 YRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfrtfprLAGECGGKNFHFVHC 325
Cdd:cd07115 164 AELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKR------VSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 326 SADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLE 405
Cdd:cd07115 238 DADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPL-DPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 406 HARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQ 485
Cdd:cd07115 317 VGREEGA-RLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDE--EEALRIANGTE-YGLAAGVWTR 392
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 795203903 486 DKDVVQEATKVLRnaAGNFYINdkSTGSVVGQQPFGGARASG 527
Cdd:cd07115 393 DLGRAHRVAAALK--AGTVWIN--TYNRFDPGSPFGGYKQSG 430
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
82-527 |
1.71e-60 |
|
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: 206.90 E-value: 1.71e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMVGQ-GKTVIQA-- 158
Cdd:cd07094 4 HNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLK--KRAEEFAKIIACEgGKPIKDArv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 159 EIDAAaelIDFFRFNAKYAVELEGQQpISVPPSTNSTVYRGLE-----GFVAAISPFNFTAiggNLAG---APAL-MGNV 229
Cdd:cd07094 81 EVDRA---IDTLRLAAEEAERIRGEE-IPLDATQGSDNRLAWTirepvGVVLAITPFNFPL---NLVAhklAPAIaTGCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 230 VLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfrtFP 309
Cdd:cd07094 154 VVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--------GK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 310 RLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFS 389
Cdd:cd07094 226 RIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDE-DTDVG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 390 AVIDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVgyfVEPCIVESKDPQEPIMKEEIFGPVLTVYVYpdDKYKETLQL 469
Cdd:cd07094 305 PLISEEAAERVERWVEEAVEAGA-RLLCGGERDGAL---FKPTVLEDVPRDTKLSTEETFGPVVPIIRY--DDFEEAIRI 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 795203903 470 VDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDkSTGSVVGQQPFGGARASG 527
Cdd:cd07094 379 ANS-TDYGLQAGIFTRDLNVAFKAAEKLE--VGGVMVND-SSAFRTDWMPFGGVKESG 432
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
88-527 |
3.63e-60 |
|
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: 206.39 E-value: 3.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGKTV--IQAEIDAAAE 165
Cdd:cd07090 7 GEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLR-ERNDEIARLETIDNGKPIeeARVDIDSSAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 166 LIDFFrfnAKYAVELEGQQpisVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLAS 242
Cdd:cd07090 86 CLEYY---AGLAPTLSGEH---VPLPGGSFAYTRREplGVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 243 YAIYRVLREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfrtfprLAGECGGKNFHF 322
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKH------VTLELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 323 VHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAeDFGTFFSAVIDAKSFARIKK 402
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPL-DEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 403 WLEHARSSPSlTILAGG-------KCDDsvGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYpdDKYKETLQLVDSTTs 475
Cdd:cd07090 312 YIESAKQEGA-KVLCGGervvpedGLEN--GFYVSPCVLTDCTDDMTIVREEIFGPVMSILPF--DTEEEVIRRANDTT- 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 795203903 476 YGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINDKSTGSVvgQQPFGGARASG 527
Cdd:cd07090 386 YGLAAGVFTRD---LQRAHRVIAQlQAGTCWINTYNISPV--EVPFGGYKQSG 433
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
88-545 |
6.24e-59 |
|
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: 203.44 E-value: 6.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 88 GHKVAKFCYADKSLLNKAIEAALAA-RKEWDLKPIADRAQIFLKAADMLSGpHRAEILAKTMVGQGKTVIQAEIDAAAEL 166
Cdd:cd07113 25 EQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQ-HGEELAQLETLCSGKSIHLSRAFEVGQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 167 IDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLE-----GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAML 240
Cdd:cd07113 104 ANFLRYFAGWATKINGETLAPSIPSMQGERYTAFTrrepvGVVAGIVPWNFSVMIAVWKIGAALAtGCTIVIKPSEFTPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 241 ASYAIYRVLREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTfprlagECGGKNF 320
Cdd:cd07113 184 TLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTL------ELGGKNA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 321 HFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARI 400
Cdd:cd07113 257 AAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE-SVMFGPLANQPHFDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 401 KKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTG 480
Cdd:cd07113 336 CSYLDDARAEGD-EIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDE--EELIQLIND-TPFGLTA 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795203903 481 AVFSQDkdvvqeATKVLRNA----AGNFYIN-----DKSTgsvvgqqPFGGARASGTNdKPGGPHYILRWTSPQ 545
Cdd:cd07113 412 SVWTNN------LSKALRYIprieAGTVWVNmhtflDPAV-------PFGGMKQSGIG-REFGSAFIDDYTELK 471
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
87-527 |
2.41e-58 |
|
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: 201.24 E-value: 2.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 87 HGHKVAKFCYADKSLLNKAIEAALAA--RKEW-DLKPIAdRAQIFLKAADMLSgpHRAEILAKTMVGQ-GKTViqAEIDA 162
Cdd:cd07114 6 TGEPWARVPEASAADVDRAVAAARAAfeGGAWrKLTPTE-RGKLLRRLADLIE--ANAEELAELETRDnGKLI--RETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 163 -AAELIDFFRFNAKYAVELEGQ-QPISVPPSTNSTVYRGLeGFVAAISPFN----FTAiggnLAGAPAL-MGNVVLWKPS 235
Cdd:cd07114 81 qVRYLAEWYRYYAGLADKIEGAvIPVDKGDYLNFTRREPL-GVVAAITPWNspllLLA----KKLAPALaAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 236 DTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfrtFPRLAGEC 315
Cdd:cd07114 156 EHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN------LAPVTLEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 316 GGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAK 395
Cdd:cd07114 230 GGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDP-ETQMGPLATER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 396 SFARIKKWLEHARSSPSlTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVD 471
Cdd:cd07114 309 QLEKVERYVARAREEGA-RVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDE--EEAIALAN 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 795203903 472 StTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSVVgqQPFGGARASG 527
Cdd:cd07114 386 D-SEYGLAAGIWTRDLARAHRVARAIE--AGTVWVNTYRALSPS--SPFGGFKDSG 436
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
76-527 |
2.66e-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: 200.93 E-value: 2.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 76 LDVQyqvSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMVGQ-GKT 154
Cdd:cd07147 1 LEVT---NPYT-GEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLE--ERFEELAETIVLEaGKP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 155 VIQAEIDAAaELIDFFRFNAKYAVELEGQ-QPISVPPSTNStvYRGL-----EGFVAAISPFNFTAiggNLAG---APAL 225
Cdd:cd07147 75 IKDARGEVA-RAIDTFRIAAEEATRIYGEvLPLDISARGEG--RQGLvrrfpIGPVSAITPFNFPL---NLVAhkvAPAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 226 -MGNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldr 304
Cdd:cd07147 149 aAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 305 frtfpRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDf 384
Cdd:cd07147 225 -----KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDD- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 385 GTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVgyfVEPCIVESKDPQEPIMKEEIFGPVLTVYVYpdDKYK 464
Cdd:cd07147 299 ATDVGPMISESEAERVEGWVNEAVDAGA-KLLTGGKRDGAL---LEPTILEDVPPDMEVNCEEVFGPVVTVEPY--DDFD 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795203903 465 ETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSvVGQQPFGGARASG 527
Cdd:cd07147 373 EALAAVND-SKFGLQAGVFTRDLEKALRAWDELE--VGGVVINDVPTFR-VDHMPYGGVKDSG 431
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
83-549 |
1.21e-57 |
|
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: 199.46 E-value: 1.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 83 SPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGKTVIQA--EI 160
Cdd:cd07101 2 APFT-GEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVL-ERRDELLDLIQLETGKARRHAfeEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 161 DAAAELIDFFRFNAKYAVELEGQQPiSVPPSTNSTVYRGLEGFVAAISPFNF---TAIGGNLagaPALM-GNVVLWKPSD 236
Cdd:cd07101 80 LDVAIVARYYARRAERLLKPRRRRG-AIPVLTRTTVNRRPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 237 TAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTssEHLCGINFTGSVPTFKHLWKQVAQNLDRFrtfprlAGECG 316
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRLIGC------SLELG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 317 GKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGdPAEDFGTFFSAVIDAKS 396
Cdd:cd07101 228 GKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLG-AALDYGPDMGSLISQAQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 397 FARIKKWLEHARSSPSlTILAGGKCDDSVG-YFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTS 475
Cdd:cd07101 307 LDRVTAHVDDAVAKGA-TVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADD--DEAIELAND-TD 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795203903 476 YGLTGAVFSQDKDVVQEATKVLRnaAGNFYIND---KSTGSVvgQQPFGGARASGTNDKpGGPHYILRWTSPQVIKE 549
Cdd:cd07101 383 YGLNASVWTRDGARGRRIAARLR--AGTVNVNEgyaAAWASI--DAPMGGMKDSGLGRR-HGAEGLLKYTETQTVAV 454
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
82-527 |
1.30e-57 |
|
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: 199.51 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 82 VSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGphRAEILAKTMVGQ-GKTV-IQAE 159
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEA--RSEELARLLALEtGNALrTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 160 IDAAAeLIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSD 236
Cdd:cd07108 79 PEAAV-LADLFRYFGGLAGELKGE---TLPFGPDVLTYTVREplGVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 237 TAMLASYAIYRVLREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfrtfPRLAG--- 313
Cdd:cd07108 155 DAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA---------DRLIPvsl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 314 ECGGKNFHFVHCSADVDSVVSGTLRSA-FEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDP---AEDFGtffs 389
Cdd:cd07108 225 ELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPldeATDIG---- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 390 AVIDAKSFARIKKWLEHARSSPSLTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDdkYKE 465
Cdd:cd07108 301 AIISEKQFAKVCGYIDLGLSTSGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKD--EDE 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795203903 466 TLQLVDSTTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKstgsvVGQQP---FGGARASG 527
Cdd:cd07108 379 VIAMANDSH-YGLAAYVWTRDLGRALRAAHALE--AGWVQVNQG-----GGQQPgqsYGGFKQSG 435
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
97-527 |
2.12e-57 |
|
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: 199.01 E-value: 2.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 97 ADKSLLNKAIEAALAARKEWDLK-PIADRAQIFLKAADMLSGphRAEILAKTMVGQ-GKTVIQAEIDAAAELIDFFRFNA 174
Cdd:cd07089 16 AGAADVDAAIAAARRAFDTGDWStDAEERARCLRQLHEALEA--RKEELRALLVAEvGAPVMTARAMQVDGPIGHLRYFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 175 KYAVELEGQQPISVPPS----TNSTVYRGLEGFVAAISPFNFtAIGGNLAG-APAL-MGNVVLWKPSDTAMLASYAIYRV 248
Cdd:cd07089 94 DLADSFPWEFDLPVPALrggpGRRVVRREPVGVVAAITPWNF-PFFLNLAKlAPALaAGNTVVLKPAPDTPLSALLLGEI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 249 LREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfrtfprLAGECGGKNFHFVHCSAD 328
Cdd:cd07089 173 IAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKR------VLLELGGKSANIVLDDAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 329 VDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHAR 408
Cdd:cd07089 247 LAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPA-DPGTVMGPLISAAQRDRVEGYIARGR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 409 SSPSlTILAGGKCDDS--VGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTGAVFSQD 486
Cdd:cd07089 326 DEGA-RLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDD--DEAVRIAND-SDYGLSGGVWSAD 401
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 795203903 487 KDVVQEATKVLRnaAGNFYINDKSTGSVVGqqPFGGARASG 527
Cdd:cd07089 402 VDRAYRVARRIR--TGSVGINGGGGYGPDA--PFGGYKQSG 438
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
105-528 |
3.33e-57 |
|
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: 198.37 E-value: 3.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMVGQGKTVIQA---EIDAAAELIDFFrfnAKYAVELE 181
Cdd:cd07107 24 AVAAARAAFPEWRATTPLERARMLRELATRLR--EHAEELALIDALDCGNPVSAmlgDVMVAAALLDYF---AGLVTELK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 182 GQqpiSVPPSTNSTVYRGLE--GFVAAISPFN----FTAigGNLAgAPALMGNVVLWKPSDTAMLASYAIYRVLREAgLP 255
Cdd:cd07107 99 GE---TIPVGGRNLHYTLREpyGVVARIVAFNhplmFAA--AKIA-APLAAGNTVVVKPPEQAPLSALRLAELAREV-LP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 256 PNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfrTFPRLAGECGGKNFHFVHCSADVDSVVSG 335
Cdd:cd07107 172 PGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAE------GIKHVTLELGGKNALIVFPDADPEAAADA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 336 TLRSA-FEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSLT 414
Cdd:cd07107 246 AVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDP-ATTMGPLVSRQQYDRVMHYIDSAKREGARL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 415 ILAGGKCDDSV---GYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvVQ 491
Cdd:cd07107 325 VTGGGRPEGPAlegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDE--AEMVAQANG-VEYGLTAAIWTND---IS 398
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 795203903 492 EATKVLRNA-AGNFYINDKST---GSvvgqqPFGGARASGT 528
Cdd:cd07107 399 QAHRTARRVeAGYVWINGSSRhflGA-----PFGGVKNSGI 434
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
82-527 |
1.06e-56 |
|
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: 196.79 E-value: 1.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 82 VSPfNHGHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSGphRAEILAKTMVGQ-GKTVIQA 158
Cdd:cd07118 2 RSP-AHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRA--RRERLALIETLEsGKPISQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 159 --EIDAAAELidfFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTA--IGGNLAGAPAlMGNVVLWKP 234
Cdd:cd07118 79 rgEIEGAADL---WRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFliLSQKLPFALA-AGCTVVVKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 235 SD-----TAMLASYaiyrvLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfrtfp 309
Cdd:cd07118 155 SEftsgtTLMLAEL-----LIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKK----- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 310 rLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFS 389
Cdd:cd07118 225 -VSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDP-ETKVG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 390 AVIDAKSFARIKKWLEHARSSPSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYpdDKYKETLQL 469
Cdd:cd07118 303 AIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTF--DTVDEAIAL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 795203903 470 VDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSVvgQQPFGGARASG 527
Cdd:cd07118 381 AND-TVYGLSAGVWSKDIDTALTVARRIR--AGTVWVNTFLDGSP--ELPFGGFKQSG 433
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
88-527 |
1.03e-55 |
|
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: 194.38 E-value: 1.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 88 GHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPiADRAQIFLKAADMLSGphRAEILAKTM-VGQGKTVIQAEIDAAA 164
Cdd:cd07109 7 GEVFARIARGGAADVDRAVQAARRAfeSGWLRLSP-AERGRLLLRIARLIRE--HADELARLEsLDTGKPLTQARADVEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 165 eLIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTA-IGGNLAgAPAL-MGNVVLWKPSDTAML 240
Cdd:cd07109 84 -AARYFEYYGGAADKLHGE---TIPLGPGYFVYTVREphGVTGHIIPWNYPLqITGRSV-APALaAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 241 ASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfrtFPRLAGECGGKNF 320
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEN------VVPVTLELGGKSP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 321 HFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDFGtfFSAVIDAKSFARI 400
Cdd:cd07109 233 QIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPD--LGPLISAKQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 401 KKWLEHARSSpSLTILAGG---KCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYG 477
Cdd:cd07109 311 EGFVARARAR-GARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDE--AEAIALANG-TDYG 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 795203903 478 LTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSVVgQQPFGGARASG 527
Cdd:cd07109 387 LVAGVWTRDGDRALRVARRLR--AGQVFVNNYGAGGGI-ELPFGGVKKSG 433
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
104-555 |
3.47e-55 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 194.33 E-value: 3.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 104 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpHRAEILaktmvgqgkTVIQAEI-----DAAAELIDFF---RFNAK 175
Cdd:PRK09407 58 AAFARARAAQRAWAATPVRERAAVLLRFHDLVLE-NREELL---------DLVQLETgkarrHAFEEVLDVAltaRYYAR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 176 YAVELEGQQPIS--VPPSTNSTVYRGLEGFVAAISPFNF---TAIGGNLagaPALM-GNVVLWKP-SDTAMLASYAIyRV 248
Cdd:PRK09407 128 RAPKLLAPRRRAgaLPVLTKTTELRQPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPdSQTPLTALAAV-EL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 249 LREAGLPPNIIQFVPADGPLFGDTVT-SSEHLCginFTGSVPTFKHLWKQVAQNLDRFrtfprlAGECGGKNFHFVHCSA 327
Cdd:PRK09407 204 LYEAGLPRDLWQVVTGPGPVVGTALVdNADYLM---FTGSTATGRVLAEQAGRRLIGF------SLELGGKNPMIVLDDA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 328 DVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGdPAEDFGTFFSAVIDAKSFARIKKWLEHA 407
Cdd:PRK09407 275 DLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLG-AGYDYSADMGSLISEAQLETVSAHVDDA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 408 RSSPSlTILAGGKCDDSVG-YFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQD 486
Cdd:PRK09407 354 VAKGA-TVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADV--DEAVERANDTP-YGLNASVWTGD 429
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795203903 487 KDVVQEATKVLRnaAGNFYINDKST---GSVvgQQPFGGARASGTNDKpGGPHYILRWTSPQVIKETHK-PLG 555
Cdd:PRK09407 430 TARGRAIAARIR--AGTVNVNEGYAaawGSV--DAPMGGMKDSGLGRR-HGAEGLLKYTESQTIATQRVlPLA 497
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
75-527 |
6.84e-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: 192.42 E-value: 6.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 75 TLDVqyqVSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPI--ADRAQIFLKAADMLSGpHRAEILAKTMVGQG 152
Cdd:cd07091 20 TFPT---INPAT-EEVICQVAEADEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIER-DRDELAALESLDNG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 153 KTV-IQAEIDAAaELIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGN 228
Cdd:cd07091 95 KPLeESAKGDVA-LSIKCLRYYAGWADKIQGK---TIPIDGNFLAYTRREpiGVCGQIIPWNFPLLMLAWKLAPALaAGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 229 VVLWKPSDTAMLasYAIY--RVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDRF 305
Cdd:cd07091 171 TVVLKPAEQTPL--SALYlaELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNLKKV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 306 rTFprlagECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfG 385
Cdd:cd07091 249 -TL-----ELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP-D 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 386 TFFSAVIDAKSFARIKKWLEHARSSpSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYvypddKYKE 465
Cdd:cd07091 322 TFQGPQVSKAQFDKILSYIESGKKE-GATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTIL-----KFKT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795203903 466 TLQLVD--STTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINdksTGSVVGQQ-PFGGARASG 527
Cdd:cd07091 396 EDEVIEraNDTEYGLAAGVFTKDINKALRVSRALK--AGTVWVN---TYNVFDAAvPFGGFKQSG 455
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
105-540 |
2.58e-54 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 199.04 E-value: 2.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSGphRAEILAKTMVGQ-GKTVIQAeIDAAAELIDFFRFnakYAVELEGQ 183
Cdd:PRK11809 687 ALESAVNAAPIWFATPPAERAAILERAADLMEA--QMQTLMGLLVREaGKTFSNA-IAEVREAVDFLRY---YAGQVRDD 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 184 qpisvppSTNSTvYRGLeGFVAAISPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAMLASYAIyRVLREAGLPPNIIQ 260
Cdd:PRK11809 761 -------FDNDT-HRPL-GPVVCISPWNFPlAIfTGQVAAALA-AGNSVLAKPAEqTPLIAAQAV-RILLEAGVPAGVVQ 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 261 FVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLD-RFRTFPRLAgECGGKNFHFVHCSADVDSVVSGTLRS 339
Cdd:PRK11809 830 LLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDpQGRPIPLIA-ETGGQNAMIVDSSALTEQVVADVLAS 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 340 AFEYGGQKCSACSRLYVP-----HSLwPQIKGRLLEehgrIKVGDPaEDFGTFFSAVIDAKSFARIKKWLEHARSS--PS 412
Cdd:PRK11809 909 AFDSAGQRCSALRVLCLQddvadRTL-KMLRGAMAE----CRMGNP-DRLSTDIGPVIDAEAKANIERHIQAMRAKgrPV 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 413 LTILAGGKCDDSVGYFVEPCIVESKDPQEpiMKEEIFGPVLTVYVYpddKYKETLQLVDS--TTSYGLTGAVFSQDKDVV 490
Cdd:PRK11809 983 FQAARENSEDWQSGTFVPPTLIELDSFDE--LKREVFGPVLHVVRY---NRNQLDELIEQinASGYGLTLGVHTRIDETI 1057
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 795203903 491 QEATKvlRNAAGNFYINDKSTGSVVGQQPFGGARASGTNDKPGGPHYILR 540
Cdd:PRK11809 1058 AQVTG--SAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYR 1105
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
105-534 |
2.72e-53 |
|
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: 187.09 E-value: 2.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSGphRAEILAKTM---VGQGKTVIQAEIDAAAELIDFfrfNAKYAVELE 181
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELLKA--NKEELARLIsreTGKPLWEAQTEVAAMAGKIDI---SIKAYHERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 182 GQQPISVPPSTNSTVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQ 260
Cdd:cd07095 80 GERATPMAQGRAVLRHRPH-GVMAVFGPFNFPGHLPNGHIVPALLaGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 261 FVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFrtfprLAGECGGKNFHFVHCSADVDSVVSGTLRSA 340
Cdd:cd07095 159 LVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI-----LALEMGGNNPLVVWDVADIDAAAYLIVQSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 341 FEYGGQKCSACSRLYVPHSLWPQ-IKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGG 419
Cdd:cd07095 233 FLTAGQRCTCARRLIVPDGAVGDaFLERLVEAAKRLRIGAPDAE-PPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 420 KCDDSvGYFVEPCIVESKDPQEPiMKEEIFGPVLTVYVYpdDKYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRn 499
Cdd:cd07095 312 RLVAG-TAFLSPGIIDVTDAADV-PDEEIFGPLLQVYRY--DDFDEAIALANA-TRFGLSAGLLSDDEALFERFLARIR- 385
|
410 420 430
....*....|....*....|....*....|....*
gi 795203903 500 aAGNFYINDKSTGSvVGQQPFGGARASGtNDKPGG 534
Cdd:cd07095 386 -AGIVNWNRPTTGA-SSTAPFGGVGLSG-NHRPSA 417
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
103-527 |
4.43e-53 |
|
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: 187.42 E-value: 4.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 103 NKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSGpHRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVEL 180
Cdd:cd07112 27 DRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEA-HRDELALLETLDMGKPISDALAVDVPSAANTFRWYAEAIDKV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 181 EGQQPiSVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAIYRVLREAGLPPNII 259
Cdd:cd07112 106 YGEVA-PTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 260 QFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDRfrtfprLAGECGGKNFHFV-HCSADVDSVVSGTL 337
Cdd:cd07112 185 NVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKR------VWLECGGKSPNIVfADAPDLDAAAEAAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 338 RSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSSpSLTILA 417
Cdd:cd07112 259 AGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPL-DPATRMGALVSEAHFDKVLGYIESGKAE-GARLVA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 418 GGKCD--DSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVdSTTSYGLTGAVFSQDKDVVQEATK 495
Cdd:cd07112 337 GGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSE--EEAVALA-NDSVYGLAASVWTSDLSRAHRVAR 413
|
410 420 430
....*....|....*....|....*....|..
gi 795203903 496 VLRnaAGNFYINDKSTGSVvgQQPFGGARASG 527
Cdd:cd07112 414 RLR--AGTVWVNCFDEGDI--TTPFGGFKQSG 441
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
96-535 |
8.24e-53 |
|
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: 185.96 E-value: 8.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 96 YADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGKTVIQAEIDAAAElIDFFRFNAK 175
Cdd:cd07152 9 VADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLE-EHADEIADWIVRESGSIRPKAGFEVGAA-IGELHEAAG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 176 YAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPS-DTAMLASYAIYRVLREAG 253
Cdd:cd07152 87 LPTQPQGEILPSAPGRLSLARRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDpRTPVSGGVVIARLFEEAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 254 LPPNIIQFVPAdGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfrtfprLAGECGGKNFHFVHCSADVDSVV 333
Cdd:cd07152 166 LPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKK------VSLELGGKNALIVLDDADLDLAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 334 SGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSl 413
Cdd:cd07152 239 SNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATG-QVALGPLINARQLDRVHAIVDDSVAAGA- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 414 TILAGGKCDdsvGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVVQEA 493
Cdd:cd07152 317 RLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSD--EEAVALAND-TEYGLSAGIISRDVGRAMAL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 795203903 494 TKVLRnaAGNFYINDKSTGSVVgQQPFGGARASGTNDKPGGP 535
Cdd:cd07152 391 ADRLR--TGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
95-527 |
1.47e-52 |
|
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: 185.62 E-value: 1.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 95 CYAD--KSLLNKAIEAALAARKE--WDLKPiADRAQIFLKAADMLSgpHRAEILAKTMV-GQGKTVIQA--EIDAAaelI 167
Cdd:cd07120 12 TYADggVAEAEAAIAAARRAFDEtdWAHDP-RLRARVLLELADAFE--ANAERLARLLAlENGKILGEArfEISGA---I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 168 DFFRFNAKYAVELEGQQpISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKP-SDTAMLASyAI 245
Cdd:cd07120 86 SELRYYAGLARTEAGRM-IEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAaGCTVVVKPaGQTAQINA-AI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 246 YRVLREA-GLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFrtfprlAGECGGKNFHFVH 324
Cdd:cd07120 164 IRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRL------GLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 325 CSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVG---DPAEDFGtffsAVIDAKSFARIK 401
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGpglDPASDMG----PLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 402 KWLEHARSSPSLTILAGGKCDD--SVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLT 479
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDE--AEAVALAND-TDYGLA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 795203903 480 GAVFSQDkdvVQEATKVLRN-AAGNFYINDKstGSVVGQQPFGGARASG 527
Cdd:cd07120 391 ASVWTRD---LARAMRVARAiRAGTVWINDW--NKLFAEAEEGGYRQSG 434
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
88-547 |
3.41e-51 |
|
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: 182.04 E-value: 3.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpHRAEILAKTMVGQGKTVIQA--EIDAAAE 165
Cdd:cd07099 6 GEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALAD-HADELAELLHAETGKPRADAglEVLLALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 166 LIDFFrfnAKYAVELEGQQPISVPPSTN---STVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLA 241
Cdd:cd07099 85 AIDWA---ARNAPRVLAPRKVPTGLLMPnkkATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAaGNAVVLKPSEVTPLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 242 SYAIYRVLREAGLPPNIIQFVPADGPlfgdtvtSSEHLCG-----INFTGSVPTFKHLWKQVAQNLdrfrtFPRLAgECG 316
Cdd:cd07099 162 GELLAEAWAAAGPPQGVLQVVTGDGA-------TGAALIDagvdkVAFTGSVATGRKVMAAAAERL-----IPVVL-ELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 317 GKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDFGTfFSAVIDAKS 396
Cdd:cd07099 229 GKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDAD-IGPMTTARQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 397 FARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDSTTsY 476
Cdd:cd07099 308 LDIVRRHVDDAVAKGA-KALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADE--DEAIALANDSR-Y 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 795203903 477 GLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSVVGQQPFGGARASGTNDKpGGPHYILRWTSPQVI 547
Cdd:cd07099 384 GLSASVFSRDLARAEAIARRLE--AGAVSINDVLLTAGIPALPFGGVKDSGGGRR-HGAEGLREFCRPKAI 451
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
103-527 |
2.76e-49 |
|
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: 177.38 E-value: 2.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 103 NKAIEAALAA-RKEWDLKPIADRAQIFLKAADMLSgPHRAEIlAKTM---VGQGKTVIQAEIDAAAELIDFFRFNAKyav 178
Cdd:cd07082 41 LEAAETAYDAgRGWWPTMPLEERIDCLHKFADLLK-ENKEEV-ANLLmweIGKTLKDALKEVDRTIDYIRDTIEELK--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 179 ELEGQ--QPISVPPSTNS--TVYRGLEGFVAAISPFNFTAiggNLAG---APAL-MGNVVLWKPSDTAMLASYAIYRVLR 250
Cdd:cd07082 116 RLDGDslPGDWFPGTKGKiaQVRREPLGVVLAIGPFNYPL---NLTVsklIPALiMGNTVVFKPATQGVLLGIPLAEAFH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 251 EAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfrtfpRLAGECGGKNFHFVHCSADVD 330
Cdd:cd07082 193 DAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMK--------RLVLELGGKDPAIVLPDADLE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 331 SVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSS 410
Cdd:cd07082 265 LAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDN-GVDITPLIDPKSADFVEGLIDDAVAK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 411 PSlTILAGGKCDdsVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVV 490
Cdd:cd07082 344 GA-TVLNGGGRE--GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDI--EEAIELANK-SNYGLQASIFTKDINKA 417
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 795203903 491 QEATKVLRnaAGNFYINDKStgsvvgQQ-----PFGGARASG 527
Cdd:cd07082 418 RKLADALE--VGTVNINSKC------QRgpdhfPFLGRKDSG 451
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
82-527 |
8.62e-49 |
|
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: 176.18 E-value: 8.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAA-RKEWDLK-PIADRAQIFLKAADMLSgpHRAEILAKT-MVGQGKTVIQA 158
Cdd:cd07143 27 YNPST-GKLITKIAEATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLME--RNLDYLASIeALDNGKTFGTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 159 EIDAAAELIDFFRFNAKYAVELEGQQpISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 237
Cdd:cd07143 104 KRVDVQASADTFRYYGGWADKIHGQV-IETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAaGNTIVLKPSEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 238 AMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfrTFPRLAGECGG 317
Cdd:cd07143 183 TPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS-----NLKKVTLELGG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 318 KNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSF 397
Cdd:cd07143 258 KSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAE-DTFQGPQVSQIQY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 398 ARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDSTTsYG 477
Cdd:cd07143 337 ERIMSYIESGKAEGA-TVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTE--EEAIKRANDST-YG 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 795203903 478 LTGAVFSQDkdvVQEATKVlRNA--AGNFYINDKSTgsVVGQQPFGGARASG 527
Cdd:cd07143 413 LAAAVFTNN---INNAIRV-ANAlkAGTVWVNCYNL--LHHQVPFGGYKQSG 458
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
88-528 |
1.19e-48 |
|
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: 174.82 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMVGQ-GKTVIQAEIDAAAEL 166
Cdd:cd07092 7 GEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIE--ENAEELAALESRNtGKPLHLVRDDELPGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 167 IDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAI 245
Cdd:cd07092 85 VDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPLTTLLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 246 YRVLREaGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfrtfprLAGECGGKNFHFVHC 325
Cdd:cd07092 165 AELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKR------VHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 326 SADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLE 405
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDE-DTEMGPLNSAAQRERVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 406 HARSSpsLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTGAVFSQ 485
Cdd:cd07092 317 RAPAH--ARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDE--DEAIELAND-VEYGLASSVWTR 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 795203903 486 DKDVVQEATKVLRnaAGNFYINDKstGSVVGQQPFGGARASGT 528
Cdd:cd07092 392 DVGRAMRLSARLD--FGTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
103-527 |
1.32e-48 |
|
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: 174.30 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLsgPHRAEILAKTM---VGQGKTVIQAEIDAAAELidfFRFNAKYAVE 179
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLL--ESRRDEFIEAMmeeTGATAAWAGFNVDLAAGM---LREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 180 LEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAIYRVLREAGLPPNI 258
Cdd:cd07105 78 IIGGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 259 IQFV---PADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfrtfPRLAgECGGKNFHFVHCSADVDSVVSG 335
Cdd:cd07105 158 LNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLK-----PVLL-ELGGKAPAIVLEDADLDAAANA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 336 TLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEdfgtffSAVIDAKSFARIKKWLEHARSSPSlTI 415
Cdd:cd07105 232 ALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL------GSLVSAAAADRVKELVDDALSKGA-KL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 416 LAGGKCDDSV-GYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvvqeAT 494
Cdd:cd07105 305 VVGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDE--EEAVRIAND-SEYGLSAAVFTRD------LA 375
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 795203903 495 KVLRNA----AGNFYINdkstGSVVG---QQPFGGARASG 527
Cdd:cd07105 376 RALAVAkrieSGAVHIN----GMTVHdepTLPHGGVKSSG 411
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
103-527 |
1.79e-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: 175.00 E-value: 1.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTM---VGQGKTV---IQAE-----IDAAAELIDFFR 171
Cdd:cd07138 39 DRAVAAARRAFPAWSATSVEERAALLERIAEAYE--ARADELAQAItleMGAPITLaraAQVGlgighLRAAADALKDFE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 172 FnakyaVELEGqqpisvppstNSTVYRGLEGFVAAISPFNFTA--IGGNLAgaPALM-GNVVLWKPSDTAMLASYAIYRV 248
Cdd:cd07138 117 F-----EERRG----------NSLVVREPIGVCGLITPWNWPLnqIVLKVA--PALAaGCTVVLKPSEVAPLSAIILAEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 249 LREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTfkhlWKQVAQNLDRfrTFPRLAGECGGKNFHFVHCSAD 328
Cdd:cd07138 180 LDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRA----GKRVAEAAAD--TVKRVALELGGKSANIILDDAD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 329 VDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWL---- 404
Cdd:cd07138 254 LEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDP-ATTLGPLASAAQFDRVQGYIqkgi 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 405 -EHARsspsltILAGG--KCDD-SVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTG 480
Cdd:cd07138 333 eEGAR------LVAGGpgRPEGlERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDE--DEAIAIAND-TPYGLAG 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 795203903 481 AVFSQDKDVVQEATKVLRnaAGNFYINDkstGSVVGQQPFGGARASG 527
Cdd:cd07138 404 YVWSADPERARAVARRLR--AGQVHING---AAFNPGAPFGGYKQSG 445
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
97-527 |
2.39e-48 |
|
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: 174.46 E-value: 2.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 97 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpHRAEILAKTMVGQGKTVIQAEIDAAaELIDFFRFNAKY 176
Cdd:cd07110 16 ATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRE-RREELAELEARDNGKPLDEAAWDVD-DVAGCFEYYADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 177 AVELEGQQPISVP---PSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAIYRVLREA 252
Cdd:cd07110 94 AEQLDAKAERAVPlpsEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSELTSLTELELAEIAAEA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 253 GLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfrtfprLAGECGGKNFHFVHCSADVDSV 332
Cdd:cd07110 174 GLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKP------VSLELGGKSPIIVFDDADLEKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 333 VSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSpS 412
Cdd:cd07110 248 VEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEE-GVRLGPLVSQAQYEKVLSFIARGKEE-G 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 413 LTILAGGKCDDSV--GYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVV 490
Cdd:cd07110 326 ARLLCGGRRPAHLekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATE--DEAIALAND-SEYGLAAAVISRDAERC 402
|
410 420 430
....*....|....*....|....*....|....*..
gi 795203903 491 QEATKVLRnaAGNFYINdkSTGSVVGQQPFGGARASG 527
Cdd:cd07110 403 DRVAEALE--AGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
82-507 |
6.81e-48 |
|
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: 172.82 E-value: 6.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGphRAEILAKTMVGQ-GKTVIQA-- 158
Cdd:cd07102 1 ISPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAA--NTDEIAEELTWQmGRPIAQAgg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 159 EIDAAAELIDFFRFNAKYAVelegqQPISVPPSTNST---VYRGLeGFVAAISPFN---FTAIGgnlAGAPALM-GNVVL 231
Cdd:cd07102 78 EIRGMLERARYMISIAEEAL-----ADIRVPEKDGFEryiRREPL-GVVLIIAPWNypyLTAVN---AVIPALLaGNAVI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 232 WKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnlDRFRTfprL 311
Cdd:cd07102 149 LKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAA---GRFIK---V 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 312 AGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAV 391
Cdd:cd07102 222 GLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDP-STTLGPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 392 IDAKSFARIKKWLEHARSSPSlTILAGGK---CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQ 468
Cdd:cd07102 301 VSARAADFVRAQIADAIAKGA-RALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSD--AEAIA 377
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 795203903 469 LV-DSTtsYGLTGAVFSQDKDVVQE-ATKVlrnAAGNFYIN 507
Cdd:cd07102 378 LMnDSE--YGLTASVWTKDIARAEAlGEQL---ETGTVFMN 413
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
74-527 |
1.07e-47 |
|
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: 173.36 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 74 WTLDVqyqVSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLK-PIADRAQIFLKAADMLSgPHRAEILAKTMVGQG 152
Cdd:cd07144 23 ETIKT---VNPST-GEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVE-KNRDLLAAIEALDSG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 153 KTVIQAEIDAAAELIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTAiggNLAG---APALM- 226
Cdd:cd07144 98 KPYHSNALGDLDEIIAVIRYYAGWADKIQGK---TIPTSPNKLAYTLHEpyGVCGQIIPWNYPL---AMAAwklAPALAa 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 227 GNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfr 306
Cdd:cd07144 172 GNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLK--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 307 tfpRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEE-HGRIKVGDPAEDfG 385
Cdd:cd07144 249 ---AVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHvKQNYKVGSPFDD-D 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 386 TFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGK--CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDdkY 463
Cdd:cd07144 325 TVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKapEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKT--Y 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795203903 464 KETLQLVDSTTsYGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINDKSTGSVvgQQPFGGARASG 527
Cdd:cd07144 403 EEAIKKANDTT-YGLAAAVFTKD---IRRAHRVARElEAGMVWINSSNDSDV--GVPFGGFKMSG 461
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
105-527 |
1.58e-47 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 172.99 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 105 AIEAALAA-----RKEWDLKPIADRAQiFLKA-ADMLSgpHRAEILAKT-MVGQGKTVIQAE--IDAAAELIDFFrfnAK 175
Cdd:PLN02467 50 AVEAARKAfkrnkGKDWARTTGAVRAK-YLRAiAAKIT--ERKSELAKLeTLDCGKPLDEAAwdMDDVAGCFEYY---AD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 176 YAVELEGQQ--PISVPPST-NSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAIYRVLRE 251
Cdd:PLN02467 124 LAEALDAKQkaPVSLPMETfKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAaGCTAVLKPSELASVTCLELADICRE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 252 AGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfrtfPrLAGECGGKNFHFVHCSADVDS 331
Cdd:PLN02467 204 VGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVK-----P-VSLELGGKSPIIVFDDVDLDK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 332 VVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSP 411
Cdd:PLN02467 278 AVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEE-GCRLGPVVSEGQYEKVLKFISTAKSEG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 412 SlTILAGGKCDD--SVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDKDV 489
Cdd:PLN02467 357 A-TILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE--DEAIELANDSH-YGLAGAVISNDLER 432
|
410 420 430
....*....|....*....|....*....|....*...
gi 795203903 490 VQEATKVLRnaAGNFYINdkSTGSVVGQQPFGGARASG 527
Cdd:PLN02467 433 CERVSEAFQ--AGIVWIN--CSQPCFCQAPWGGIKRSG 466
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
88-527 |
4.65e-46 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 168.55 E-value: 4.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMVGQ-GK---TVIQAEIDAA 163
Cdd:PRK13473 27 GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIE--ENADEFARLESLNcGKplhLALNDEIPAI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 164 aelIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLAS 242
Cdd:PRK13473 105 ---VDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAaGNTVVLKPSEITPLTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 243 YAIYRVLREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTfprlagECGGKNFHF 322
Cdd:PRK13473 182 LKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHL------ELGGKAPVI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 323 VHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPaEDFGTFFSAVIDAKSFARIKK 402
Cdd:PRK13473 255 VFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDP-DDEDTELGPLISAAHRDRVAG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 403 WLEHARSSPSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDsTTSYGLTGAV 482
Cdd:PRK13473 334 FVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE--DQAVRWAN-DSDYGLASSV 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 795203903 483 FSQDKDVVQEATKVLRnaAGNFYINDKstGSVVGQQPFGGARASG 527
Cdd:PRK13473 411 WTRDVGRAHRVSARLQ--YGCTWVNTH--FMLVSEMPHGGQKQSG 451
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
75-527 |
9.01e-45 |
|
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: 164.67 E-value: 9.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 75 TLDVqyqVSPFNhGHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSGphRAEILAKTMVGQ- 151
Cdd:cd07139 15 TIDV---VSPAT-EEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEA--RADELARLWTAEn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 152 GKTVIQAEIDAAAELIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVV 230
Cdd:cd07139 89 GMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAaGCTV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 231 LWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADgplfgdtVTSSEHLCG------INFTGSVPTFKHLWKQVAQNLDR 304
Cdd:cd07139 169 VLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPAD-------REVGEYLVRhpgvdkVSFTGSTAAGRRIAAVCGERLAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 305 FRTfprlagECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDf 384
Cdd:cd07139 242 VTL------ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 385 GTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGKCDD-SVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDKy 463
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGlDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED- 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795203903 464 ketlQLV----DSttSYGLTGAVFSQDkdvVQEATKVLRNA-AGNFYINDKSTGSVVgqqPFGGARASG 527
Cdd:cd07139 394 ----DAVrianDS--DYGLSGSVWTAD---VERGLAVARRIrTGTVGVNGFRLDFGA---PFGGFKQSG 450
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
102-527 |
1.47e-44 |
|
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: 163.40 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 102 LNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMVGQ-GKTVIQA--EIDAAAELIDFFrfnAKYAV 178
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLR--ERKDELARLITLEmGKPIAEAraEVEKCAWICRYY---AENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 179 ELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFT-------AiggnlagAPALM-GNVVLWKPSDTAMLASYAIYRVLR 250
Cdd:cd07100 76 AFLADEPIETDAGKAYVRYEPL-GVVLGIMPWNFPfwqvfrfA-------APNLMaGNTVLLKHASNVPGCALAIEELFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 251 EAGLPPNIIQFVPADGPLFgDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTfprlagECGGKNFHFVHCSADVD 330
Cdd:cd07100 148 EAGFPEGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVL------ELGGSDPFIVLDDADLD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 331 SVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFS--AVIDAKSfaRIKKWLEHAR 408
Cdd:cd07100 221 KAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDE-DTDLGplARKDLRD--ELHEQVEEAV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 409 SSpSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKD 488
Cdd:cd07100 298 AA-GATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDE--EEAIALAND-SPFGLGGSVFTTDLE 373
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 795203903 489 vvqEATKVLRN-AAGNFYIND--KSTGSVvgqqPFGGARASG 527
Cdd:cd07100 374 ---RAERVARRlEAGMVFINGmvKSDPRL----PFGGVKRSG 408
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
102-533 |
1.09e-43 |
|
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: 161.37 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 102 LNKAIEAALAARKEwdLKPiADRAQIFLKAADMLSgpHRAEILAKTMVGQ-GKTVIQA--EIDAAaelIDFFRFNAKYAV 178
Cdd:cd07146 23 LREALALAASYRST--LTR-YQRSAILNKAAALLE--ARREEFARLITLEsGLCLKDTryEVGRA---ADVLRFAAAEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 179 ELEGQQpISVPPSTNSTVYRGLE-----GFVAAISPFNFTAiggNLAG---APALM-GNVVLWKPSDTAMLASYAIYRVL 249
Cdd:cd07146 95 RDDGES-FSCDLTANGKARKIFTlreplGVVLAITPFNHPL---NQVAhkiAPAIAaNNRIVLKPSEKTPLSAIYLADLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 250 REAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfrtFPRLAGECGGKNFHFVHCSADV 329
Cdd:cd07146 171 YEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLELGGNDPLIVMDDADL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 330 DSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARS 409
Cdd:cd07146 243 ERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDP-ATDMGTVIDEEAAIQIENRVEEAIA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 410 SPSLTILAGGKcddsVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDV 489
Cdd:cd07146 322 QGARVLLGNQR----QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDL--DEAIAISNS-TAYGLSSGVCTNDLDT 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 795203903 490 VQEATKVLRNAAGNfyINDkSTGSVVGQQPFGGARASGTNDKPG 533
Cdd:cd07146 395 IKRLVERLDVGTVN--VNE-VPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
88-533 |
1.34e-43 |
|
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: 161.89 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 88 GHKVAKFCYADKSLLNKAIEAALAARKE--WDLKPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGKTVIQAEIDAAAE 165
Cdd:cd07142 29 GEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLE-KHADELAALETWDNGKPYEQARYAEVPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 166 LIDFFRFNAKYAVELEGqqpISVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLAS 242
Cdd:cd07142 108 AARLFRYYAGWADKIHG---MTLPADGPHHVYTLHEpiGVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEQTPLSA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 243 YAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDrfrtfpRLAGECGGKNFH 321
Cdd:cd07142 185 LLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLK------PVTLELGGKSPF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 322 FVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPaedfgtFFSAV-----IDAKS 396
Cdd:cd07142 259 IVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDP------FRKGVeqgpqVDKEQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 397 FARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDdkYKETLQLVDStTSY 476
Cdd:cd07142 333 FEKILSYIEHGKEEGA-TLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKT--VDEVIKRANN-SKY 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 795203903 477 GLTGAVFSQDKDVVQEATKVLRnaAGNFYIN--DKSTGSVvgqqPFGGARASGTNDKPG 533
Cdd:cd07142 409 GLAAGVFSKNIDTANTLSRALK--AGTVWVNcyDVFDASI----PFGGYKMSGIGREKG 461
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
103-538 |
2.95e-43 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 161.40 E-value: 2.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGphRAEILAKTMVG-QGKTVIQA--EIDAAAELIDFFrfnAKYAVE 179
Cdd:PLN02278 65 NDAIASAHDAFPSWSKLTASERSKILRRWYDLIIA--NKEDLAQLMTLeQGKPLKEAigEVAYGASFLEYF---AEEAKR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 180 LEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTaiggnLA-----GAPALM-GNVVLWKPSDTAMLASYAIYRVLREAG 253
Cdd:PLN02278 140 VYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFP-----LAmitrkVGPALAaGCTVVVKPSELTPLTALAAAELALQAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 254 LPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfrTFPRLAGECGGKNFHFVHCSADVDSVV 333
Cdd:PLN02278 215 IPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAA------TVKRVSLELGGNAPFIVFDDADLDVAV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 334 SGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSl 413
Cdd:PLN02278 289 KGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEE-GVTQGPLINEAAVQKVESHVQDAVSKGA- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 414 TILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDKDVVQEA 493
Cdd:PLN02278 367 KVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE--EEAIAIANDTE-AGLAAYIFTRDLQRAWRV 443
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 795203903 494 TKVLRNaaGNFYINDKSTGSVVGqqPFGGARASGTNdKPGGPHYI 538
Cdd:PLN02278 444 SEALEY--GIVGVNEGLISTEVA--PFGGVKQSGLG-REGSKYGI 483
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
82-528 |
5.85e-43 |
|
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: 160.21 E-value: 5.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARK---EWDLKPIADRAQIFLKAADMLSGpHRAEILAKTMVGQGKTVIQA 158
Cdd:cd07141 27 INPAT-GEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIER-DRAYLASLETLDNGKPFSKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 159 EIDAAAELIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPS 235
Cdd:cd07141 105 YLVDLPGAIKVLRYYAGWADKIHGK---TIPMDGDFFTYTRHEpvGVCGQIIPWNFPLLMAAWKLAPALaCGNTVVLKPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 236 DTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTfKHLWKQVA--QNLDrfrtfpRLAG 313
Cdd:cd07141 182 EQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV-GKLIQQAAgkSNLK------RVTL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 314 ECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVID 393
Cdd:cd07141 255 ELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDP-KTEQGPQID 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 394 AKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYvypddKYKETLQLVD-- 471
Cdd:cd07141 334 EEQFKKILELIESGKKEGA-KLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIF-----KFKTIDEVIEra 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 795203903 472 STTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSVvgQQPFGGARASGT 528
Cdd:cd07141 408 NNTTYGLAAAVFTKDIDKAITFSNALR--AGTVWVNCYNVVSP--QAPFGGYKMSGN 460
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
97-527 |
1.45e-42 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 159.28 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 97 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMV-GQGKTvIQ----AEIDAAAELIDFFr 171
Cdd:PRK13252 41 ATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILR--ERNDELAALETlDTGKP-IQetsvVDIVTGADVLEYY- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 172 fnAKYAVELEGQQpisVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAIYRV 248
Cdd:PRK13252 117 --AGLAPALEGEQ---IPLRGGSFVYTRREplGVCAGIGAWNYPIQIACWKSAPALaAGNAMIFKPSEVTPLTALKLAEI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 249 LREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfrtfprLAGECGGKNFHFVHCSAD 328
Cdd:PRK13252 192 YTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKE------VTMELGGKSPLIVFDDAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 329 VDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPaEDFGTFFSAVIDAKSFARIKKWLEHAR 408
Cdd:PRK13252 265 LDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDP-MDPATNFGPLVSFAHRDKVLGYIEKGK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 409 SSPSlTILAGGKC----DDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDSTTsYGLTGAVFS 484
Cdd:PRK13252 344 AEGA-RLLCGGERltegGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDE--DEVIARANDTE-YGLAAGVFT 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 795203903 485 QDkdvVQEATKVL-RNAAGNFYINdkSTGSVVGQQPFGGARASG 527
Cdd:PRK13252 420 AD---LSRAHRVIhQLEAGICWIN--TWGESPAEMPVGGYKQSG 458
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
140-507 |
1.61e-42 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 157.21 E-value: 1.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 140 RAEILAKTMVG-QGKTVIQAEIDAAAElIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFT--AIG 216
Cdd:PRK10090 11 RASEISALIVEeGGKIQQLAEVEVAFT-ADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPffLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 217 GNLAgaPALM-GNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLW 295
Cdd:PRK10090 90 RKMA--PALLtGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 296 KQVAQNLdrfrtfPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRI 375
Cdd:PRK10090 168 AAAAKNI------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 376 KVGDPAEDFGTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTV 455
Cdd:PRK10090 242 QFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGA-RVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 795203903 456 YVYpdDKYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIN 507
Cdd:PRK10090 321 VAF--DTLEEAIAMAND-SDYGLTSSIYTQNLNVAMKAIKGLK--FGETYIN 367
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
84-527 |
1.87e-42 |
|
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: 158.39 E-value: 1.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 84 PFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAK--TMvGQGKTVIQ---A 158
Cdd:cd07117 23 PAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIID--ENKELLAMveTL-DNGKPIREtraV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 159 EIDAAAeliDFFRFNAKyAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 237
Cdd:cd07117 99 DIPLAA---DHFRYFAG-VIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAaGNTVVIKPSST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 238 AMLASYAIYRVLREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfrtFPRLAgECGG 317
Cdd:cd07117 175 TSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL-----IPATL-ELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 318 KNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSF 397
Cdd:cd07117 248 KSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDP-DTQMGAQVNKDQL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 398 ARIKKWLEHARSSPSlTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDSt 473
Cdd:cd07117 327 DKILSYVDIAKEEGA-KILTGGHrlteNGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTE--DEVIDMAND- 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 795203903 474 TSYGLTGAVFSQDkdvVQEATKVLRNA-AGNFYINdkSTGSVVGQQPFGGARASG 527
Cdd:cd07117 403 SEYGLGGGVFTKD---INRALRVARAVeTGRVWVN--TYNQIPAGAPFGGYKKSG 452
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
82-486 |
2.66e-42 |
|
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: 158.14 E-value: 2.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPiadraqiflkaadmlsGPHRAEIL---------AKTMVGQ- 151
Cdd:cd07130 17 ISPAN-GEPIARVRQATPEDYESTIKAAQEAFKEWRDVP----------------APKRGEIVrqigdalrkKKEALGKl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 152 -----GKTVIQA--EIDaaaELIDFfrfnAKYAVELEGQQPISVPPSTNSTvYRGLE-----GFVAAISPFNF-TAIGG- 217
Cdd:cd07130 80 vslemGKILPEGlgEVQ---EMIDI----CDFAVGLSRQLYGLTIPSERPG-HRMMEqwnplGVVGVITAFNFpVAVWGw 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 218 NLAGApALMGNVVLWKPSDTAMLASYAIY----RVLREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVptfkH 293
Cdd:cd07130 152 NAAIA-LVCGNVVVWKPSPTTPLTAIAVTkivaRVLEKNGLPGAIASLVCGGADV-GEALVKDPRVPLVSFTGST----A 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 294 LWKQVAQNLDRfRtFPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHG 373
Cdd:cd07130 226 VGRQVGQAVAA-R-FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 374 RIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKdPQEPIMKEEIFGPVL 453
Cdd:cd07130 304 QVRIGDPLDD-GTLVGPLHTKAAVDNYLAAIEEAKSQGG-TVLFGGKVIDGPGNYVEPTIVEGL-SDAPIVKEETFAPIL 380
|
410 420 430
....*....|....*....|....*....|...
gi 795203903 454 tvYVYPDDKYKETLQLVDStTSYGLTGAVFSQD 486
Cdd:cd07130 381 --YVLKFDTLEEAIAWNNE-VPQGLSSSIFTTD 410
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
88-536 |
6.59e-42 |
|
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: 157.17 E-value: 6.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPHRAEILAKTMVGqGKTVIQ---AEIDAAA 164
Cdd:cd07111 47 GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDN-GKPIREsrdCDIPLVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 165 ELidfFRFNAKYA----VELEGQQPIsvppstnstvyrgleGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAM 239
Cdd:cd07111 126 RH---FYHHAGWAqlldTELAGWKPV---------------GVVGQIVPWNFPLLMLAWKICPALaMGNTVVLKPAEYTP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 240 LASYAIYRVLREAGLPPNIIQFVPADGPlFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfrTFPRLAGECGGKN 319
Cdd:cd07111 188 LTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAG------TGKKLSLELGGKS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 320 FHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDP---AEDFGtffsAVIDAKS 396
Cdd:cd07111 261 PFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPldkAIDMG----AIVDPAQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 397 FARIKKWLEHARSSPSLTILAGGKCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLTvyVYPDDKYKETLQLVDStTSY 476
Cdd:cd07111 337 LKRIRELVEEGRAEGADVFQPGADLPSK-GPFYPPTLFTNVPPASRIAQEEIFGPVLV--VLTFRTAKEAVALANN-TPY 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 477 GLTGAVFSQDKDVVQEATKVLRnaAGNFYINdkSTGSVVGQQPFGGARASGTNdKPGGPH 536
Cdd:cd07111 413 GLAASVWSENLSLALEVALSLK--AGVVWIN--GHNLFDAAAGFGGYRESGFG-REGGKE 467
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
82-527 |
1.09e-41 |
|
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: 156.35 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAK--TMvGQGKTV---I 156
Cdd:cd07559 21 YNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIE--ENLELLAVaeTL-DNGKPIretL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 157 QAEIDAAaelIDFFRFNAKYAVELEGQqpIS-VPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKP 234
Cdd:cd07559 97 AADIPLA---IDHFRYFAGVIRAQEGS--LSeIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAaGNTVVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 235 SDTAMLASYAIYRVLREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfrtFPrLAGE 314
Cdd:cd07559 172 ASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL-----IP-VTLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 315 CGGK--NFHFvhcsADV--------DSVVSGTLRSAFEYGgQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDf 384
Cdd:cd07559 245 LGGKspNIFF----DDAmdadddfdDKAEEGQLGFAFNQG-EVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 385 GTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPD 460
Cdd:cd07559 319 ETMMGAQVSKDQLEKILSYVDIGKEEGA-EVLTGGErltlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795203903 461 DkyKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINdkSTGSVVGQQPFGGARASG 527
Cdd:cd07559 398 E--EEAIAIAND-TEYGLGGGVWTRD---INRALRVARGiQTGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
75-526 |
5.03e-40 |
|
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: 151.90 E-value: 5.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 75 TLDVqyqVSPfNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTMV-GQGK 153
Cdd:cd07085 17 WLDV---YNP-ATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLE--ENLDELARLITlEHGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 154 TVIQA--EIDAAAELIDFfrfNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIggnlagAPALM----- 226
Cdd:cd07085 91 TLADArgDVLRGLEVVEF---ACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAM------IPLWMfpmai 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 227 --GNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGplfgDTVtssEHLC------GINFTGSVPTFKHLWKQV 298
Cdd:cd07085 162 acGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGK----EAV---NALLdhpdikAVSFVGSTPVGEYIYERA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 299 AQNLDRFRTFprlageCGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVG 378
Cdd:cd07085 235 AANGKRVQAL------GGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 379 dPAEDFGTFFSAVIDAKSFARIKKWLEHArsspsltILAGGKC-----DDSV-----GYFVEPCIVESKDPQEPIMKEEI 448
Cdd:cd07085 309 -AGDDPGADMGPVISPAAKERIEGLIESG-------VEEGAKLvldgrGVKVpgyenGNFVGPTILDNVTPDMKIYKEEI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 449 FGPVLTVyVYPDDkYKETLQLVDStTSYGLTGAVFSQDKDVvqeATKVLRNA-AGNFYINdkstgsV-----VGQQPFGG 522
Cdd:cd07085 381 FGPVLSI-VRVDT-LDEAIAIINA-NPYGNGAAIFTRSGAA---ARKFQREVdAGMVGIN------VpipvpLAFFSFGG 448
|
....
gi 795203903 523 ARAS 526
Cdd:cd07085 449 WKGS 452
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
104-535 |
9.92e-40 |
|
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: 150.91 E-value: 9.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 104 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpHRAEILAKTMVGQGKTVIQA---EIDAAAELIDFFRFNAKYAVel 180
Cdd:cd07098 22 EAIAAARAAQREWAKTSFAERRKVLRSLLKYILE-NQEEICRVACRDTGKTMVDAslgEILVTCEKIRWTLKHGEKAL-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 181 egqQPISVPPSTNsTVYRGLE------GFVAAISPFNF---TAIGGNLAgapALM-GNVVLWKPSDTAMLASYAIYRVLR 250
Cdd:cd07098 99 ---RPESRPGGLL-MFYKRARveyeplGVVGAIVSWNYpfhNLLGPIIA---ALFaGNAIVVKVSEQVAWSSGFFLSIIR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 251 EA----GLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfrtfPRLAgECGGKNFHFVHCS 326
Cdd:cd07098 172 EClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLT-----PVVL-ELGGKDPAIVLDD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 327 ADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAE---DFGtffsAVIDAKSFARIKKW 403
Cdd:cd07098 245 ADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDgdvDVG----AMISPARFDRLEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 404 LEHARSSPSlTILAGGK----CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLT 479
Cdd:cd07098 321 VADAVEKGA-RLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDD--EEAVEIANS-TEYGLG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 795203903 480 GAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSVVGQQPFGGARASGTnDKPGGP 535
Cdd:cd07098 397 ASVFGKDIKRARRIASQLE--TGMVAINDFGVNYYVQQLPFGGVKGSGF-GRFAGE 449
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
97-532 |
7.57e-38 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 145.87 E-value: 7.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 97 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAkTMVGQ--GKTVIQAEIDAAAELidffrfnA 174
Cdd:PRK09457 34 ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLE--ENKEELA-EVIARetGKPLWEAATEVTAMI-------N 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 175 KYAV------ELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAIYR 247
Cdd:PRK09457 104 KIAIsiqayhERTGEKRSEMADGAAVLRHRPH-GVVAVFGPYNFPGHLPNGHIVPALLaGNTVVFKPSELTPWVAELTVK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 248 VLREAGLPPNIIQFVPAdGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFrtfprLAGECGGKNFHFVHCSA 327
Cdd:PRK09457 183 LWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKI-----LALEMGGNNPLVIDEVA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 328 DVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQ-IKGRLLEEHGRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEH 406
Cdd:PRK09457 257 DIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWDAEPQPFMGAVISEQAAQGLVAAQAQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 407 ARSSPSLTILAGGKCDDSVGyFVEPCIVESKDPQEPImKEEIFGPVLTVYVYPDdkYKETLQLVDStTSYGLTGAVFSQD 486
Cdd:PRK09457 337 LLALGGKSLLEMTQLQAGTG-LLTPGIIDVTGVAELP-DEEYFGPLLQVVRYDD--FDEAIRLANN-TRFGLSAGLLSDD 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 795203903 487 KDVVQEATKVLRnaAGNFYINDKSTGSvVGQQPFGGARASGtNDKP 532
Cdd:PRK09457 412 REDYDQFLLEIR--AGIVNWNKPLTGA-SSAAPFGGVGASG-NHRP 453
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
88-533 |
5.81e-37 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 144.18 E-value: 5.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 88 GHKVAKFCYADKSLLNKAIEAALAARKE--WDLKPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGKTVIQAeidAAAE 165
Cdd:PLN02466 83 GEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLE-KHNDELAALETWDNGKPYEQS---AKAE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 166 L---IDFFRFNAKYAVELEGqqpISVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAM 239
Cdd:PLN02466 159 LpmfARLFRYYAGWADKIHG---LTVPADGPHHVQTLHEpiGVAGQIIPWNFPLLMFAWKVGPALAcGNTIVLKTAEQTP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 240 LASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTFprlagECGGKN 319
Cdd:PLN02466 236 LSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVTL-----ELGGKS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 320 FHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQI----KGRLLeehgRIKVGDPaedfgtFFSAV---- 391
Cdd:PLN02466 311 PFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFvekaKARAL----KRVVGDP------FKKGVeqgp 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 392 -IDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYvypddKYKETLQLV 470
Cdd:PLN02466 381 qIDSEQFEKILRYIKSGVESGA-TLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSIL-----KFKDLDEVI 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795203903 471 D--STTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIN--DKSTGSVvgqqPFGGARASGTNDKPG 533
Cdd:PLN02466 455 RraNNTRYGLAAGVFTQNLDTANTLSRALR--VGTVWVNcfDVFDAAI----PFGGYKMSGIGREKG 515
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
88-527 |
1.58e-36 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 142.27 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 88 GHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGKTVI---QAEIDA 162
Cdd:PLN02766 46 GEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIE-EHIEELAALDTIDAGKLFAlgkAVDIPA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 163 AAELidfFRFNAKYAVELEGQQpISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLA 241
Cdd:PLN02766 125 AAGL---LRYYAGAADKIHGET-LKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQTPLS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 242 SYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDRfrtfprLAGECGGKNF 320
Cdd:PLN02766 201 ALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNLKQ------VSLELGGKSP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 321 HFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAeDFGTFFSAVIDAKSFARI 400
Cdd:PLN02766 275 LLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF-DPRARQGPQVDKQQFEKI 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 401 KKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYvypddKYK---ETLQLVDStTSYG 477
Cdd:PLN02766 354 LSYIEHGKREGA-TLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLM-----KFKtveEAIKKANN-TKYG 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 795203903 478 LTGAVFSQDKDVVQEATKVLRnaAGNFYIN-----DKSTgsvvgqqPFGGARASG 527
Cdd:PLN02766 427 LAAGIVTKDLDVANTVSRSIR--AGTIWVNcyfafDPDC-------PFGGYKMSG 472
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
88-527 |
8.40e-36 |
|
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: 139.94 E-value: 8.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 88 GHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGKTVIQAEIDAAAE 165
Cdd:cd07140 31 GSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLME-EHQEELATIESLDSGAVYTLALKTHVGM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 166 LIDFFRFNAKYAVELEGQQ-PIS-VPPSTNSTVYRGLE-GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLA 241
Cdd:cd07140 110 SIQTFRYFAGWCDKIQGKTiPINqARPNRNLTLTKREPiGVCGIVIPWNYPLMMLAWKMAACLAaGNTVVLKPAQVTPLT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 242 SYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVA-QNLDRfrtfprLAGECGGKNF 320
Cdd:cd07140 190 ALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAvSNLKK------VSLELGGKSP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 321 HFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDP---AEDFGTffsavidAKSF 397
Cdd:cd07140 264 LIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPldrSTDHGP-------QNHK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 398 ARIKKWLEHARSS--PSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDKYKETLQLVDsTTS 475
Cdd:cd07140 337 AHLDKLVEYCERGvkEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDVDGVLQRAN-DTE 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 795203903 476 YGLTGAVFSQDkdvvqeATKVLRNA----AGNFYINDKSTGSVVGqqPFGGARASG 527
Cdd:cd07140 416 YGLASGVFTKD------INKALYVSdkleAGTVFVNTYNKTDVAA--PFGGFKQSG 463
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
104-527 |
1.62e-35 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 139.27 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 104 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpHRAEILAKTM-VGQGKTVIQA--EIDAAAELIDFFRFNAK--YAV 178
Cdd:PRK11241 52 AAIDAANRALPAWRALTAKERANILRRWFNLMM--EHQDDLARLMtLEQGKPLAEAkgEISYAASFIEWFAEEGKriYGD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 179 ELEGQQPisvppSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAIYRVLREAGLPPN 257
Cdd:PRK11241 130 TIPGHQA-----DKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIRAGIPAG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 258 IIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfrtfprLAGECGGKNFHFVHCSADVDSVVSGTL 337
Cdd:PRK11241 205 VFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK------VSLELGGNAPFIVFDDADLDKAVEGAL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 338 RSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPSlTILA 417
Cdd:PRK11241 279 ASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK-GVTIGPLIDEKAVAKVEEHIADALEKGA-RVVC 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 418 GGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvvqeATKVL 497
Cdd:PRK11241 357 GGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE--ADVIAQAND-TEFGLAAYFYARD------LSRVF 427
|
410 420 430
....*....|....*....|....*....|..
gi 795203903 498 RNA-AGNFYINDKSTGSVVGQ-QPFGGARASG 527
Cdd:PRK11241 428 RVGeALEYGIVGINTGIISNEvAPFGGIKASG 459
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
82-529 |
5.02e-35 |
|
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: 137.16 E-value: 5.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 82 VSPFNHGHkVAKFCYADKSLLNKAIEAALAA---RKEWdlKPIADRAQIFLKAADMLSGphRAEILAKTMVGQG-KTVIQ 157
Cdd:cd07148 4 VNPFDLKP-IGEVPTVDWAAIDKALDTAHALfldRNNW--LPAHERIAILERLADLMEE--RADELALLIAREGgKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 158 A--EIDAAaelIDFFRFNAKYAVELEGQQ-PISV-PPSTNSTVYRGLE--GFVAAISPFNFTAiggNLA---GAPAL-MG 227
Cdd:cd07148 79 AkvEVTRA---IDGVELAADELGQLGGREiPMGLtPASAGRIAFTTREpiGVVVAISAFNHPL---NLIvhqVAPAIaAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 228 NVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEhLCGINFTGSVPTFKHLWKQVAQNldrfrt 307
Cdd:cd07148 153 CPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPR-VAFFSFIGSARVGWMLRSKLAPG------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 308 fPRLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAeDFGTF 387
Cdd:cd07148 226 -TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPT-DPDTE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 388 FSAVIDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYfvEPCIVESKDPQEPIMKEEIFGPVLTVYVYpdDKYKETL 467
Cdd:cd07148 304 VGPLIRPREVDRVEEWVNEAVAAGA-RLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSY--DDLDEAI 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795203903 468 QLVDStTSYGLTGAVFSQDKDVVQEATKVLrnAAGNFYINDKsTGSVVGQQPFGGARASGTN 529
Cdd:cd07148 379 AQANS-LPVAFQAAVFTKDLDVALKAVRRL--DATAVMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
102-547 |
1.15e-32 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 131.17 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 102 LNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSGPHRAEILAKTMvGQGKTV---IQAEIDAAAELIdffRFNAKY 176
Cdd:PRK09847 59 IDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETL-DTGKPIrhsLRDDIPGAARAI---RWYAEA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 177 AVELEGQqpisVPPSTN---STVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAIYRVLREA 252
Cdd:PRK09847 135 IDKVYGE----VATTSShelAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLAKEA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 253 GLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfrTFPRLAGECGGK--NFHFVHCsADVD 330
Cdd:PRK09847 211 GLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS-----NMKRVWLEAGGKsaNIVFADC-PDLQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 331 SVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAeDFGTFFSAVIDAKSFARIKKWLEHARSS 410
Cdd:PRK09847 285 QAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL-DPATTMGTLIDCAHADSVHSFIREGESK 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 411 PSLtiLAGGKCDDSVGYfVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVV 490
Cdd:PRK09847 364 GQL--LLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSE--EQALQLAND-SQYGLGAAVWTRDLSRA 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 795203903 491 QEATKVLRnaAGNFYINDKSTGSVVgqQPFGGARASGtNDKPGGPHYILRWTSPQVI 547
Cdd:PRK09847 438 HRMSRRLK--AGSVFVNNYNDGDMT--VPFGGYKQSG-NGRDKSLHALEKFTELKTI 489
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
88-527 |
7.26e-31 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 125.24 E-value: 7.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGphRAEILAKTMVGQ-GKTVIQAEIDAAaEL 166
Cdd:PRK09406 11 GETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEA--EADQVAALMTLEmGKTLASAKAEAL-KC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 167 IDFFRFNAKYAVELEGQQPISVPPSTNS---TVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWK-PSDTAMLA 241
Cdd:PRK09406 88 AKGFRYYAEHAEALLADEPADAAAVGASrayVRYQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGNVGLLKhASNVPQTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 242 SYaIYRVLREAGLPPNIIQ--FVPADGPlfgDTVTSSEHLCGINFTGSVPTfkhlWKQVAQnldrfrtfprLAG------ 313
Cdd:PRK09406 167 LY-LADLFRRAGFPDGCFQtlLVGSGAV---EAILRDPRVAAATLTGSEPA----GRAVAA----------IAGdeikkt 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 314 --ECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAV 391
Cdd:PRK09406 229 vlELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDP-DTDVGPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 392 IDAKSFARIKKWLEHARSSPSlTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDdkYKETLQLVD 471
Cdd:PRK09406 308 ATEQGRDEVEKQVDDAVAAGA-TILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVAD--IDEAIEIAN 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 795203903 472 STTsYGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINDKSTGSvvGQQPFGGARASG 527
Cdd:PRK09406 385 ATT-FGLGSNAWTRD---EAEQERFIDDlEAGQVFINGMTVSY--PELPFGGVKRSG 435
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
104-533 |
9.69e-31 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 125.72 E-value: 9.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 104 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSG--PHRAEILAKTMvgqGKTVIQAeIDAAAELIDFfrfnAKYAVELE 181
Cdd:PLN02315 60 EGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAklDYLGRLVSLEM---GKILAEG-IGEVQEIIDM----CDFAVGLS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 182 GQQPISVPPSTNST-----VYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAIYR----VLRE 251
Cdd:PLN02315 132 RQLNGSIIPSERPNhmmmeVWNPL-GIVGVITAFNFpCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKlvaeVLEK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 252 AGLPPNIIQFVpADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfrtFPRLAGECGGKNFHFVHCSADVDS 331
Cdd:PLN02315 211 NNLPGAIFTSF-CGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR------FGKCLLELSGNNAIIVMDDADIQL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 332 VVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSP 411
Cdd:PLN02315 284 AVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK-GTLLGPLHTPESKKNFEKGIEIIKSQG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 412 SlTILAGGKCDDSVGYFVEPCIVESKdPQEPIMKEEIFGPVLtvYVYPDDKYKETLQLVDSTTSyGLTGAVFSQDKDVVQ 491
Cdd:PLN02315 363 G-KILTGGSAIESEGNFVQPTIVEIS-PDADVVKEELFGPVL--YVMKFKTLEEAIEINNSVPQ-GLSSSIFTRNPETIF 437
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 795203903 492 EATKVLRNAAGNFYINDKSTGSVVGQQpFGGARASGTNDKPG 533
Cdd:PLN02315 438 KWIGPLGSDCGIVNVNIPTNGAEIGGA-FGGEKATGGGREAG 478
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
102-547 |
3.60e-30 |
|
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: 123.12 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 102 LNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGKTVIQAEiDAAAeliDFFRFNAKYAVELE 181
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLA-AKSYDIAAGAVLVTGKGWMFAE-NICG---DQVQLRARAFVIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 182 GQQP------ISVPPSTNSTVYRGLEGFVAAISPFNF--TAIGGNLAGAPAlMGNVVLWKPSDTAMLASYAIYRVLREAG 253
Cdd:cd07084 76 YRIPhepgnhLGQGLKQQSHGYRWPYGPVLVIGAFNFplWIPLLQLAGALA-MGNPVIVKPHTAVSIVMQIMVRLLHYAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 254 -LPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVptfkhlwkQVAQNLDRFRTFPRLAGECGGKNFHFVHCSAD-VDS 331
Cdd:cd07084 155 lLPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSS--------RVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 332 VVSGTLRSAFEYGGQKCSACSRLYVPH--SLWPQIKgRLLEEHGRIKVGDpaedfgTFFSAVIDAKSFARIkkwlEHARS 409
Cdd:cd07084 226 VAWQCVQDMTACSGQKCTAQSMLFVPEnwSKTPLVE-KLKALLARRKLED------LLLGPVQTFTTLAMI----AHMEN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 410 SPSLTILAGGK--CDDSVGYFVEPCI-------VESKDPQEPIMKEEIFGPVLTVYVYPDDKYKETLQLVDSTTSYgLTG 480
Cdd:cd07084 295 LLGSVLLFSGKelKNHSIPSIYGACVasalfvpIDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGS-LTA 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795203903 481 AVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSVVGQQPFGGARASGTNDKPGGPHYILRWTSPQVI 547
Cdd:cd07084 374 AIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
94-527 |
1.04e-26 |
|
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: 113.32 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 94 FCYADKSL---LNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPHRAEILAKTmVGQGKTV---IQAEIDAAaelI 167
Cdd:cd07116 29 FCEVPRSTaedIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET-WDNGKPVretLAADIPLA---I 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 168 DFFRFNAKYAVELEGqqpiSVPPSTNSTV-YRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASY 243
Cdd:cd07116 105 DHFRYFAGCIRAQEG----SISEIDENTVaYHFHEplGVVGQIIPWNFPLLMATWKLAPALAaGNCVVLKPAEQTPASIL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 244 AIYRVLREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfrtFPrLAGECGGK--NFH 321
Cdd:cd07116 181 VLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI-----IP-VTLELGGKspNIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 322 FvhcsADV--------DSVVSGTLRSAFEYGgQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAeDFGTFFSAVID 393
Cdd:cd07116 254 F----ADVmdaddaffDKALEGFVMFALNQG-EVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL-DTETMIGAQAS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 394 AKSFARIKKWLEHARSSPSlTILAGGK----CDDSVGYFVEPCIVEsKDPQEPIMKEEIFGPVLTVYVYPDdkYKETLQL 469
Cdd:cd07116 328 LEQLEKILSYIDIGKEEGA-EVLTGGErnelGGLLGGGYYVPTTFK-GGNKMRIFQEEIFGPVLAVTTFKD--EEEALEI 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 795203903 470 VDSTTsYGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINdkSTGSVVGQQPFGGARASG 527
Cdd:cd07116 404 ANDTL-YGLGAGVWTRD---GNTAYRMGRGiQAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
119-527 |
1.48e-26 |
|
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: 112.23 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 119 KPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGK---TVIQAEIDAAAELIDFFRFN-AKYAVELEGQQPISVPPSTNS 194
Cdd:cd07087 17 RSLEWRKAQLKALKRMLT-ENEEEIAAALYADLGKppaEAYLTEIAVVLGEIDHALKHlKKWMKPRRVSVPLLLQPAKAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 195 TVYRGLeGFVAAISPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAMLASYAIYRVLREAgLPPNIIQFVPADGPlfgd 271
Cdd:cd07087 96 VIPEPL-GVVLIIGPWNYplqLALA-PLIGAIA-AGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 272 tVTS---SEHLCGINFTGSVPTFKHLWKQVAQNLdrfrTFPRLagECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKC 348
Cdd:cd07087 168 -VATallAEPFDHIFFTGSPAVGKIVMEAAAKHL----TPVTL--ELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 349 SACSRLYVPHSLWPQ----IKGRLLEEHGRikvgDPAE--DFGtffsAVIDAKSFARIKKWLEHArsspslTILAGGKCD 422
Cdd:cd07087 241 IAPDYVLVHESIKDElieeLKKAIKEFYGE----DPKEspDYG----RIINERHFDRLASLLDDG------KVVIGGQVD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 423 DSvGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDdkYKETLQLVDStTSYGLTGAVFSQDKDVVQeatKVLRN-AA 501
Cdd:cd07087 307 KE-ERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDD--LDEAIEFINS-RPKPLALYLFSEDKAVQE---RVLAEtSS 379
|
410 420
....*....|....*....|....*.
gi 795203903 502 GNFYINDKSTGSVVGQQPFGGARASG 527
Cdd:cd07087 380 GGVCVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
184-527 |
9.60e-25 |
|
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: 106.93 E-value: 9.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 184 QPISVPPS-----TNSTVYRGLEGFVAAISPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAMLASYAIYRVLREAglp 255
Cdd:cd07134 79 KPKRVRTPlllfgTKSKIRYEPKGVCLIISPWNYpfnLAFG-PLVSAIA-AGNTAILKPSELTPHTSAVIAKIIREA--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 256 pniiqFVPADGPLF-GDTVTSSE-------HlcgINFTGSVPTFKHLWKQVAQNLdrfrTFPRLagECGGKNFHFVHCSA 327
Cdd:cd07134 154 -----FDEDEVAVFeGDAEVAQAllelpfdH---IFFTGSPAVGKIVMAAAAKHL----ASVTL--ELGGKSPTIVDETA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 328 DVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEHA 407
Cdd:cd07134 220 DLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 408 RSSPSlTILAGGKCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPD-DkyketlQLVDSTTSYG--LTGAVFS 484
Cdd:cd07134 300 VAKGA-KVEFGGQFDAA-QRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDlD------EVIEYINAKPkpLALYVFS 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 795203903 485 QDKDVVQeatKVLRN-AAGNFYINDKSTGSVVGQQPFGGARASG 527
Cdd:cd07134 372 KDKANVN---KVLARtSSGGVVVNDVVLHFLNPNLPFGGVNNSG 412
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
82-527 |
8.72e-24 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 104.56 E-value: 8.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGphRAEILAKTMVGQ-GKTVIQA-- 158
Cdd:PRK13968 12 VNPAT-GEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRA--RSEEMAQMITREmGKPINQAra 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 159 EIDAAAELIDFFrfnAKYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFtAIGGNLAGA-PALM-GNVVLWKPSD 236
Cdd:PRK13968 89 EVAKSANLCDWY---AEHGPAMLKAEPTLVENQQAVIEYRPL-GTILAIMPWNF-PLWQVMRGAvPILLaGNGYLLKHAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 237 TAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEhLCGINFTGSVPTFKHLWKQVAQNLDRfrtfprLAGECG 316
Cdd:PRK13968 164 NVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIGAQAGAALKK------CVLELG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 317 GKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDFGtffsaviDAKS 396
Cdd:PRK13968 237 GSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEEN-------ALGP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 397 FARIKKWLE-HARSSPSL----TILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDDKYkeTLQLVD 471
Cdd:PRK13968 310 MARFDLRDElHHQVEATLaegaRLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEH--ALELAN 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 795203903 472 StTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSvvGQQPFGGARASG 527
Cdd:PRK13968 388 D-SEFGLSATIFTTDETQARQMAARLE--CGGVFINGYCASD--ARVAFGGVKKSG 438
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
75-488 |
1.83e-23 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 103.68 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 75 TLDVQYQVSPfnhghkvakfCYADKslLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPHRAEIlAKTMVgqgKT 154
Cdd:PLN00412 40 TRKTQYKVQA----------CTQEE--VNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILK-EHKAPI-AECLV---KE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 155 VIQAEIDAAAELI---DFFRFNAKYAVEL--EGQQPISVP-PSTNSTVY----RGLEGFVAAISPFNFTAiggNLAG--- 221
Cdd:PLN00412 103 IAKPAKDAVTEVVrsgDLISYTAEEGVRIlgEGKFLVSDSfPGNERNKYcltsKIPLGVVLAIPPFNYPV---NLAVski 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 222 APALM-GNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSvptfkhlwkqvaq 300
Cdd:PLN00412 180 APALIaGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 301 nlDRFRTFPRLAG------ECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGR 374
Cdd:PLN00412 247 --DTGIAISKKAGmvplqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 375 IKVGDPAEDfgTFFSAVIDAKSFARIKKWLEHARSSPSlTILAGGKCDdsvGYFVEPCIVESKDPQEPIMKEEIFGPVLT 454
Cdd:PLN00412 325 LTVGPPEDD--CDITPVVSESSANFIEGLVMDAKEKGA-TFCQEWKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVLP 398
|
410 420 430
....*....|....*....|....*....|....
gi 795203903 455 VYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKD 488
Cdd:PLN00412 399 VIRINSV--EEGIHHCNA-SNFGLQGCVFTRDIN 429
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
202-528 |
1.56e-22 |
|
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: 100.37 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 202 GFVAAISPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAMLASYAIYRVLREAgLPPNIIQFVPADGPLFGDTVTSS-E 277
Cdd:cd07135 110 GVVLIIGPWNYpvlLALS-PLVGAIA-AGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQKfD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 278 HlcgINFTGSVPTFKHLWKQVAQNLDrfrtfPrLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVP 357
Cdd:cd07135 187 K---IFYTGSGRVGRIIAEAAAKHLT-----P-VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 358 HSLWPQIKGRLLEEHGRIKVGDPAEDfgTFFSAVIDAKSFARIKKWLEHARSspslTILAGGKCDDSVgYFVEPCIVESK 437
Cdd:cd07135 258 PSVYDEFVEELKKVLDEFYPGGANAS--PDYTRIVNPRHFNRLKSLLDTTKG----KVVIGGEMDEAT-RFIPPTIVSDV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 438 DPQEPIMKEEIFGPVLTVYVYPD-DKYKETLQLVDSTtsygLTGAVFSQDKDVVQeatKVL-RNAAGNFYINDKSTGSVV 515
Cdd:cd07135 331 SWDDSLMSEELFGPVLPIIKVDDlDEAIKVINSRDTP----LALYIFTDDKSEID---HILtRTRSGGVVINDTLIHVGV 403
|
330
....*....|...
gi 795203903 516 GQQPFGGARASGT 528
Cdd:cd07135 404 DNAPFGGVGDSGY 416
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
155-527 |
6.63e-21 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 95.87 E-value: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 155 VIQAEIDAAAELIDffrfnaKYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNF---TAIGgNLAGAPAlMGNVVL 231
Cdd:PTZ00381 71 LTVAEIEHLLKHLD------EYLKPEKVDTVGVFGPGKSYIIPEPL-GVVLVIGAWNYplnLTLI-PLAGAIA-AGNTVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 232 WKPSDTAMLASYAIYRVLREAgLPPNIIQFVPADgplfgdtVTSSEHLCG-----INFTGSVPTFKHLWKQVAQNLdrfr 306
Cdd:PTZ00381 142 LKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGG-------VEVTTELLKepfdhIFFTGSPRVGKLVMQAAAENL---- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 307 TFPRLagECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPHSlwpqIKGRLLEEHGRIKVGDPAEDFGT 386
Cdd:PTZ00381 210 TPCTL--ELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS----IKDKFIEALKEAIKEFFGEDPKK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 387 F--FSAVIDAKSFARIKKWLEHARSspslTILAGGKCDDSVGYfVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDdkYK 464
Cdd:PTZ00381 284 SedYSRIVNEFHTKRLAELIKDHGG----KVVYGGEVDIENKY-VAPTIIVNPDLDSPLMQEEIFGPILPILTYEN--ID 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795203903 465 ETLQLVDStTSYGLTGAVFSQDKDVVQeatKVLRN-AAGNFYINDkstgSVV----GQQPFGGARASG 527
Cdd:PTZ00381 357 EVLEFINS-RPKPLALYYFGEDKRHKE---LVLENtSSGAVVIND----CVFhllnPNLPFGGVGNSG 416
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
202-527 |
2.03e-20 |
|
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: 94.11 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 202 GFVAAISPFN--FTAIGGNLAGAPAlMGNVVLWKPSDTAMLASYAIYRVLREAgLPPNIIQFVPadgplfGDTVTSSEHL 279
Cdd:cd07136 102 GVVLIIAPWNypFQLALAPLIGAIA-AGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVE------GGVEENQELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 280 CG----INFTGSVPTFKHLWKQVAQNLdrfrTFPRLagECGGKNFHFVHCSADVD----SVVSGTLRSAfeygGQKCSAC 351
Cdd:cd07136 174 DQkfdyIFFTGSVRVGKIVMEAAAKHL----TPVTL--ELGGKSPCIVDEDANLKlaakRIVWGKFLNA----GQTCVAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 352 SRLYVPHSlwpqIKGRLLEEHGR-IK---VGDPAE--DFGTffsaVIDAKSFARIKKWLEHArsspslTILAGGKCDDSV 425
Cdd:cd07136 244 DYVLVHES----VKEKFIKELKEeIKkfyGEDPLEspDYGR----IINEKHFDRLAGLLDNG------KIVFGGNTDRET 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 426 GYfVEPCIVESKDPQEPIMKEEIFGPVLTVYVYpdDKYKETLQLVDStTSYGLTGAVFSQDKDVvqeATKVLRNAA-GNF 504
Cdd:cd07136 310 LY-IEPTILDNVTWDDPVMQEEIFGPILPVLTY--DTLDEAIEIIKS-RPKPLALYLFSEDKKV---EKKVLENLSfGGG 382
|
330 340
....*....|....*....|...
gi 795203903 505 YINDKSTGSVVGQQPFGGARASG 527
Cdd:cd07136 383 CINDTIMHLANPYLPFGGVGNSG 405
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
190-527 |
8.98e-19 |
|
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: 89.08 E-value: 8.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 190 PSTNSTVYRGLeGFVAAISPFNF---TAIGGnLAGAPAlMGNVVLWKPSDTAMLASYAIYRVLREAgLPPNIIQFV---P 263
Cdd:cd07133 92 PAKAEVEYQPL-GVVGIIVPWNYplyLALGP-LIAALA-AGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVtggA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 264 ADGPLFgdtvtSS---EHLCginFTGSVPTFKHLWKQVAQNLdrfrTFPRLagECGGKNFHFVHCSADVDSVVSGTLRSA 340
Cdd:cd07133 168 DVAAAF-----SSlpfDHLL---FTGSTAVGRHVMRAAAENL----TPVTL--ELGGKSPAIIAPDADLAKAAERIAFGK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 341 FEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIkvgdpaedFGTF-----FSAVIDAKSFARIKKWLEHARSSPS-LT 414
Cdd:cd07133 234 LLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM--------YPTLadnpdYTSIINERHYARLQGLLEDARAKGArVI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 415 ILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYpdDKYKETLQLVDSTTS----YgltgaVFSQDKdvv 490
Cdd:cd07133 306 ELNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTY--DSLDEAIDYINARPRplalY-----YFGEDK--- 375
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 795203903 491 QEATKVLRN-AAGNFYINDksTGSVVGQ--QPFGGARASG 527
Cdd:cd07133 376 AEQDRVLRRtHSGGVTIND--TLLHVAQddLPFGGVGASG 413
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
103-484 |
1.11e-18 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 89.42 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 103 NKAIEAALAARKE----WDLKPIADRAQIFLKAADMLSgPHRAEILAKTMVGQGKTVIQAEIDAAAELiDFFRFNAKYAV 178
Cdd:PLN02419 150 NEEFKAAVSAAKQafplWRNTPITTRQRVMLKFQELIR-KNMDKLAMNITTEQGKTLKDSHGDIFRGL-EVVEHACGMAT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 179 ELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIggnlagAPALM-------GNVVLWKPSDTAMLASYAIYRVLRE 251
Cdd:PLN02419 228 LQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAM------IPLWMfpvavtcGNTFILKPSEKDPGASVILAELAME 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 252 AGLPPNIIQFVPADGplfgDTVTS---SEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTfprlagECGGKNFHFVHCSAD 328
Cdd:PLN02419 302 AGLPDGVLNIVHGTN----DTVNAicdDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQS------NMGAKNHGLVLPDAN 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 329 VDSVVSGTLRSAFEYGGQKCSACSRL-YVPHSL-WpqiKGRLLEEHGRIKV---GDPAEDFGtffsAVIDAKSFARIKKW 403
Cdd:PLN02419 372 IDATLNALLAAGFGAAGQRCMALSTVvFVGDAKsW---EDKLVERAKALKVtcgSEPDADLG----PVISKQAKERICRL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 404 LEHARSSPSLTILAGgkcDDSV------GYFVEPCIVESKDPQEPIMKEEIFGPVLTvyVYPDDKYKETLQLVDStTSYG 477
Cdd:PLN02419 445 IQSGVDDGAKLLLDG---RDIVvpgyekGNFIGPTILSGVTPDMECYKEEIFGPVLV--CMQANSFDEAISIINK-NKYG 518
|
....*..
gi 795203903 478 LTGAVFS 484
Cdd:PLN02419 519 NGAAIFT 525
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
314-527 |
1.52e-16 |
|
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: 82.27 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 314 ECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSA-----CSRlYVPHSLWPQIKGRLLEEHGrikvGDPAE--DFGT 386
Cdd:cd07132 206 ELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdyvlCTP-EVQEKFVEALKKTLKEFYG----EDPKEspDYGR 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 387 ffsaVIDAKSFARIKKWLEharsspSLTILAGGKCDDSVGYfVEPCIVESKDPQEPIMKEEIFGPVLTVYVYPDdkYKET 466
Cdd:cd07132 281 ----IINDRHFQRLKKLLS------GGKVAIGGQTDEKERY-IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNN--LDEA 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795203903 467 LQLVDSTTSyGLTGAVFSQDKDVVQeatKVLRN-AAGNFYINDKSTGSVVGQQPFGGARASG 527
Cdd:cd07132 348 IEFINSREK-PLALYVFSNNKKVIN---KILSNtSSGGVCVNDTIMHYTLDSLPFGGVGNSG 405
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
200-527 |
3.69e-13 |
|
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: 71.92 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 200 LEGFVAAISPFNFTAIGGNLAGAPALMGNV-VLWKP-SDTAMLAsYAIYRVLREAG-LPPNIIQFVPAD-GPLFgDTVTS 275
Cdd:cd07128 144 RRGVAVHINAFNFPVWGMLEKFAPALLAGVpVIVKPaTATAYLT-EAVVKDIVESGlLPEGALQLICGSvGDLL-DHLGE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 276 SEHlcgINFTGSVPTFKHLwkqvaqnldrfRTFPRLAGEcggkNFHF------VHCS---ADV-------DSVVSGTLRS 339
Cdd:cd07128 222 QDV---VAFTGSAATAAKL-----------RAHPNIVAR----SIRFnaeadsLNAAilgPDAtpgtpefDLFVKEVARE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 340 AFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfGTFFSAVIDAKSFARIKKWLEHARSSPslTILAGG 419
Cdd:cd07128 284 MTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLE-GVRMGPLVSREQREDVRAAVATLLAEA--EVVFGG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 420 K-------CDDSVGYFVEPCIVESKDPQEP--IMKEEIFGPVLTVYVYpdDKYKETLQLVdsttSYG---LTGAVFSQDK 487
Cdd:cd07128 361 PdrfevvgADAEKGAFFPPTLLLCDDPDAAtaVHDVEAFGPVATLMPY--DSLAEAIELA----ARGrgsLVASVVTNDP 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 795203903 488 DvvqEATKVLRNAA---GNFYINDKST-------GSVVGQQPFGG-ARASG 527
Cdd:cd07128 435 A---FARELVLGAApyhGRLLVLNRDSakestghGSPLPQLVHGGpGRAGG 482
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
198-460 |
7.08e-12 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 67.81 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 198 RGLEGFVAAispFNFTAIGGNLAGAPALMGNV-VLWKP-SDTAMLASYAIYRVLREAGLPPNIIQFV---PAD-----GP 267
Cdd:PRK11903 149 RGVALFINA---FNFPAWGLWEKAAPALLAGVpVIVKPaTATAWLTQRMVKDVVAAGILPAGALSVVcgsSAGlldhlQP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 268 lfGDTVTssehlcginFTGSvptfkhlwkqvAQNLDRFRTFPRLAGecggknfHFVHCSADVDSVVSGTL-------RSA 340
Cdd:PRK11903 226 --FDVVS---------FTGS-----------AETAAVLRSHPAVVQ-------RSVRVNVEADSLNSALLgpdaapgSEA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 341 FEY------------GGQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAED---FGTFFSAVIDAKSFARIKKWLE 405
Cdd:PRK11903 277 FDLfvkevvremtvkSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDgvrMGPLVSRAQLAAVRAGLAALRA 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795203903 406 HArsspslTILAGGK------CDDSVGYFVEPCIVESKDPQEP--IMKEEIFGPVLTVYVYPD 460
Cdd:PRK11903 357 QA------EVLFDGGgfalvdADPAVAACVGPTLLGASDPDAAtaVHDVEVFGPVATLLPYRD 413
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
82-543 |
1.07e-11 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 67.14 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIA--DRAQ----IFLKAADMLSGPHRAEILAK-TMVGQGKT 154
Cdd:cd07126 17 LDPLN-GDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKnpERYLlygdVSHRVAHELRKPEVEDFFARlIQRVAPKS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 155 VIQA--EIDAAAELIDFF-----RFNAK-YAV--ELEGQQpisvppstnSTVYRGLEGFVAAISPFNFT----AIggNLA 220
Cdd:cd07126 96 DAQAlgEVVVTRKFLENFagdqvRFLARsFNVpgDHQGQQ---------SSGYRWPYGPVAIITPFNFPleipAL--QLM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 221 GApALMGNVVLWKPSDTAMLASYAIYRVLREAGLPPNIIQFVPADGPLFGDTVTSSEHLCgINFTGSvptfkhlwKQVAQ 300
Cdd:cd07126 165 GA-LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRM-TLFTGS--------SKVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 301 nldrfrtfpRLAGECGGK------NFHFVHCSADV---DSVVSGTLRSAFEYGGQKCSACSRLYVpHSLWPQ--IKGRLL 369
Cdd:cd07126 235 ---------RLALELHGKvkledaGFDWKILGPDVsdvDYVAWQCDQDAYACSGQKCSAQSILFA-HENWVQagILDKLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 370 EEHGRIKVGD----PAEDFGTffsavidaksfARIKKWLEHARSSPSLTILAGGK-----CDDSVGYFVEPC-----IVE 435
Cdd:cd07126 305 ALAEQRKLEDltigPVLTWTT-----------ERILDHVDKLLAIPGAKVLFGGKpltnhSIPSIYGAYEPTavfvpLEE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 436 SKDPQE-PIMKEEIFGPVLTVYVYPDDKYKETLQLVDSTTSYgLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSV 514
Cdd:cd07126 374 IAIEENfELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAH-LTAAVVSNDIRFLQEVLANTVNGTTYAGIRARTTGAP 452
|
490 500 510
....*....|....*....|....*....|..
gi 795203903 515 VGQ--QPFGGARASGTndkpGGPHYI-LRWTS 543
Cdd:cd07126 453 QNHwfGPAGDPRGAGI----GTPEAIrLVWSC 480
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
185-528 |
7.42e-11 |
|
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: 64.35 E-value: 7.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 185 PISVPPSTNSTVYRGLeGFVAAISPFNFtAIGGNL---AGAPAlMGNVVLWKPSDTAMlASYAIYRVLREAGLPPNIIQF 261
Cdd:cd07137 87 PLTTFPAKAEIVSEPL-GVVLVISAWNF-PFLLSLepvIGAIA-AGNAVVLKPSELAP-ATSALLAKLIPEYLDTKAIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 262 VPAdgplfgdTVTSSEHLC-----GINFTGSVPTFKHLWKQVAQNLDrfrtfPrLAGECGGKNFHFVHCSADVDSVVSGT 336
Cdd:cd07137 163 IEG-------GVPETTALLeqkwdKIFFTGSPRVGRIIMAAAAKHLT-----P-VTLELGGKCPVIVDSTVDLKVAVRRI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 337 LrsAFEYG---GQKCSACSRLYVPHSLWP----QIKGRLLEEHGRikvgDPAEDfgTFFSAVIDAKSFARIKKWLEHARS 409
Cdd:cd07137 230 A--GGKWGcnnGQACIAPDYVLVEESFAPtlidALKNTLEKFFGE----NPKES--KDLSRIVNSHHFQRLSRLLDDPSV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 410 SPSltILAGGKCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYpdDKYKETLQLVdSTTSYGLTGAVFSQDKDV 489
Cdd:cd07137 302 ADK--IVHGGERDEK-NLYIEPTILLDPPLDSSIMTEEIFGPLLPIITV--KKIEESIEII-NSRPKPLAAYVFTKNKEL 375
|
330 340 350
....*....|....*....|....*....|....*....
gi 795203903 490 vqEATKVLRNAAGNFYINDKSTGSVVGQQPFGGARASGT 528
Cdd:cd07137 376 --KRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVGESGF 412
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
102-527 |
1.02e-05 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 48.12 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 102 LNKAIEAALAARKEWDLKPIADRAQIFLKaadmlsgpHRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAK----YA 177
Cdd:PLN02174 19 LRRSFDDGVTRGYEWRVTQLKKLMIICDN--------HEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKqlknWM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 178 VELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFTAIGG--NLAGAPAlMGNVVLWKPSDTAMlASYAIYRVLREAGLP 255
Cdd:PLN02174 91 APEKAKTSLTTFPASAEIVSEPL-GVVLVISAWNYPFLLSidPVIGAIS-AGNAVVLKPSELAP-ASSALLAKLLEQYLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 256 PNIIQFVpaDGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfrtfprLAGECGGKNFHFVHCSADVDSVVSG 335
Cdd:PLN02174 168 SSAVRVV--EGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTP------VVLELGGKSPVVVDSDTDLKVTVRR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 336 TLrsAFEYG---GQKCSACSRLYVPHSLWPQIKGRLLEEHGRIKVGDPAEDfgTFFSAVIDAKSFARIKKWLEHARSSPS 412
Cdd:PLN02174 240 II--AGKWGcnnGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMES--KDMSRIVNSTHFDRLSKLLDEKEVSDK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 413 ltILAGGKcDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYpdDKYKETLQLVDSTTSyGLTGAVFSQDKDVVQE 492
Cdd:PLN02174 316 --IVYGGE-KDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTL--NNLEESFDVIRSRPK-PLAAYLFTHNKKLKER 389
|
410 420 430
....*....|....*....|....*....|....*.
gi 795203903 493 -ATKVlrnAAGNFYINDKSTGSVVGQQPFGGARASG 527
Cdd:PLN02174 390 fAATV---SAGGIVVNDIAVHLALHTLPFGGVGESG 422
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
227-529 |
7.89e-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: 45.55 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 227 GNVVLWKPSDTAMLA---SYAIYR-VLREAGLPPNIIQFV--PADGPLFGDTVTSSEhLCGINFTGSVPTFKHLWKQVAQ 300
Cdd:cd07127 221 GNPVIVKPHPAAILPlaiTVQVAReVLAEAGFDPNLVTLAadTPEEPIAQTLATRPE-VRIIDFTGSNAFGDWLEANARQ 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 301 NLdrfrtfprLAGECGGKNFHFVHCSADVDSVVSGTLRSAFEYGGQKCSACSRLYVP---------HSLWPQIKGRLLEE 371
Cdd:cd07127 300 AQ--------VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPrdgiqtddgRKSFDEVAADLAAA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 372 HGRIkVGDPAEDFGtFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGKCDDSVGYfvEPCIVESKDPQEPIMKEEIFGP 451
Cdd:cd07127 372 IDGL-LADPARAAA-LLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPDARVR--TPLLLKLDASDEAAYAEERFGP 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 452 VLtvYVYPDDKYKETLQLV-DSTTSYG-LTGAVFSQDKDVVQEATKVLRNAAGNFYINdkSTGSVVGQQP--FGGARASG 527
Cdd:cd07127 448 IA--FVVATDSTDHSIELArESVREHGaMTVGVYSTDPEVVERVQEAALDAGVALSIN--LTGGVFVNQSaaFSDFHGTG 523
|
..
gi 795203903 528 TN 529
Cdd:cd07127 524 AN 525
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
175-527 |
1.11e-04 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 44.72 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 175 KYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFtAIGGNL---AGAPAlMGNVVLWKPSDtamlasyaiyrvlre 251
Cdd:PLN02203 84 KWMAPKKAKLPLVAFPATAEVVPEPL-GVVLIFSSWNF-PIGLSLeplIGAIA-AGNAVVLKPSE--------------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 252 agLPPNIIQFVPADGPLFGDT---------VTSSEHLC-----GINFTGSVPTFKHLWKQVAQNLDrfrtfPrLAGECGG 317
Cdd:PLN02203 146 --LAPATSAFLAANIPKYLDSkavkvieggPAVGEQLLqhkwdKIFFTGSPRVGRIIMTAAAKHLT-----P-VALELGG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 318 KnfhfvhCSADVDSVVSGTLRS-------AFEYG---GQKCSACSRLYVPHSLWPqIKGRLLEEHGRIKVGDPAEDFGTF 387
Cdd:PLN02203 218 K------CPCIVDSLSSSRDTKvavnrivGGKWGscaGQACIAIDYVLVEERFAP-ILIELLKSTIKKFFGENPRESKSM 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 388 fSAVIDAKSFARIKKWLEHARSSPSltILAGGKCDDSvGYFVEPCIVESKDPQEPIMKEEIFGPVLTVYVYpdDKYKETL 467
Cdd:PLN02203 291 -ARILNKKHFQRLSNLLKDPRVAAS--IVHGGSIDEK-KLFIEPTILLNPPLDSDIMTEEIFGPLLPIITV--KKIEDSI 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 795203903 468 QLVDSTTSyGLTGAVFSQDKDVVQEAtkVLRNAAGNFYINDKSTGSVVGQQPFGGARASG 527
Cdd:PLN02203 365 AFINSKPK-PLAIYAFTNNEKLKRRI--LSETSSGSVTFNDAIIQYACDSLPFGGVGESG 421
|
|
| |
