|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
31-485 |
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: 871.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 31 VTNEPILAFSQGSPERDALQKALKDLKGQMEAIPCVVGDEEVWTSDIQYQLSPFNHAHKVAKFCYADKALLNRAIDAALA 110
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 111 ARKEWDLKPMADRAQVFLKAADMLSGPRRAEVLAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKFAVELEGEQPISVPPS 190
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 191 T-NHTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFG 269
Cdd:cd07123 161 VwNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 270 DTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFRTFPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSA 349
Cdd:cd07123 241 DTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 350 CSRLYVPKSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKAFARIKKWLEHARSSPSLSILAGGQCNESVGYYVE 429
Cdd:cd07123 321 ASRAYVPESLWPEVKERLLEELKEIKMGDP-DDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 568930882 430 PCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKYRETLQLVDSTTSYGLTGAVFAQD 485
Cdd:cd07123 400 PTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQD 455
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
33-489 |
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: 812.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 33 NEPILAFSQGSPERDALQKALKDLKGQMEAIPCVVGDEEVWTSDI-QYQLSPFNHAHKVAKFCYADKALLNRAIDAALAA 111
Cdd:TIGR01236 2 NEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEVYDSNErIPQVNPHNHQAVLAKATNATEEDAMKAVEAALDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 112 RKEWDLKPMADRAQVFLKAADMLSGPRRAEVLAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKFAVELEGEQPISVPPST 191
Cdd:TIGR01236 82 KKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPISAPGEW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 192 NHTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDT 271
Cdd:TIGR01236 162 NRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 272 VTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFRTFPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACS 351
Cdd:TIGR01236 242 VLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAAS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 352 RLYVPKSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKAFARIKKWLEHARSSPS-LSILAGGQCNESVGYYVEP 430
Cdd:TIGR01236 322 RLYVPHSKWPEFKSDLLAELQSVKVGDP-DDFRGFMGAVIDEQSFDKIVKYIEDAKKDPEaLTILYGGKYDDSQGYFVEP 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 568930882 431 CIIESKDPQEPIMKEEIFGPVLTVYVYPDDKYRETLQLVDSTTSYGLTGAVFAQDNHSV 489
Cdd:TIGR01236 401 TVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAI 459
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
46-487 |
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: 693.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 46 RDALQKALKDLKG-QMEAIPCVVGDEEVWTSDIQYQLSPFNHAHKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRA 124
Cdd:cd07083 1 RRAMREALRRVKEeFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 125 QVFLKAADMLSGPRRAEVLAKTMVGqGKTVIQaEIDAAAELIDFFRFNAKFAVELEGEQPI--SVPPSTNHTVYRGLeGF 202
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEV-GKNWVE-AIDDVAEAIDFIRYYARAALRLRYPAVEvvPYPGEDNESFYVGL-GA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 203 VAAISPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGI 281
Cdd:cd07083 158 GVVISPWNFPvAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 282 NFTGSVPTFKHLWRQVAQNLDRFRTFPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWP 361
Cdd:cd07083 238 NFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 362 QIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHARSspSLSILAGGQCNESVGYYVEPCIIESKDPQEP 441
Cdd:cd07083 318 PVLERLLKRAERLSVGPPEEN-GTDLGPVIDAEQEAKVLSYIEHGKN--EGQLVLGGKRLEGEGYFVAPTVVEEVPPKAR 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 568930882 442 IMKEEIFGPVLTVYVYPDDKYRETLQLVDSTTSYGLTGAVFAQDNH 487
Cdd:cd07083 395 IAQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREH 440
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
102-485 |
2.87e-122 |
|
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: 364.22 E-value: 2.87e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 102 NRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMV-GQGKTVIQAEIDAAaELIDFFRFNAKFAVELE 180
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLE--ERREELAALETlETGKPIEEALGEVA-RAADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 181 GEQ-PISVPPSTNHTVYRGLeGFVAAISPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNII 258
Cdd:cd07078 78 GEViPSPDPGELAIVRREPL-GVVGAITPWNFPlLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 259 QFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLdrfrtfPRLAGECGGKNFHFVHSSADVDSVVSGTLRS 338
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 339 AFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKAFARIKKWLEHARSSPSlSILAGG 418
Cdd:cd07078 231 AFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPL-DPDTDMGPLISAAQLDRVLAYIEDAKAEGA-KLLCGG 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930882 419 QCNES-VGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDSTTsYGLTGAVFAQD 485
Cdd:cd07078 309 KRLEGgKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEE--EAIELANDTE-YGLAAGVFTRD 373
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
63-485 |
1.03e-120 |
|
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: 361.75 E-value: 1.03e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 63 IPCVVGDEEVWTSDIQYQ--LSPFNhAHKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRA 140
Cdd:COG1012 6 YPLFIGGEWVAAASGETFdvINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE--ERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 141 EVLAKTMV-GQGKTVIQAEIDAAaELIDFFRFNAKFAVELEGEQ-PISVPPSTNHTVYRGLeGFVAAISPFNFTAIGGNL 218
Cdd:COG1012 83 EELAALLTlETGKPLAEARGEVD-RAADFLRYYAGEARRLYGETiPSDAPGTRAYVRREPL-GVVGAITPWNFPLALAAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 219 AGAPAL-MGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQV 297
Cdd:COG1012 161 KLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 298 AQNLdrfrtfPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVG 377
Cdd:COG1012 241 AENL------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 378 DPAeDFGTFFSAVIDAKAFARIKKWLEHARSSpSLSILAGGQCNE-SVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYV 456
Cdd:COG1012 315 DPL-DPGTDMGPLISEAQLERVLAYIEDAVAE-GAELLTGGRRPDgEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIP 392
|
410 420
....*....|....*....|....*....
gi 568930882 457 YPDDKyrETLQLVDStTSYGLTGAVFAQD 485
Cdd:COG1012 393 FDDEE--EAIALAND-TEYGLAASVFTRD 418
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
33-485 |
5.43e-113 |
|
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: 343.44 E-value: 5.43e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 33 NEPILAFSQGSpERDALQKALKDLKGQMEA-IPCVVGDEEVWTSDIQYQLSPFNHAHKVAKFCYADKALLNRAIDAALAA 111
Cdd:cd07124 3 NEPFTDFADEE-NRAAFRAALARVREELGReYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 112 RKEWDLKPMADRAQVFLKAADMLSgPRRAEvLAKTMVGQ-GKTVIQAEIDAAaELIDFFRFNAKFAVELEGEQPISVPPS 190
Cdd:cd07124 82 FPTWRRTPPEERARLLLRAAALLR-RRRFE-LAAWMVLEvGKNWAEADADVA-EAIDFLEYYAREMLRLRGFPVEMVPGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 191 TNHTVYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFG 269
Cdd:cd07124 159 DNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 270 DTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFRTFPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSA 349
Cdd:cd07124 238 DYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 350 CSRLYVPKSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKAFARIKKWLEHARSSPSLsiLAGGQCNESV--GYY 427
Cdd:cd07124 318 CSRVIVHESVYDEFLERLVERTKALKVGDP-EDPEVYMGPVIDKGARDRIRRYIEIGKSEGRL--LLGGEVLELAaeGYF 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 568930882 428 VEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDdkYRETLQLVDStTSYGLTGAVFAQD 485
Cdd:cd07124 395 VQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD--FDEALEIAND-TEYGLTGGVFSRS 449
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
81-485 |
2.38e-109 |
|
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: 332.19 E-value: 2.38e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 81 LSPFNHaHKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMV-GQGKTVIQAEI 159
Cdd:pfam00171 12 INPATG-EVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLE--ERKDELAELETlENGKPLAEARG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 160 DAAaELIDFFRFNAKFAVELEGEqpiSVPPSTNHTVYRGLE--GFVAAISPFNFTAiggNLAG---APALM-GNVVLWKP 233
Cdd:pfam00171 89 EVD-RAIDVLRYYAGLARRLDGE---TLPSDPGRLAYTRREplGVVGAITPWNFPL---LLPAwkiAPALAaGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 234 SDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLdrfrtfPRLAGE 313
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 314 CGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDA 393
Cdd:pfam00171 236 LGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDP-LDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 394 KAFARIKKWLEHARSSpSLSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDSTT 473
Cdd:pfam00171 315 AQLERVLKYVEDAKEE-GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEE--EAIEIANDTE 391
|
410
....*....|..
gi 568930882 474 sYGLTGAVFAQD 485
Cdd:pfam00171 392 -YGLAAGVFTSD 402
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
32-487 |
3.71e-98 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 304.94 E-value: 3.71e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 32 TNEPILAFSQgsPE-RDALQKALKDLKGQM-EAIPCVVGDEEVWTSDIQYQLSPFNHAHKVAKFCYADKALLNRAIDAAL 109
Cdd:PRK03137 6 KHEPFTDFSV--EEnVEAFEEALKKVEKELgQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 110 AARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTVIQAEIDAAaELIDFFRFNAKFAVEL-EGEQPISV 187
Cdd:PRK03137 84 EAFETWKKWSPEDRARILLRAAAIIR--RRKHEFSAWLVKEaGKPWAEADADTA-EAIDFLEYYARQMLKLaDGKPVESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 188 PPSTNHTVYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGP 266
Cdd:PRK03137 161 PGEHNRYFYIPL-GVGVVISPWNFpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 267 TFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFRTFPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQK 346
Cdd:PRK03137 240 EVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 347 CSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfgTFFSAVIDAKAFARIKKWLEHARSSPSLsiLAGGQCNESVGY 426
Cdd:PRK03137 320 CSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN--AYMGPVINQASFDKIMSYIEIGKEEGRL--VLGGEGDDSKGY 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568930882 427 YVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDdkYRETLQLVDStTSYGLTGAVFAQDNH 487
Cdd:PRK03137 396 FIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD--FDHALEIANN-TEYGLTGAVISNNRE 453
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
106-485 |
4.76e-85 |
|
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: 266.40 E-value: 4.76e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 106 DAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKFAVELEG-EQP 184
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLE--ERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGpELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 185 ISVPPSTNHTVYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPA 263
Cdd:cd06534 79 SPDPGGEAYVRREPL-GVVGVITPWNFpLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 264 DGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLdrfrtfPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYG 343
Cdd:cd06534 158 GGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 344 GQKCSACSRLYVPKSLWPQIKGRLLeehsrikvgdpaedfgtffsavidakafarikkwleharsspslsilaggqcnes 423
Cdd:cd06534 232 GQICTAASRLLVHESIYDEFVEKLV------------------------------------------------------- 256
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568930882 424 vgyyvepCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDSTTsYGLTGAVFAQD 485
Cdd:cd06534 257 -------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEE--EAIALANDTE-YGLTAGVFTRD 308
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
38-488 |
6.82e-76 |
|
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: 247.49 E-value: 6.82e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 38 AFSQGSPERDALQKALKDLK-GQMEAIPCVVGDEEVWTSDIQYqLSPFNHAHKVAKFCYADKALLNRAIDAALAARKEWD 116
Cdd:cd07125 8 RIFDLEVPLEALADALKAFDeKEWEAIPIINGEETETGEGAPV-IDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 117 LKPMADRAQVFLKAADMLSGpRRAEVLAKTMVGQGKTVIQAeIDAAAELIDFFRFNAKFAVELEGEQPISVPPS-TNHTV 195
Cdd:cd07125 87 ATPVEERAEILEKAADLLEA-NRGELIALAAAEAGKTLADA-DAEVREAIDFCRYYAAQARELFSDPELPGPTGeLNGLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 196 YRGLeGFVAAISPFNF---TAIGGNLAgapALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDT 271
Cdd:cd07125 165 LHGR-GVFVCISPWNFplaIFTGQIAA---ALAaGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 272 VTSSEHLCGINFTGSVPTFKHLWRQVAQnldRFRTFPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACS 351
Cdd:cd07125 241 LVAHPRIDGVIFTGSTETAKLINRALAE---RDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 352 RLYVPKSLWP----QIKGRLLEehsrIKVGDPAeDFGTFFSAVIDAKAFARIKKWLEHARSSPSLsiLAGGQCNESVGYY 427
Cdd:cd07125 318 LLYLQEEIAErfieMLKGAMAS----LKVGDPW-DLSTDVGPLIDKPAGKLLRAHTELMRGEAWL--IAPAPLDDGNGYF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568930882 428 VEPCIIESKDPQEpiMKEEIFGPVLTVYVYPDDKYRETLQLVDStTSYGLTGAVfaqdnHS 488
Cdd:cd07125 391 VAPGIIEIVGIFD--LTTEVFGPILHVIRFKAEDLDEAIEDINA-TGYGLTLGI-----HS 443
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
83-485 |
3.37e-71 |
|
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: 233.68 E-value: 3.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 83 PFNHAHKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMV-GQGKTVIQA--EI 159
Cdd:cd07097 21 PSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELE--ARKEELARLLTrEEGKTLPEArgEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 160 DAAaelIDFFRFNAKFAVELEGEQPISVPPSTNHTVYRGLEGFVAAISPFNF-TAIGGNLAgAPALM-GNVVLWKPSDTA 237
Cdd:cd07097 99 TRA---GQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFpIAIPAWKI-APALAyGNTVVFKPAELT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 238 MLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFRTfprlagECGGK 317
Cdd:cd07097 175 PASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQL------EMGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 318 NFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFA 397
Cdd:cd07097 249 NPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE-GVDIGPVVSERQLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 398 RIKKWLEHARSSPSlSILAGGQC--NESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDdkYRETLQLVDStTSY 475
Cdd:cd07097 328 KDLRYIEIARSEGA-KLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRD--YDEALAIAND-TEF 403
|
410
....*....|
gi 568930882 476 GLTGAVFAQD 485
Cdd:cd07097 404 GLSAGIVTTS 413
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
81-485 |
1.03e-65 |
|
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: 219.44 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 81 LSPFNHAhKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVG-QGKTVIQA-- 157
Cdd:cd07088 18 LNPATGE-VVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIR--ENADELAKLIVEeQGKTLSLArv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 158 EIDAAAeliDFFRFNAKFAVELEGEQPISVPPSTNHTVYRGLEGFVAAISPFNFTAIggnLAG---APALM-GNVVLWKP 233
Cdd:cd07088 95 EVEFTA---DYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFF---LIArklAPALVtGNTIVIKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 234 SDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLdrfrTFPRLagE 313
Cdd:cd07088 169 SEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI----TKVSL--E 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 314 CGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDA 393
Cdd:cd07088 243 LGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDA-ATDMGPLVNE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 394 KAFARIKKWLEHARSSPSLSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYpdDKYRETLQLVDStT 473
Cdd:cd07088 322 AALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKF--SSLDEAIELAND-S 398
|
410
....*....|..
gi 568930882 474 SYGLTGAVFAQD 485
Cdd:cd07088 399 EYGLTSYIYTEN 410
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
96-485 |
1.97e-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: 212.81 E-value: 1.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 96 ADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKT-MVGQGKTVIQA---EIDAAAElidFFRF 171
Cdd:cd07093 16 GGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIE--ARADELALLeSLDTGKPITLArtrDIPRAAA---NFRF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 172 NAKFAVELEGEQPISVPPSTNHTVYRGLeGFVAAISPFNFTAIggnLAG---APAL-MGNVVLWKPSDTAMLASYAVYRI 247
Cdd:cd07093 91 FADYILQLDGESYPQDGGALNYVLRQPV-GVAGLITPWNLPLM---LLTwkiAPALaFGNTVVLKPSEWTPLTAWLLAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 248 LREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFrTFprlagECGGKNFHFVHSSAD 327
Cdd:cd07093 167 ANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPV-SL-----ELGGKNPNIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 328 VDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKAFARIKKWLEHAR 407
Cdd:cd07093 241 LDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDP-LDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 408 SSPSlSILAGGQCNESV----GYYVEPCIIESKDPQEPIMKEEIFGPVLTvyVYPDDKYRETLQLVDSTTsYGLTGAVFA 483
Cdd:cd07093 320 AEGA-TILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVT--VIPFDDEEEAIELANDTP-YGLAAYVWT 395
|
..
gi 568930882 484 QD 485
Cdd:cd07093 396 RD 397
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
101-485 |
3.38e-62 |
|
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: 208.92 E-value: 3.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 101 LNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTVIQAEIDAAAElIDFFRFNAKFAVEL 179
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILE--ERRDEIADWLIREsGSTRPKAAFEVGAA-IAILREAAGLPRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 180 EGEQPISVPPSTNHTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPS-DTAMLASYAVYRILREAGLPPNI 257
Cdd:cd07104 79 EGEILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDsRTPVTGGLLIAEIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 258 IQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAqnldrfRTFPRLAGECGGKNFHFVHSSADVDSVVSGTLR 337
Cdd:cd07104 159 LNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAG------RHLKKVALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 338 SAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHARSSpSLSILAG 417
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDP-DTVIGPLINERQVDRVHAIVEDAVAA-GARLLTG 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930882 418 GqcnESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAVFAQD 485
Cdd:cd07104 311 G---TYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDE--EAVELAND-TEYGLSAAVFTRD 372
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
83-485 |
9.67e-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: 208.44 E-value: 9.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 83 PFNHAHkVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMV-GQGKTVIQA--EI 159
Cdd:cd07103 4 PATGEV-IGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIR--ERAEDLARLLTlEQGKPLAEArgEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 160 DAAAeliDFFRFNAKFAVELEGEQPISVPPSTNHTVYRGLEGFVAAISPFNFTAigGNLA--GAPAL-MGNVVLWKPSDT 236
Cdd:cd07103 81 DYAA---SFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPA--AMITrkIAPALaAGCTVVLKPAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 237 AMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDrfrtfpRLAGECGG 316
Cdd:cd07103 156 TPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVK------RVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 317 kNFHF-VHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKA 395
Cdd:cd07103 230 -NAPFiVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDE-GTDMGPLINERA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 396 FARIKKWLEHARSSPSlSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSY 475
Cdd:cd07103 308 VEKVEALVEDAVAKGA-KVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTED--EVIARAND-TPY 383
|
410
....*....|
gi 568930882 476 GLTGAVFAQD 485
Cdd:cd07103 384 GLAAYVFTRD 393
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
45-488 |
9.99e-61 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 215.19 E-value: 9.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 45 ERDALQKALKDLKG-QMEAIPCVVGDEEvwTSDIQYQLSPFNHAHKVAKFCYADKALLNRAIDAALAARKEWDLKPMADR 123
Cdd:COG4230 540 VLAALSAALAAAAEkQWQAAPLIAGEAA--SGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEER 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 124 AQVFLKAADMLSGpRRAEVLAKTMVGQGKTvIQaeiDAAAEL---IDFFRFNAKFAVELEGeqpisvppstNHTVYRGLe 200
Cdd:COG4230 618 AAILERAADLLEA-HRAELMALLVREAGKT-LP---DAIAEVreaVDFCRYYAAQARRLFA----------APTVLRGR- 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 201 GFVAAISPFNFTaiggnLAG-----APALM-GNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQFVPADGPTFGDTVT 273
Cdd:COG4230 682 GVFVCISPWNFP-----LAIftgqvAAALAaGNTVLAKPAEqTPLIAARAV-RLLHEAGVPADVLQLLPGDGETVGAALV 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 274 SSEHLCGINFTGSVPTFKHLWRQVAQNLDRFRTFprLAgECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRL 353
Cdd:COG4230 756 ADPRIAGVAFTGSTETARLINRTLAARDGPIVPL--IA-ETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVL 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 354 YVPKSLWPQ----IKGRLLEehsrIKVGDPAE---DFGtffsAVIDAKAFARIKKWLEHARSSPSL--SILAGGQCNEsv 424
Cdd:COG4230 833 CVQEDIADRvlemLKGAMAE----LRVGDPADlstDVG----PVIDAEARANLEAHIERMRAEGRLvhQLPLPEECAN-- 902
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568930882 425 GYYVEPCIIESKDPQEpiMKEEIFGPVLTVYVYpddKYRETLQLVDS--TTSYGLTGAVfaqdnHS 488
Cdd:COG4230 903 GTFVAPTLIEIDSISD--LEREVFGPVLHVVRY---KADELDKVIDAinATGYGLTLGV-----HS 958
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
90-485 |
2.03e-60 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 205.49 E-value: 2.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 90 VAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTM---VGQGKTVIQAEIDaaaELI 166
Cdd:cd07086 26 IARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALR--KKKEALGRLVsleMGKILPEGLGEVQ---EMI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 167 DFfrfnAKFAV----ELEGEqpisVPPS--TNH---TVYRGLeGFVAAISPFNF-TAIGG-NLAgaPALM-GNVVLWKPS 234
Cdd:cd07086 101 DI----CDYAVglsrMLYGL----TIPSerPGHrlmEQWNPL-GVVGVITAFNFpVAVPGwNAA--IALVcGNTVVWKPS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 235 DTAMLASYAVYRILREA----GLPPNIIQFVPADGPtFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAqnldrfRTFPRL 310
Cdd:cd07086 170 ETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVA------RRFGRV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 311 AGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 390
Cdd:cd07086 243 LLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE-GTLVGPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 391 IDAKAFARIKKWLEHARSSpSLSILAGGQC--NESVGYYVEPCIIESKDPQEPIMKEEIFGPVLtvYVYPDDKYRETLQL 468
Cdd:cd07086 322 INQAAVEKYLNAIEIAKSQ-GGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPIL--YVIKFDSLEEAIAI 398
|
410
....*....|....*..
gi 568930882 469 VDStTSYGLTGAVFAQD 485
Cdd:cd07086 399 NND-VPQGLSSSIFTED 414
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
43-478 |
2.81e-60 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 213.52 E-value: 2.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 43 SPERDALQKALKDLKG-QMEAIPCVVGDEEVwtsdiQYQLSPFNHAHKVAKFCYADKALLNRAIDAALAARKEWDLKPMA 121
Cdd:PRK11904 533 RSELEPLAAAIAAFLEkQWQAGPIINGEGEA-----RPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 122 DRAQVFLKAADMLSGpRRAEVLAKTMVGQGKTVIQAeIDAAAELIDFFRFNAKFAVELEGeQPISVPPSTNHTVYRGLEG 201
Cdd:PRK11904 608 ERAAILERAADLLEA-NRAELIALCVREAGKTLQDA-IAEVREAVDFCRYYAAQARRLFG-APEKLPGPTGESNELRLHG 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 202 ---FVAaISPFNFT-AIggnLAG--APALM-GNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQFVPADGPTFGDTVT 273
Cdd:PRK11904 685 rgvFVC-ISPWNFPlAI---FLGqvAAALAaGNTVIAKPAEqTPLIAAEAV-KLLHEAGIPKDVLQLLPGDGATVGAALT 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 274 SSEHLCGINFTGSVPTFKHLWRQVAQnldrfRTFP--RLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACS 351
Cdd:PRK11904 760 ADPRIAGVAFTGSTETARIINRTLAA-----RDGPivPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALR 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 352 RLYVPKSLWPQ----IKGRLLEehsrIKVGDPAeDFGTFFSAVIDAKAFARIKKWLEHARSSPSLsiLAGGQCNES--VG 425
Cdd:PRK11904 835 VLFVQEDIADRviemLKGAMAE----LKVGDPR-LLSTDVGPVIDAEAKANLDAHIERMKREARL--LAQLPLPAGteNG 907
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 568930882 426 YYVEPCIIESKDPQEpiMKEEIFGPVLTVYVYpddKYRETLQLVDS--TTSYGLT 478
Cdd:PRK11904 908 HFVAPTAFEIDSISQ--LEREVFGPILHVIRY---KASDLDKVIDAinATGYGLT 957
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
91-485 |
7.63e-60 |
|
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: 203.55 E-value: 7.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 91 AKFCYADKALLNRAIDAALAA--RKEW-DLKPMAdRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTViqAEIDA-AAEL 165
Cdd:cd07114 11 ARVPEASAADVDRAVAAARAAfeGGAWrKLTPTE-RGKLLRRLADLIE--ANAEELAELETRDnGKLI--RETRAqVRYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 166 IDFFRFNAKFAVELEGE-QPISVPPSTNHTVYRGLeGFVAAISPFN----FTAiggnLAGAPAL-MGNVVLWKPSDTAML 239
Cdd:cd07114 86 AEWYRYYAGLADKIEGAvIPVDKGDYLNFTRREPL-GVVAAITPWNspllLLA----KKLAPALaAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 240 ASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNldrfrtFPRLAGECGGKNF 319
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN------LAPVTLELGGKSP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 320 HFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARI 399
Cdd:cd07114 235 NIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDP-ETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 400 KKWLEHARSSPSlSILAGGQCNESV----GYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSY 475
Cdd:cd07114 314 ERYVARAREEGA-RVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEE--EAIALAND-SEY 389
|
410
....*....|
gi 568930882 476 GLTGAVFAQD 485
Cdd:cd07114 390 GLAAGIWTRD 399
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
82-485 |
9.42e-60 |
|
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: 203.21 E-value: 9.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 82 SPFnHAHKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTVIQA--E 158
Cdd:cd07149 5 SPY-DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLE--ERREEFARTIALEaGKPIKDArkE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 159 IDAAaelIDFFRFNAKFAVELEGEQ-PISVPPSTNHTV---YRGLEGFVAAISPFNFTAiggNLAG---APALM-GNVVL 230
Cdd:cd07149 82 VDRA---IETLRLSAEEAKRLAGETiPFDASPGGEGRIgftIREPIGVVAAITPFNFPL---NLVAhkvGPAIAaGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 231 WKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAqnldrfrtFPRL 310
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 311 AGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 390
Cdd:cd07149 228 TLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDE-DTDVGPM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 391 IDAKAFARIKKWLEHARSSPSlSILAGGQCNESVgyyVEPCIIESKDPQEPIMKEEIFGPVLTVYVYpdDKYRETLQLVD 470
Cdd:cd07149 307 ISEAEAERIEEWVEEAVEGGA-RLLTGGKRDGAI---LEPTVLTDVPPDMKVVCEEVFAPVVSLNPF--DTLDEAIAMAN 380
|
410
....*....|....*
gi 568930882 471 StTSYGLTGAVFAQD 485
Cdd:cd07149 381 D-SPYGLQAGVFTND 394
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
81-485 |
3.77e-59 |
|
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: 202.16 E-value: 3.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 81 LSPFNhAHKVAKFCYADKALLNRAIDAALAA--RKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAK-TMVGQGKTVIQA 157
Cdd:cd07119 18 INPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIR--EDAEELARlETLNTGKTLRES 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 158 EIDAAaELIDFFRFNAKFAVELEGEQpISVPPSTNHTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 236
Cdd:cd07119 95 EIDID-DVANCFRYYAGLATKETGEV-YDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAaGNTVVIKPSEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 237 AMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNldrfrtFPRLAGECGG 316
Cdd:cd07119 173 TPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN------VKKVALELGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 317 KNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKAF 396
Cdd:cd07119 247 KNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNG-LDADTEMGPLVSAEHR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 397 ARIKKWLEHARSSPSlSILAGGQCNE----SVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDkyRETLQLVDST 472
Cdd:cd07119 326 EKVLSYIQLGKEEGA-RLVCGGKRPTgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE--EEAIRLANDT 402
|
410
....*....|...
gi 568930882 473 TsYGLTGAVFAQD 485
Cdd:cd07119 403 P-YGLAGAVWTKD 414
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
103-485 |
3.15e-58 |
|
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: 199.11 E-value: 3.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 103 RAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTVIQA--EIDAAAELidfFRFNAKFAVEL 179
Cdd:cd07145 25 EAIEVAEKAKDVMSNLPAYKRYKILMKVAELIE--RRKEELAKLLTIEvGKPIKQSrvEVERTIRL---FKLAAEEAKVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 180 EGEqpisVPPSTNhtvYRGLE-----------GFVAAISPFNFTAiggNLAG---APAL-MGNVVLWKPSDTAMLASYAV 244
Cdd:cd07145 100 RGE----TIPVDA---YEYNErriaftvrepiGVVGAITPFNFPA---NLFAhkiAPAIaVGNSVVVKPSSNTPLTAIEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 245 YRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAqnldrfRTFPRLAGECGGKNFHFVHS 324
Cdd:cd07145 170 AKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG------GTGKKVALELGGSDPMIVLK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 325 SADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLE 404
Cdd:cd07145 244 DADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDE-STDLGPLISPEAVERMENLVN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 405 HARSSPSlSILAGGQCNEsvGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDkyRETLQLVDStTSYGLTGAVFAQ 484
Cdd:cd07145 323 DAVEKGG-KILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDD--EEAVEIANS-TEYGLQASVFTN 396
|
.
gi 568930882 485 D 485
Cdd:cd07145 397 D 397
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
86-485 |
8.97e-58 |
|
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: 197.97 E-value: 8.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 86 HAHKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSGprRAEVLAKTMVGQ-GKTV-IQAEIDAAA 163
Cdd:cd07108 6 TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEA--RSEELARLLALEtGNALrTQARPEAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 164 eLIDFFRFNAKFAVELEGEqpiSVPPSTNHTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLA 240
Cdd:cd07108 84 -LADLFRYFGGLAGELKGE---TLPFGPDVLTYTVREplGVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 241 SYAVYRILREAgLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAqnldrfrtfPRLAG---ECGGK 317
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA---------DRLIPvslELGGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 318 NFHFVHSSADVDSVVSGTLRSA-FEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDP---AEDFGtffsAVIDA 393
Cdd:cd07108 230 SPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPldeATDIG----AIISE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 394 KAFARIKKWLEHARSSPSLSILAGGQCNESV----GYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDdkYRETLQLV 469
Cdd:cd07108 306 KQFAKVCGYIDLGLSTSGATVLRGGPLPGEGpladGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKD--EDEVIAMA 383
|
410
....*....|....*.
gi 568930882 470 DSTTsYGLTGAVFAQD 485
Cdd:cd07108 384 NDSH-YGLAAYVWTRD 398
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
102-487 |
9.25e-58 |
|
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: 197.94 E-value: 9.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 102 NRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKFAVELEG 181
Cdd:cd07150 24 ERAIAAAYDAFPAWAATTPSERERILLKAAEIME--RRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVRG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 182 EQPISVPPSTNHTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQF 260
Cdd:cd07150 102 ETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 261 VPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAqnldrfRTFPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAF 340
Cdd:cd07150 182 VTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG------RHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 341 EYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKAFARIKKWLEHARSSPSlSILAGGQC 420
Cdd:cd07150 256 MHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPR-DPDTVIGPLISPRQVERIKRQVEDAVAKGA-KLLTGGKY 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568930882 421 NesvGYYVEPCIIESKDPQEPIMKEEIFGPVltVYVYPDDKYRETLQLVDStTSYGLTGAVFAQDNH 487
Cdd:cd07150 334 D---GNFYQPTVLTDVTPDMRIFREETFGPV--TSVIPAKDAEEALELAND-TEYGLSAAILTNDLQ 394
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
85-485 |
2.91e-57 |
|
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: 197.18 E-value: 2.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 85 NHAHK---VAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTVIQAEID 160
Cdd:cd07131 20 NPADLeevVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLK--KRKEELARLVTREmGKPLAEGRGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 161 AAaELIDFFRFNAKFAVELEGEQ-PISVPPSTNHTVYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAM 238
Cdd:cd07131 98 VQ-EAIDMAQYAAGEGRRLFGETvPSELPNKDAMTRRQPI-GVVALITPWNFpVAIPSWKIFPALVCGNTVVFKPAEDTP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 239 LASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAqnldrfRTFPRLAGECGGKN 318
Cdd:cd07131 176 ACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA------RPNKRVALEMGGKN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 319 FHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFAR 398
Cdd:cd07131 250 PIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDE-ETDMGPLINEAQLEK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 399 IKKWLEHARSSPSLSILAGGQCNESV---GYYVEPCIIESKDPQEPIMKEEIFGPVltVYVYPDDKYRETLQLVDStTSY 475
Cdd:cd07131 329 VLNYNEIGKEEGATLLLGGERLTGGGyekGYFVEPTVFTDVTPDMRIAQEEIFGPV--VALIEVSSLEEAIEIAND-TEY 405
|
410
....*....|
gi 568930882 476 GLTGAVFAQD 485
Cdd:cd07131 406 GLSSAIYTED 415
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
96-485 |
3.71e-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: 196.31 E-value: 3.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 96 ADKALLNRAIDAALAARKEWDLK-PMADRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTVIQAEIDAAAELIDFFRFNA 173
Cdd:cd07089 16 AGAADVDAAIAAARRAFDTGDWStDAEERARCLRQLHEALE--ARKEELRALLVAEvGAPVMTARAMQVDGPIGHLRYFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 174 KFAVELEGEQPISVPPS----TNHTVYRGLEGFVAAISPFNFtAIGGNLAG-APAL-MGNVVLWKPSDTAMLASYAVYRI 247
Cdd:cd07089 94 DLADSFPWEFDLPVPALrggpGRRVVRREPVGVVAAITPWNF-PFFLNLAKlAPALaAGNTVVLKPAPDTPLSALLLGEI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 248 LREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRfrtfprLAGECGGKNFHFVHSSAD 327
Cdd:cd07089 173 IAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKR------VLLELGGKSANIVLDDAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 328 VDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKAFARIKKWLEHAR 407
Cdd:cd07089 247 LAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPA-DPGTVMGPLISAAQRDRVEGYIARGR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 408 SSPSlSILAGGQCNES--VGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAVFAQD 485
Cdd:cd07089 326 DEGA-RLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDD--EAVRIAND-SDYGLSGGVWSAD 401
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
90-485 |
8.11e-57 |
|
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: 195.35 E-value: 8.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 90 VAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSGpRRAEVLAKTMVGQGKTVIQAEIDAAAELIDFF 169
Cdd:cd07115 10 IARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILA-NADELARLESLDTGKPIRAARRLDVPRAADTF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 170 RFNAKFAVELEGEQ-PISvPPSTNHTVyRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRI 247
Cdd:cd07115 89 RYYAGWADKIEGEViPVR-GPFLNYTV-REPVGVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELTPLSALRIAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 248 LREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDrfrtfpRLAGECGGKNFHFVHSSAD 327
Cdd:cd07115 167 MAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLK------RVSLELGGKSANIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 328 VDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKAFARIKKWLEHAR 407
Cdd:cd07115 241 LDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPL-DPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930882 408 SSPSlSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDSTTsYGLTGAVFAQD 485
Cdd:cd07115 320 EEGA-RLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEE--EALRIANGTE-YGLAAGVWTRD 393
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
73-485 |
1.24e-56 |
|
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: 195.22 E-value: 1.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 73 WTSDIqyqLSPFNhAHKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgPRRAEVLAKTMVGQGK 152
Cdd:cd07151 10 RTIDV---LNPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILE-ERRDEIVEWLIRESGS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 153 TVIQAEIDAAAElIDFFRFNAKFAVELEGEQPISVPPSTNHTVYRGLEGFVAAISPFNFTAiggNLAG---APAL-MGNV 228
Cdd:cd07151 85 TRIKANIEWGAA-MAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPL---HLSMrsvAPALaLGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 229 VLWKP-SDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDrfrtf 307
Cdd:cd07151 161 VVLKPaSDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 308 pRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFF 387
Cdd:cd07151 236 -KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDP-DTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 388 SAVIDAKAFARIKKWLEHARSSpSLSILAGGqcnESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQ 467
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEE-GATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEE--EALE 387
|
410
....*....|....*...
gi 568930882 468 LVDStTSYGLTGAVFAQD 485
Cdd:cd07151 388 LAND-TEYGLSGAVFTSD 404
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
96-485 |
1.05e-55 |
|
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: 191.97 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 96 ADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVG-QGKTVIQA--EIDAAAeliDFFRFN 172
Cdd:cd07106 16 ASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIE--ANAEELARLLTLeQGKPLAEAqfEVGGAV---AWLRYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 173 AKFAVElegeqPISVPPSTNHTV---YRGLeGFVAAISPFNFTAIggnLAG---APALM-GNVVLWKPSDTAMLASYAVY 245
Cdd:cd07106 91 ASLDLP-----DEVIEDDDTRRVelrRKPL-GVVAAIVPWNFPLL---LAAwkiAPALLaGNTVVLKPSPFTPLCTLKLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 246 RILREAgLPPNIIQFVPADGPtFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRfrtfprLAGECGGKNFHFVHSS 325
Cdd:cd07106 162 ELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKR------VTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 326 ADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEH 405
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDP-GTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 406 ARSSpSLSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAVFAQD 485
Cdd:cd07106 313 AKAK-GAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDED--EVIARAND-SEYGLGASVWSSD 388
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
90-485 |
2.08e-55 |
|
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: 191.75 E-value: 2.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 90 VAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMV-GQGKTV--IQAEIDAAAELI 166
Cdd:cd07090 10 LATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLR--ERNDEIARLETiDNGKPIeeARVDIDSSADCL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 167 DFFrfnAKFAVELEGEQpisVPPSTNHTVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYA 243
Cdd:cd07090 88 EYY---AGLAPTLSGEH---VPLPGGSFAYTRREplGVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSPFTPLTALL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 244 VYRILREAGLPPNIIQFVPADGPTfGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRfrtfprLAGECGGKNFHFVH 323
Cdd:cd07090 162 LAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKH------VTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 324 SSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKAFARIKKWL 403
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPL-DEDTQMGALISEEHLEKVLGYI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 404 EHARSSPSlSILAGGqcnESV--------GYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYpdDKYRETLQLVDSTTsY 475
Cdd:cd07090 314 ESAKQEGA-KVLCGG---ERVvpedglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPF--DTEEEVIRRANDTT-Y 386
|
410
....*....|
gi 568930882 476 GLTGAVFAQD 485
Cdd:cd07090 387 GLAAGVFTRD 396
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
103-491 |
4.64e-55 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 190.66 E-value: 4.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 103 RAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQGKTVIQA---EIDAAAELIDFFrfnAKFAVEL 179
Cdd:cd07107 23 RAVAAARAAFPEWRATTPLERARMLRELATRLR--EHAEELALIDALDCGNPVSAmlgDVMVAAALLDYF---AGLVTEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 180 EGEqpiSVPPSTNHTVYRGLE--GFVAAISPFN--FTAIGGNLAgAPALMGNVVLWKPSDTAMLASYAVYRILREAgLPP 255
Cdd:cd07107 98 KGE---TIPVGGRNLHYTLREpyGVVARIVAFNhpLMFAAAKIA-APLAAGNTVVVKPPEQAPLSALRLAELAREV-LPP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 256 NIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQnldrfrTFPRLAGECGGKNFHFVHSSADVDSVVSGT 335
Cdd:cd07107 173 GVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAE------GIKHVTLELGGKNALIVFPDADPEAAADAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 336 LRSA-FEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHARSSPSlSI 414
Cdd:cd07107 247 VAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDP-ATTMGPLVSRQQYDRVMHYIDSAKREGA-RL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 415 LAGGQCNESV----GYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAVFAQDNHSVC 490
Cdd:cd07107 325 VTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEA--EMVAQANG-VEYGLTAAIWTNDISQAH 401
|
.
gi 568930882 491 R 491
Cdd:cd07107 402 R 402
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
32-478 |
3.30e-54 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 196.62 E-value: 3.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 32 TNEPILAfsqgsperdALQKALKDLKGQM-EAIPCVVGDEEvwTSDIQYQLSPFNHAHKVAKFCYADKALLNRAIDAALA 110
Cdd:PRK11905 533 SDEATLA---------ALDEALNAFAAKTwHAAPLLAGGDV--DGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 111 ARKEWDLKPMADRAQVFLKAADMLSGpRRAEVLAKTMVGQGKTVIqaeiDAAAEL---IDFFRFNAKFAVELEGEQPIsv 187
Cdd:PRK11905 602 AFPEWSATPAAERAAILERAADLMEA-HMPELFALAVREAGKTLA----NAIAEVreaVDFLRYYAAQARRLLNGPGH-- 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 188 ppstnhtvyRGLeGFVAAISPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQFVPAD 264
Cdd:PRK11905 675 ---------KPL-GPVVCISPWNFPlAIfTGQIAAALV-AGNTVLAKPAEqTPLIAARAV-RLLHEAGVPKDALQLLPGD 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 265 GPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRfrtFPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGG 344
Cdd:PRK11905 743 GRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGP---PVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAG 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 345 QKCSACSRLYVPKSLWPQI----KGRLLEehsrIKVGDPAE---DFGtffsAVIDAKAFARIKKWLEHARSSPSL--SIL 415
Cdd:PRK11905 820 QRCSALRVLCLQEDVADRVltmlKGAMDE----LRIGDPWRlstDVG----PVIDAEAQANIEAHIEAMRAAGRLvhQLP 891
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568930882 416 AGGQCNEsvGYYVEPCIIESKDPQEpiMKEEIFGPVLTVYVYpddKYRETLQLVDS--TTSYGLT 478
Cdd:PRK11905 892 LPAETEK--GTFVAPTLIEIDSISD--LEREVFGPVLHVVRF---KADELDRVIDDinATGYGLT 949
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
90-485 |
9.97e-54 |
|
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: 187.06 E-value: 9.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 90 VAKFCYADKALLNRAIDAALAA--RKEWDLKPmADRAQVFLKAADMLSgpRRAEVLAKTM-VGQGKTVIQAEIDAAAeLI 166
Cdd:cd07109 10 FARIARGGAADVDRAVQAARRAfeSGWLRLSP-AERGRLLLRIARLIR--EHADELARLEsLDTGKPLTQARADVEA-AA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 167 DFFRFNAKFAVELEGEqpiSVPPSTNHTVYRGLE--GFVAAISPFNFTA-IGGNLAgAPAL-MGNVVLWKPSDTAMLASY 242
Cdd:cd07109 86 RYFEYYGGAADKLHGE---TIPLGPGYFVYTVREphGVTGHIIPWNYPLqITGRSV-APALaAGNAVVVKPAEDAPLTAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 243 AVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNldrfrtFPRLAGECGGKNFHFV 322
Cdd:cd07109 162 RLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEN------VVPVTLELGGKSPQIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 323 HSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDFGtfFSAVIDAKAFARIKKW 402
Cdd:cd07109 236 FADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPD--LGPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 403 LEHARSSpSLSILAGGQCNE---SVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTG 479
Cdd:cd07109 314 VARARAR-GARIVAGGRIAEgapAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEA--EAIALANG-TDYGLVA 389
|
....*.
gi 568930882 480 AVFAQD 485
Cdd:cd07109 390 GVWTRD 395
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
90-485 |
7.08e-53 |
|
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: 185.34 E-value: 7.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 90 VAKFCYADKALLNRAIDAALAA-RKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAK-TMVGQGKTVIQAEIDAAAELID 167
Cdd:cd07113 28 IASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIE--QHGEELAQlETLCSGKSIHLSRAFEVGQSAN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 168 FFRFNAKFAVELEGEQPISVPPSTNHTVYRGLE-----GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLAS 241
Cdd:cd07113 106 FLRYFAGWATKINGETLAPSIPSMQGERYTAFTrrepvGVVAGIVPWNFSVMIAVWKIGAALAtGCTIVIKPSEFTPLTL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 242 YAVYRILREAGLPPNIIQFVPADGPTfGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFRTfprlagECGGKNFHF 321
Cdd:cd07113 186 LRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTL------ELGGKNAAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 322 VHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKK 401
Cdd:cd07113 259 FLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE-SVMFGPLANQPHFDKVCS 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 402 WLEHARSSPSlSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAV 481
Cdd:cd07113 338 YLDDARAEGD-EIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEE--ELIQLIND-TPFGLTASV 413
|
....
gi 568930882 482 FAQD 485
Cdd:cd07113 414 WTNN 417
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
82-485 |
1.49e-52 |
|
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: 184.17 E-value: 1.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 82 SPFNHAHkVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTVIQA--E 158
Cdd:cd07094 5 NPYDGEV-IGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLK--KRAEEFAKIIACEgGKPIKDArvE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 159 IDAAaelIDFFRFNAKFAVELEGEQpISVPPSTNHTVYRGLE-----GFVAAISPFNFTAiggNLAG---APAL-MGNVV 229
Cdd:cd07094 82 VDRA---IDTLRLAAEEAERIRGEE-IPLDATQGSDNRLAWTirepvGVVLAITPFNFPL---NLVAhklAPAIaTGCPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 230 LWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAqnldrfrtFPR 309
Cdd:cd07094 155 VLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--------GKR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 310 LAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSA 389
Cdd:cd07094 227 IALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDE-DTDVGP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 390 VIDAKAFARIKKWLEHARSSPSlSILAGGqcnESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLV 469
Cdd:cd07094 306 LISEEAAERVERWVEEAVEAGA-RLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFE--EAIRIA 379
|
410
....*....|....*.
gi 568930882 470 DStTSYGLTGAVFAQD 485
Cdd:cd07094 380 NS-TDYGLQAGIFTRD 394
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
82-485 |
1.01e-51 |
|
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: 181.67 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 82 SPFNHaHKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTVIQAEID 160
Cdd:cd07147 5 NPYTG-EVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLE--ERFEELAETIVLEaGKPIKDARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 161 AAaELIDFFRFNAKFAVELEGE-QPISVPPSTNHtvYRGL-----EGFVAAISPFNFTAiggNLAG---APAL-MGNVVL 230
Cdd:cd07147 82 VA-RAIDTFRIAAEEATRIYGEvLPLDISARGEG--RQGLvrrfpIGPVSAITPFNFPL---NLVAhkvAPAIaAGCPFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 231 WKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTfGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNldrfrtfpRL 310
Cdd:cd07147 156 LKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--------KV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 311 AGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 390
Cdd:cd07147 227 VLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDD-ATDVGPM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 391 IDAKAFARIKKWLEHARSSPSlSILAGGQCNESVgyyVEPCIIESKDPQEPIMKEEIFGPVLTVYVYpdDKYRETLQLVD 470
Cdd:cd07147 306 ISESEAERVEGWVNEAVDAGA-KLLTGGKRDGAL---LEPTILEDVPPDMEVNCEEVFGPVVTVEPY--DDFDEALAAVN 379
|
410
....*....|....*
gi 568930882 471 StTSYGLTGAVFAQD 485
Cdd:cd07147 380 D-SKFGLQAGVFTRD 393
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
81-485 |
2.07e-51 |
|
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: 181.00 E-value: 2.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 81 LSPfNHAHKVAKFCYADKALLNRAIDAALAA--RKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTVIQA 157
Cdd:cd07118 2 RSP-AHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIR--ARRERLALIETLEsGKPISQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 158 --EIDAAAELidfFRFNAKFAVELEGEQPISVPPSTNHTVYRGLEGFVAAISPFNFTA--IGGNLAGAPAlMGNVVLWKP 233
Cdd:cd07118 79 rgEIEGAADL---WRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFliLSQKLPFALA-AGCTVVVKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 234 SD-----TAMLAsyavyRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRfrtfp 308
Cdd:cd07118 155 SEftsgtTLMLA-----ELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKK----- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 309 rLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFS 388
Cdd:cd07118 225 -VSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDP-ETKVG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 389 AVIDAKAFARIKKWLEHARSSPSLSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYpdDKYRETLQL 468
Cdd:cd07118 303 AIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTF--DTVDEAIAL 380
|
410
....*....|....*..
gi 568930882 469 VDStTSYGLTGAVFAQD 485
Cdd:cd07118 381 AND-TVYGLSAGVWSKD 396
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
96-485 |
2.67e-51 |
|
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: 181.25 E-value: 2.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 96 ADKALLNRAIDAALAARKEWDLKPM--ADRAQVFLKAADMLSgpRRAEVLAK--TMVGqGKTV-IQAEIDAAaELIDFFR 170
Cdd:cd07091 38 ADEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIE--RDRDELAAleSLDN-GKPLeESAKGDVA-LSIKCLR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 171 FNAKFAVELEGEqpiSVPPSTNHTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRI 247
Cdd:cd07091 114 YYAGWADKIQGK---TIPIDGNFLAYTRREpiGVCGQIIPWNFPLLMLAWKLAPALaAGNTVVLKPAEQTPLSALYLAEL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 248 LREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQ-NLDRFrTFprlagECGGKNFHFVHSSA 326
Cdd:cd07091 191 IKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNLKKV-TL-----ELGGKSPNIVFDDA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 327 DVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHA 406
Cdd:cd07091 265 DLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP-DTFQGPQVSKAQFDKILSYIESG 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930882 407 RSSpSLSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDSTTsYGLTGAVFAQD 485
Cdd:cd07091 344 KKE-GATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTED--EVIERANDTE-YGLAAGVFTKD 418
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
89-491 |
8.79e-51 |
|
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: 179.34 E-value: 8.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 89 KVAKfcyADKALLNRAIDAALAA--RKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKT-MVGQGKTVIQAEIDAAAEL 165
Cdd:cd07112 17 EVAA---CDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIE--AHRDELALLeTLDMGKPISDALAVDVPSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 166 IDFFRFNAKFAVELEGEqpisVPPSTNH---TVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLAS 241
Cdd:cd07112 92 ANTFRWYAEAIDKVYGE----VAPTGPDalaLITREPLGVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAEQSPLTA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 242 YAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQ-NLDRfrtfprLAGECGGKNFH 320
Cdd:cd07112 168 LRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKR------VWLECGGKSPN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 321 FV-HSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKAFARI 399
Cdd:cd07112 242 IVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPL-DPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 400 KKWLEHARSSpSLSILAGGQ--CNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDkyRETLQLVdSTTSYGL 477
Cdd:cd07112 321 LGYIESGKAE-GARLVAGGKrvLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSE--EEAVALA-NDSVYGL 396
|
410
....*....|....*..
gi 568930882 478 TGAVFAQD---NHSVCR 491
Cdd:cd07112 397 AASVWTSDlsrAHRVAR 413
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
94-485 |
4.70e-50 |
|
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: 177.15 E-value: 4.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 94 CYAD--KALLNRAIDAALAARKE--WDLKPMAdRAQVFLKAADMLSgpRRAEVLAKTMV-GQGKTVIQA--EIDAAaelI 166
Cdd:cd07120 12 TYADggVAEAEAAIAAARRAFDEtdWAHDPRL-RARVLLELADAFE--ANAERLARLLAlENGKILGEArfEISGA---I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 167 DFFRFNAKFAVELEGeQPISVPPSTNHTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKP-SDTAMLASyAV 244
Cdd:cd07120 86 SELRYYAGLARTEAG-RMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAaGCTVVVKPaGQTAQINA-AI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 245 YRILREA-GLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFrtfprlAGECGGKNFHFVH 323
Cdd:cd07120 164 IRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRL------GLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 324 SSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVG---DPAEDFGtffsAVIDAKAFARIK 400
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGpglDPASDMG----PLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 401 KWLEHARSSPSLSILAGGQCNE--SVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLT 478
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEA--EAVALAND-TDYGLA 390
|
....*..
gi 568930882 479 GAVFAQD 485
Cdd:cd07120 391 ASVWTRD 397
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
95-487 |
1.08e-49 |
|
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: 176.28 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 95 YADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTVIQA--EIDAAAELIDFFRF 171
Cdd:cd07102 14 LASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLA--ANTDEIAEELTWQmGRPIAQAggEIRGMLERARYMIS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 172 NAKFAVelegeQPISVPPSTNHT---VYRGLeGFVAAISPFN---FTAIGgnlAGAPALM-GNVVLWKPSDTAMLASYAV 244
Cdd:cd07102 92 IAEEAL-----ADIRVPEKDGFEryiRREPL-GVVLIIAPWNypyLTAVN---AVIPALLaGNAVILKHSPQTPLCGERF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 245 YRILREAGLPPNIIQFVPADGPTfGDTVTSSEHLCGINFTGSVPTFKHLWRQVAqnlDRFRTfprLAGECGGKNFHFVHS 324
Cdd:cd07102 163 AAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAA---GRFIK---VGLELGGKDPAYVRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 325 SADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLE 404
Cdd:cd07102 236 DADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDP-STTLGPVVSARAADFVRAQIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 405 HARSSPSLSILAGGQCNES--VGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLV-DSTtsYGLTGAV 481
Cdd:cd07102 315 DAIAKGARALIDGALFPEDkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDA--EAIALMnDSE--YGLTASV 390
|
....*.
gi 568930882 482 FAQDNH 487
Cdd:cd07102 391 WTKDIA 396
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
103-485 |
8.59e-49 |
|
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: 174.03 E-value: 8.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 103 RAIDAALAARKEWDLKPMADRAQVFLKAADMLSgPRRAEVLAKTMVGQGKTVIQAeIDAAAELIDFFRFNAKFAVE-LEG 181
Cdd:cd07101 22 AAFARARAAQRAWAARPFAERAAVFLRFHDLVL-ERRDELLDLIQLETGKARRHA-FEEVLDVAIVARYYARRAERlLKP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 182 EQPIS-VPPSTNHTVYRGLEGFVAAISPFNF---TAIGGNLagaPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPN 256
Cdd:cd07101 100 RRRRGaIPVLTRTTVNRRPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPDSQTALTALWAVELLIEAGLPRD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 257 IIQFVPADGPTFGDTVTssEHLCGINFTGSVPTFKHLWRQVAQNLDRFrtfprlAGECGGKNFHFVHSSADVDSVVSGTL 336
Cdd:cd07101 177 LWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRLIGC------SLELGGKNPMIVLEDADLDKAAAGAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 337 RSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGdPAEDFGTFFSAVIDAKAFARIKKWLEHARSSPSlSILA 416
Cdd:cd07101 249 RACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLG-AALDYGPDMGSLISQAQLDRVTAHVDDAVAKGA-TVLA 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 417 GGQCNESVG-YYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAVFAQD 485
Cdd:cd07101 327 GGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDD--EAIELAND-TDYGLNASVWTRD 393
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
24-481 |
8.01e-48 |
|
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: 172.40 E-value: 8.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 24 KHTSSLKVTNEPILAFSQGSPERDALQKalkdlkgqMEAIPcVVGDEEVWTSDIQYQLSPFNHAHKVAKFCYADKALLNR 103
Cdd:TIGR01238 8 KNSLGIDLDNESELKPLEAQIHAWADKT--------WQAAP-IIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 104 AIDAALAARKEWDLKPMADRAQVFLKAADMLSgPRRAEVLAKTMVGQGKTVIQAeIDAAAELIDFFRFNAKFAVELEGEQ 183
Cdd:TIGR01238 79 AIDSAQQAFPTWNATPAKERAAKLDRLADLLE-LHMPELMALCVREAGKTIHNA-IAEVREAVDFCRYYAKQVRDVLGEF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 184 piSVPPstnhtvyrglEGFVAAISPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQF 260
Cdd:TIGR01238 157 --SVES----------RGVFVCISPWNFPlAIfTGQISAALA-AGNTVIAKPAEqTSLIAYRAV-ELMQEAGFPAGTIQL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 261 VPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDrfRTFPRLAgECGGKNFHFVHSSADVDSVVSGTLRSAF 340
Cdd:TIGR01238 223 LPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRED--APVPLIA-ETGGQNAMIVDSTALPEQVVRDVLRSAF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 341 EYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEdFGTFFSAVIDAKAFARIKKWLEH----ARSSPSLSILA 416
Cdd:TIGR01238 300 DSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHL-LTTDVGPVIDAEAKQNLLAHIEHmsqtQKKIAQLTLDD 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568930882 417 GGQCNEsvGYYVEPCIIESKDPQEpiMKEEIFGPVLTVYVYpddKYRETLQLVD--STTSYGLTGAV 481
Cdd:TIGR01238 379 SRACQH--GTFVAPTLFELDDIAE--LSEEVFGPVLHVVRY---KARELDQIVDqiNQTGYGLTMGV 438
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
104-485 |
9.58e-48 |
|
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: 170.53 E-value: 9.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 104 AIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTM---VGQGKTVIQAEIDAAAELIDFfrfNAKFAVELE 180
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELLK--ANKEELARLIsreTGKPLWEAQTEVAAMAGKIDI---SIKAYHERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 181 GEQPISVPPSTNHTVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQ 259
Cdd:cd07095 80 GERATPMAQGRAVLRHRPH-GVMAVFGPFNFPGHLPNGHIVPALLaGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 260 FVPADGPTfGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFrtfprLAGECGGKNFHFVHSSADVDSVVSGTLRSA 339
Cdd:cd07095 159 LVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI-----LALEMGGNNPLVVWDVADIDAAAYLIVQSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 340 FEYGGQKCSACSRLYVPKSLWPQ-IKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHARSSPSLSILAGG 418
Cdd:cd07095 233 FLTAGQRCTCARRLIVPDGAVGDaFLERLVEAAKRLRIGAPDAE-PPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568930882 419 QCNESvGYYVEPCIIESKDPQEPiMKEEIFGPVLTVYVYpdDKYRETLQLVDStTSYGLTGAVFAQD 485
Cdd:cd07095 312 RLVAG-TAFLSPGIIDVTDAADV-PDEEIFGPLLQVYRY--DDFDEAIALANA-TRFGLSAGLLSDD 373
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
103-485 |
1.27e-47 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 172.37 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 103 RAIDAALAARKEWDLKPMADRAQVFLKAADMLSGpRRAEVLaktmvgqgkTVIQAEI-----DAAAELIDFF---RFNAK 174
Cdd:PRK09407 58 AAFARARAAQRAWAATPVRERAAVLLRFHDLVLE-NREELL---------DLVQLETgkarrHAFEEVLDVAltaRYYAR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 175 FAVELEGEQPIS--VPPSTNHTVYRGLEGFVAAISPFNF---TAIGGNLagaPALM-GNVVLWKP-SDTAMLASYAVyRI 247
Cdd:PRK09407 128 RAPKLLAPRRRAgaLPVLTKTTELRQPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPdSQTPLTALAAV-EL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 248 LREAGLPPNIIQFVPADGPTFGDTVT-SSEHLCginFTGSVPTFKHLWRQVAQNLDRFrtfprlAGECGGKNFHFVHSSA 326
Cdd:PRK09407 204 LYEAGLPRDLWQVVTGPGPVVGTALVdNADYLM---FTGSTATGRVLAEQAGRRLIGF------SLELGGKNPMIVLDDA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 327 DVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGdPAEDFGTFFSAVIDAKAFARIKKWLEHA 406
Cdd:PRK09407 275 DLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLG-AGYDYSADMGSLISEAQLETVSAHVDDA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 407 RSSPSlSILAGGQCNESVG-YYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDSTTsYGLTGAVFAQD 485
Cdd:PRK09407 354 VAKGA-TVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVD--EAVERANDTP-YGLNASVWTGD 429
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
68-485 |
2.30e-47 |
|
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: 170.44 E-value: 2.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 68 GDEEVWTSDIQYQLSPFNHAhKVAKFCYADKALLNRAIDAALAA-RKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKT 146
Cdd:cd07082 8 GEWKESSGKTIEVYSPIDGE-VIGSVPALSALEILEAAETAYDAgRGWWPTMPLEERIDCLHKFADLLK--ENKEEVANL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 147 M---VGQGKTVIQAEIDAAAELIDFFRFNAKfavELEGEQpiSVPPSTNHT------VYRGLEGFVAAISPFNFTAiggN 217
Cdd:cd07082 85 LmweIGKTLKDALKEVDRTIDYIRDTIEELK---RLDGDS--LPGDWFPGTkgkiaqVRREPLGVVLAIGPFNYPL---N 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 218 LAG---APAL-MGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHL 293
Cdd:cd07082 157 LTVsklIPALiMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 294 WRQVAQNldrfrtfpRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSR 373
Cdd:cd07082 237 KKQHPMK--------RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 374 IKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHARSSPSLSILAGGQCNESvgyYVEPCIIESKDPQEPIMKEEIFGPVLT 453
Cdd:cd07082 309 LKVGMPWDN-GVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGGN---LIYPTLLDPVTPDMRLAWEEPFGPVLP 384
|
410 420 430
....*....|....*....|....*....|..
gi 568930882 454 VYVYPDDKyrETLQLVDStTSYGLTGAVFAQD 485
Cdd:cd07082 385 IIRVNDIE--EAIELANK-SNYGLQASIFTKD 413
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
96-485 |
2.63e-47 |
|
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: 169.81 E-value: 2.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 96 ADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTVIQAEIDAAAELIDFFRFNAK 174
Cdd:cd07092 16 ASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIE--ENAEELAALESRNtGKPLHLVRDDELPGAVDNFRFFAG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 175 FAVELEGEQPISVPPSTNHTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRILREaGL 253
Cdd:cd07092 94 AARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPLTTLLLAELAAE-VL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 254 PPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRfrtfprLAGECGGKNFHFVHSSADVDSVVS 333
Cdd:cd07092 173 PPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKR------VHLELGGKAPVIVFDDADLDAAVA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 334 GTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLE----HARss 409
Cdd:cd07092 247 GIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDE-DTEMGPLNSAAQRERVAGFVErapaHAR-- 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568930882 410 pslsILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAVFAQD 485
Cdd:cd07092 324 ----VLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDED--EAIELAND-VEYGLASSVWTRD 392
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
96-485 |
3.83e-47 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 169.70 E-value: 3.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 96 ADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GK---TVIQAEIDAAaelIDFFRF 171
Cdd:PRK13473 36 ASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIE--ENADEFARLESLNcGKplhLALNDEIPAI---VDVFRF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 172 NAKFAVELEGeqPISVPPSTNHT--VYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRIL 248
Cdd:PRK13473 111 FAGAARCLEG--KAAGEYLEGHTsmIRRDPVGVVASIAPWNYPLMMAAWKLAPALAaGNTVVLKPSEITPLTALKLAELA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 249 REAgLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFRTfprlagECGGKNFHFVHSSADV 328
Cdd:PRK13473 189 ADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHL------ELGGKAPVIVFDDADL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 329 DSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKAFARIKKWLEHARS 408
Cdd:PRK13473 262 DAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDP-DDEDTELGPLISAAHRDRVAGFVERAKA 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568930882 409 SPSLSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDsTTSYGLTGAVFAQD 485
Cdd:PRK13473 341 LGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED--QAVRWAN-DSDYGLASSVWTRD 414
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
95-485 |
6.19e-47 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 168.63 E-value: 6.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 95 YADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQGKTVI---QAEIDAAAElidFFRF 171
Cdd:cd07152 9 VADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLE--EHADEIADWIVRESGSIRpkaGFEVGAAIG---ELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 172 NAKFAVELEGEQPISVPPSTNHTVYRGLeGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPS-DTAMLASYAVYRILR 249
Cdd:cd07152 84 AAGLPTQPQGEILPSAPGRLSLARRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDpRTPVSGGVVIARLFE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 250 EAGLPPNIIQFVPADGPTfGDTVTSSEHLCGINFTGSVPTfkhlWRQVAQNLDRfrTFPRLAGECGGKNFHFVHSSADVD 329
Cdd:cd07152 163 EAGLPAGVLHVLPGGADA-GEALVEDPNVAMISFTGSTAV----GRKVGEAAGR--HLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 330 SVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHARSS 409
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATG-QVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568930882 410 PSlSILAGGQCNesvGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAVFAQD 485
Cdd:cd07152 315 GA-RLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDE--EAVALAND-TEYGLSAGIISRD 383
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
102-485 |
2.45e-46 |
|
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: 166.60 E-value: 2.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 102 NRAIDAALAARKEWDLKPMADRAQVFLKAADMLsgPRRAEVLAKTMvgqgktviQAEIDAAAElidFFRFNAKFAVEL-- 179
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLL--ESRRDEFIEAM--------MEETGATAA---WAGFNVDLAAGMlr 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 180 ---------EGEQPISVPPSTNHTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILR 249
Cdd:cd07105 70 eaaslitqiIGGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRVFH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 250 EAGLPPNIIQFV---PADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDrfrtfPRLAgECGGKNFHFVHSSA 326
Cdd:cd07105 150 EAGLPKGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLK-----PVLL-ELGGKAPAIVLEDA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 327 DVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEdfgtffSAVIDAKAFARIKKWLEHA 406
Cdd:cd07105 224 DLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL------GSLVSAAAADRVKELVDDA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 407 RSSPSlSILAGGQCNESV-GYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAVFAQD 485
Cdd:cd07105 298 LSKGA-KLVVGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEE--EAVRIAND-SEYGLSAAVFTRD 373
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
104-485 |
1.63e-45 |
|
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: 165.22 E-value: 1.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 104 AIDAALAARKEWDLKPMADRAQVFLKAADMLSGpRRAEVLAKTMVGQGKTVIQAEIDAAaELIDFFRFNAKFAVELEGEQ 183
Cdd:cd07110 24 AVRAARRAFPRWKKTTGAERAKYLRAIAEGVRE-RREELAELEARDNGKPLDEAAWDVD-DVAGCFEYYADLAEQLDAKA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 184 PISVP-PSTNHTVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQ 259
Cdd:cd07110 102 ERAVPlPSEDFKARVRREpvGVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 260 FVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRfrtfprLAGECGGKNFHFVHSSADVDSVVSGTLRSA 339
Cdd:cd07110 182 VVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKP------VSLELGGKSPIIVFDDADLEKAVEWAMFGC 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 340 FEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHARSSpSLSILAGGQ 419
Cdd:cd07110 256 FWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEE-GVRLGPLVSQAQYEKVLSFIARGKEE-GARLLCGGR 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930882 420 CNESV--GYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAVFAQD 485
Cdd:cd07110 334 RPAHLekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATED--EAIALAND-SEYGLAAAVISRD 398
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
96-485 |
2.96e-45 |
|
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: 164.60 E-value: 2.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 96 ADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQGKTVIQAEIDAAAEL-IDFFRFNAK 174
Cdd:cd07138 33 GTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYE--ARADELAQAITLEMGAPITLARAAQVGLgIGHLRAAAD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 175 FAVELEGEQPISvppstNHTVYRGLEGFVAAISPFNFTA--IGGNLAgaPALM-GNVVLWKPSDTAMLASYAVYRILREA 251
Cdd:cd07138 111 ALKDFEFEERRG-----NSLVVREPIGVCGLITPWNWPLnqIVLKVA--PALAaGCTVVLKPSEVAPLSAIILAEILDEA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 252 GLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTfkhlWRQVAQNLDRfrTFPRLAGECGGKNFHFVHSSADVDSV 331
Cdd:cd07138 184 GLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRA----GKRVAEAAAD--TVKRVALELGGKSANIILDDADLEKA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 332 VSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWL-----EHA 406
Cdd:cd07138 258 VPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDP-ATTLGPLASAAQFDRVQGYIqkgieEGA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 407 RsspslsILAGG-----QCNesVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAV 481
Cdd:cd07138 337 R------LVAGGpgrpeGLE--RGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDED--EAIAIAND-TPYGLAGYV 405
|
....
gi 568930882 482 FAQD 485
Cdd:cd07138 406 WSAD 409
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
96-485 |
9.99e-45 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 163.47 E-value: 9.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 96 ADKALLNRAIDAALAA-RKEWDLK-PMADRAQVFLKAADMLSgpRRAEVLAKT-MVGQGKTVIQAEIDAAAELIDFFRFN 172
Cdd:cd07143 41 ATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLME--RNLDYLASIeALDNGKTFGTAKRVDVQASADTFRYY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 173 AKFAVELEGeQPISVPPST-NHTVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILRE 250
Cdd:cd07143 119 GGWADKIHG-QVIETDIKKlTYTRHEPI-GVCGQIIPWNFPLLMCAWKIAPALAaGNTIVLKPSELTPLSALYMTKLIPE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 251 AGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNldrfrTFPRLAGECGGKNFHFVHSSADVDS 330
Cdd:cd07143 197 AGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS-----NLKKVTLELGGKSPNIVFDDADLES 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 331 VVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHARSSP 410
Cdd:cd07143 272 AVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAE-DTFQGPQVSQIQYERIMSYIESGKAEG 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568930882 411 SLSILAGGQC-NEsvGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDSTTsYGLTGAVFAQD 485
Cdd:cd07143 351 ATVETGGKRHgNE--GYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE--EAIKRANDST-YGLAAAVFTNN 421
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
104-485 |
1.50e-44 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 163.36 E-value: 1.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 104 AIDAALAA-----RKEWDLKPMADRAQvFLKA-ADMLSgpRRAEVLAKT-MVGQGKTVIQAE--IDAAAELIDFFrfnAK 174
Cdd:PLN02467 50 AVEAARKAfkrnkGKDWARTTGAVRAK-YLRAiAAKIT--ERKSELAKLeTLDCGKPLDEAAwdMDDVAGCFEYY---AD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 175 FAVELEGEQ--PISVPPST-NHTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILRE 250
Cdd:PLN02467 124 LAEALDAKQkaPVSLPMETfKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAaGCTAVLKPSELASVTCLELADICRE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 251 AGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDrfrtfPrLAGECGGKNFHFVHSSADVDS 330
Cdd:PLN02467 204 VGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVK-----P-VSLELGGKSPIIVFDDVDLDK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 331 VVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHARSSP 410
Cdd:PLN02467 278 AVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEE-GCRLGPVVSEGQYEKVLKFISTAKSEG 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568930882 411 SlSILAGGQCNE--SVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDkyRETLQLVDSTTsYGLTGAVFAQD 485
Cdd:PLN02467 357 A-TILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE--DEAIELANDSH-YGLAGAVISND 429
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
96-487 |
1.99e-44 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 162.01 E-value: 1.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 96 ADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVG-QGKTVIQA--EIDAAAELIDFFrfn 172
Cdd:cd07099 15 TDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALA--DHADELAELLHAeTGKPRADAglEVLLALEAIDWA--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 173 AKFAVELEGEQPISVPPSTNH---TVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRIL 248
Cdd:cd07099 90 ARNAPRVLAPRKVPTGLLMPNkkaTVEYRPYGVVGVISPWNYPLLTPMGDIIPALAaGNAVVLKPSEVTPLVGELLAEAW 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 249 REAGLPPNIIQFVPADGPTfgdtvtsSEHLCG-----INFTGSVPTFKHLWRQVAQNLdrfrtFPRLAgECGGKNFHFVH 323
Cdd:cd07099 170 AAAGPPQGVLQVVTGDGAT-------GAALIDagvdkVAFTGSVATGRKVMAAAAERL-----IPVVL-ELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 324 SSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDFGTfFSAVIDAKAFARIKKWL 403
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDAD-IGPMTTARQLDIVRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 404 EHARSSPSlSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDSTTsYGLTGAVFA 483
Cdd:cd07099 316 DDAVAKGA-KALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADED--EAIALANDSR-YGLSASVFS 391
|
....
gi 568930882 484 QDNH 487
Cdd:cd07099 392 RDLA 395
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
102-491 |
1.20e-43 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 161.01 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 102 NRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVG-QGKTVIQA--EIDAAAELIDFFrfnAKFAVE 178
Cdd:PLN02278 65 NDAIASAHDAFPSWSKLTASERSKILRRWYDLII--ANKEDLAQLMTLeQGKPLKEAigEVAYGASFLEYF---AEEAKR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 179 LEGEQPISVPPSTNHTVYRGLEGFVAAISPFNFTaiggnLA-----GAPALM-GNVVLWKPSDTAMLASYAVYRILREAG 252
Cdd:PLN02278 140 VYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFP-----LAmitrkVGPALAaGCTVVVKPSELTPLTALAAAELALQAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 253 LPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQnldrfrTFPRLAGECGGKNFHFVHSSADVDSVV 332
Cdd:PLN02278 215 IPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAA------TVKRVSLELGGNAPFIVFDDADLDVAV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 333 SGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHARSSPSl 412
Cdd:PLN02278 289 KGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEE-GVTQGPLINEAAVQKVESHVQDAVSKGA- 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930882 413 SILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDkyRETLQLVDSTTsYGLTGAVFAQDNHSVCR 491
Cdd:PLN02278 367 KVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE--EEAIAIANDTE-AGLAAYIFTRDLQRAWR 442
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
139-485 |
4.68e-43 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 157.21 E-value: 4.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 139 RAEVLAKTMVG-QGKTVIQAEIDAAAElIDFFRFNAKFAVELEGEQPISVPPSTNHTVYRGLEGFVAAISPFNFT--AIG 215
Cdd:PRK10090 11 RASEISALIVEeGGKIQQLAEVEVAFT-ADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPffLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 216 GNLAgaPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLW 294
Cdd:PRK10090 90 RKMA--PALLtGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 295 RQVAQNLdrfrtfPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRI 374
Cdd:PRK10090 168 AAAAKNI------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 375 KVGDPAEDFGTFFSAVIDAKAFARIKKWLEHARSSPSlSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTV 454
Cdd:PRK10090 242 QFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGA-RVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350
....*....|....*....|....*....|.
gi 568930882 455 YVYpdDKYRETLQLVDStTSYGLTGAVFAQD 485
Cdd:PRK10090 321 VAF--DTLEEAIAMAND-SDYGLTSSIYTQN 348
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
101-491 |
6.57e-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: 157.91 E-value: 6.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 101 LNRAIDAALAARKEwdLKPMaDRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTVIQA--EIDAAaelIDFFRFNAKFAV 177
Cdd:cd07146 23 LREALALAASYRST--LTRY-QRSAILNKAAALLE--ARREEFARLITLEsGLCLKDTryEVGRA---ADVLRFAAAEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 178 ELEGEQpISVPPSTNHTVYRGLE-----GFVAAISPFNFTAiggNLAG---APALM-GNVVLWKPSDTAMLASYAVYRIL 248
Cdd:cd07146 95 RDDGES-FSCDLTANGKARKIFTlreplGVVLAITPFNHPL---NQVAhkiAPAIAaNNRIVLKPSEKTPLSAIYLADLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 249 REAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAqnldrfrtFPRLAGECGGKNFHFVHSSADV 328
Cdd:cd07146 171 YEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLELGGNDPLIVMDDADL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 329 DSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHARS 408
Cdd:cd07146 243 ERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDP-ATDMGTVIDEEAAIQIENRVEEAIA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 409 SPSlSILAGgqcNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAVFAQDNHS 488
Cdd:cd07146 322 QGA-RVLLG---NQRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLD--EAIAISNS-TAYGLSSGVCTNDLDT 394
|
...
gi 568930882 489 VCR 491
Cdd:cd07146 395 IKR 397
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
96-478 |
8.56e-43 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 162.84 E-value: 8.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 96 ADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSGprRAEVLAKTMVGQ-GKTVIQAeIDAAAELIDFFRFnak 174
Cdd:PRK11809 679 ATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEA--QMQTLMGLLVREaGKTFSNA-IAEVREAVDFLRY--- 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 175 FAVELEGEqpisvppSTNHTvYRGLeGFVAAISPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAMLASYAVyRILREA 251
Cdd:PRK11809 753 YAGQVRDD-------FDNDT-HRPL-GPVVCISPWNFPlAIfTGQVAAALA-AGNSVLAKPAEqTPLIAAQAV-RILLEA 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 252 GLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLD-RFRTFPRLAgECGGKNFHFVHSSADVDS 330
Cdd:PRK11809 822 GVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDpQGRPIPLIA-ETGGQNAMIVDSSALTEQ 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 331 VVSGTLRSAFEYGGQKCSA----CSRLYVPKSLWPQIKGRLLEehsrIKVGDPaEDFGTFFSAVIDAKAFARIKKWLEHA 406
Cdd:PRK11809 901 VVADVLASAFDSAGQRCSAlrvlCLQDDVADRTLKMLRGAMAE----CRMGNP-DRLSTDIGPVIDAEAKANIERHIQAM 975
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568930882 407 RSS--PSLSILAGGQCNESVGYYVEPCIIESKDPQEpiMKEEIFGPVLTVYVYPddkyRETL-QLVDS--TTSYGLT 478
Cdd:PRK11809 976 RAKgrPVFQAARENSEDWQSGTFVPPTLIELDSFDE--LKREVFGPVLHVVRYN----RNQLdELIEQinASGYGLT 1046
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
105-485 |
1.32e-42 |
|
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: 157.35 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 105 IDAAL-AARK-----EWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTVIQAEIDAAAELIDFFRFNAKFAV 177
Cdd:cd07139 38 VDAAVaAARRafdngPWPRLSPAERAAVLRRLADALE--ARADELARLWTAEnGMPISWSRRAQGPGPAALLRYYAALAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 178 ELEGEQPISvPPSTNHT-VYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPP 255
Cdd:cd07139 116 DFPFEERRP-GSGGGHVlVRREPVGVVAAIVPWNAPLFLAALKIAPALAaGCTVVLKPSPETPLDAYLLAEAAEEAGLPP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 256 NIIQFVPADgptfgdtVTSSEHLCG------INFTGSVPTFKHLWRQVAQNLDRFRTfprlagECGGKNFHFVHSSADVD 329
Cdd:cd07139 195 GVVNVVPAD-------REVGEYLVRhpgvdkVSFTGSTAAGRRIAAVCGERLARVTL------ELGGKSAAIVLDDADLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 330 SVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHARSS 409
Cdd:cd07139 262 AAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP-ATQIGPLASARQRERVEGYIAKGRAE 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568930882 410 PSLSILAGGQCNE-SVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAVFAQD 485
Cdd:cd07139 341 GARLVTGGGRPAGlDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED--DAVRIAND-SDYGLSGSVWTAD 414
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
90-485 |
1.43e-42 |
|
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: 157.57 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 90 VAKFCYADKALLNRAIDAALAARKEWDLK-PMADRAQVFLKAADMLSgpRRAEVLA--KTMvGQGKTVIQAEIDAAAELI 166
Cdd:cd07144 36 IASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVE--KNRDLLAaiEAL-DSGKPYHSNALGDLDEII 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 167 DFFRFNAKFAVELEGEQPISVPPSTNHTVYRGLeGFVAAISPFNFTAiggNLAG---APALM-GNVVLWKPSDTAMLASY 242
Cdd:cd07144 113 AVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPY-GVCGQIIPWNYPL---AMAAwklAPALAaGNTVVIKPAENTPLSLL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 243 AVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDrfrtfpRLAGECGGKNFHFV 322
Cdd:cd07144 189 YFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLK------AVTLECGGKSPALV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 323 HSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEE-HSRIKVGDPAEDfGTFFSAVIDAKAFARIKK 401
Cdd:cd07144 263 FEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHvKQNYKVGSPFDD-DTVVGPQVSKTQYDRVLS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 402 WLEHARSSPSlSILAGGQCNESV---GYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDdkYRETLQLVDSTTsYGLT 478
Cdd:cd07144 342 YIEKGKKEGA-KLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKT--YEEAIKKANDTT-YGLA 417
|
....*..
gi 568930882 479 GAVFAQD 485
Cdd:cd07144 418 AAVFTKD 424
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
96-485 |
2.37e-42 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 156.96 E-value: 2.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 96 ADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMV-GQGKTvIQ----AEIDAAAELIDFFr 170
Cdd:PRK13252 41 ATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILR--ERNDELAALETlDTGKP-IQetsvVDIVTGADVLEYY- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 171 fnAKFAVELEGEQpisVPPSTNHTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRI 247
Cdd:PRK13252 117 --AGLAPALEGEQ---IPLRGGSFVYTRREplGVCAGIGAWNYPIQIACWKSAPALaAGNAMIFKPSEVTPLTALKLAEI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 248 LREAGLPPNIIQFVPADGPTfGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRfrtfprLAGECGGKNFHFVHSSAD 327
Cdd:PRK13252 192 YTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKE------VTMELGGKSPLIVFDDAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 328 VDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAKAFARIKKWLEHAR 407
Cdd:PRK13252 265 LDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDP-MDPATNFGPLVSFAHRDKVLGYIEKGK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 408 SSPSlSILAGGQC----NESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDSTTsYGLTGAVFA 483
Cdd:PRK13252 344 AEGA-RLLCGGERltegGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDED--EVIARANDTE-YGLAAGVFT 419
|
..
gi 568930882 484 QD 485
Cdd:PRK13252 420 AD 421
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
89-485 |
2.84e-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: 156.60 E-value: 2.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 89 KVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLsgprRAEvlaKTMVGQ------GKTVIQA--EID 160
Cdd:cd07130 24 PIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDAL----RKK---KEALGKlvslemGKILPEGlgEVQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 161 aaaELIDFfrfnAKFAVELEGEQPISVPPS--TNHtvyRGLE-----GFVAAISPFNF-TAIGG-NLAGApALMGNVVLW 231
Cdd:cd07130 97 ---EMIDI----CDFAVGLSRQLYGLTIPSerPGH---RMMEqwnplGVVGVITAFNFpVAVWGwNAAIA-LVCGNVVVW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 232 KPSDTAMLASYAVYRI----LREAGLPPNIIQFVPADGPTfGDTVTSSEHLCGINFTGSVptfkHLWRQVAQNLDRfRtF 307
Cdd:cd07130 166 KPSPTTPLTAIAVTKIvarvLEKNGLPGAIASLVCGGADV-GEALVKDPRVPLVSFTGST----AVGRQVGQAVAA-R-F 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 308 PRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFF 387
Cdd:cd07130 239 GRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDD-GTLV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 388 SAVIDAKAFARIKKWLEHARSSPSlSILAGGQCNESVGYYVEPCIIESKdPQEPIMKEEIFGPVLtvYVYPDDKYRETLQ 467
Cdd:cd07130 318 GPLHTKAAVDNYLAAIEEAKSQGG-TVLFGGKVIDGPGNYVEPTIVEGL-SDAPIVKEETFAPIL--YVLKFDTLEEAIA 393
|
410
....*....|....*...
gi 568930882 468 LVDStTSYGLTGAVFAQD 485
Cdd:cd07130 394 WNNE-VPQGLSSSIFTTD 410
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
101-485 |
7.06e-42 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 154.54 E-value: 7.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 101 LNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQ-GKTVIQA--EIDAAAELIDFFrfnAKFAV 177
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLR--ERKDELARLITLEmGKPIAEAraEVEKCAWICRYY---AENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 178 ELEGEQPISVPPSTNHTVYRGLeGFVAAISPFNFT-------AiggnlagAPALM-GNVVLWKPSDTAMLASYAVYRILR 249
Cdd:cd07100 76 AFLADEPIETDAGKAYVRYEPL-GVVLGIMPWNFPfwqvfrfA-------APNLMaGNTVLLKHASNVPGCALAIEELFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 250 EAGLPPNIIQFVPADGPTFgDTVTSSEHLCGINFTGSVPTfkhlWRQVAQnldrfrtfprLAG--------ECGGKNFHF 321
Cdd:cd07100 148 EAGFPEGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERA----GRAVAA----------EAGknlkksvlELGGSDPFI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 322 VHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKK 401
Cdd:cd07100 213 VLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDE-DTDLGPLARKDLRDELHE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 402 WLEHARSSpSLSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAV 481
Cdd:cd07100 292 QVEEAVAA-GATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEE--EAIALAND-SPFGLGGSV 367
|
....
gi 568930882 482 FAQD 485
Cdd:cd07100 368 FTTD 371
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
81-491 |
1.03e-40 |
|
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: 152.50 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 81 LSPFNhAHKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSGPRRAEVLAKTMvGQGKTV---IQA 157
Cdd:cd07559 21 YNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETL-DNGKPIretLAA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 158 EIDAAaelIDFFRFNAKFAVELEG------EQPISVppstnhtVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVL 230
Cdd:cd07559 99 DIPLA---IDHFRYFAGVIRAQEGslseidEDTLSY-------HFHEPLGVVGQIIPWNFPLLMAAWKLAPALAaGNTVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 231 WKPSDTAMLASYAVYRILREAgLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLdrfrtFPrL 310
Cdd:cd07559 169 LKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL-----IP-V 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 311 AGECGGK--NFHF--VHSSAD--VDSVVSGTLRSAFEYGgQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfG 384
Cdd:cd07559 242 TLELGGKspNIFFddAMDADDdfDDKAEEGQLGFAFNQG-EVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP-E 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 385 TFFSAVIDAKAFARIKKWLEHARSSPSlSILAGGQCNESV----GYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDD 460
Cdd:cd07559 320 TMMGAQVSKDQLEKILSYVDIGKEEGA-EVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE 398
|
410 420 430
....*....|....*....|....*....|.
gi 568930882 461 KyrETLQLVDStTSYGLTGAVFAQDNHSVCR 491
Cdd:cd07559 399 E--EAIAIAND-TEYGLGGGVWTRDINRALR 426
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
90-485 |
2.07e-40 |
|
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: 151.49 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 90 VAKFCYADKALLNRAIDAALAARKE--WDLKPMADRAQVFLKAADMLSgpRRAEVLAK-TMVGQGKTVIQAEIDAAAELI 166
Cdd:cd07142 32 IAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLE--KHADELAAlETWDNGKPYEQARYAEVPLAA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 167 DFFRFNAKFAVELEGEqpiSVPPSTNHTVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYA 243
Cdd:cd07142 110 RLFRYYAGWADKIHGM---TLPADGPHHVYTLHEpiGVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEQTPLSALL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 244 VYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQ-NLDrfrtfpRLAGECGGKNFHFV 322
Cdd:cd07142 187 AAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLK------PVTLELGGKSPFIV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 323 HSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPaedfgtFFSAV-----IDAKAFA 397
Cdd:cd07142 261 CEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDP------FRKGVeqgpqVDKEQFE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 398 RIKKWLEHARSSPSlSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDdkYRETLQLVDStTSYGL 477
Cdd:cd07142 335 KILSYIEHGKEEGA-TLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKT--VDEVIKRANN-SKYGL 410
|
....*...
gi 568930882 478 TGAVFAQD 485
Cdd:cd07142 411 AAGVFSKN 418
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
89-485 |
3.75e-40 |
|
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: 150.68 E-value: 3.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 89 KVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAK--TMvGQGKTVIQ---AEIDAAA 163
Cdd:cd07117 28 TLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIID--ENKELLAMveTL-DNGKPIREtraVDIPLAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 164 eliDFFRFnakFAVELEGE--QPISVPPSTNHTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLA 240
Cdd:cd07117 105 ---DHFRY---FAGVIRAEegSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAaGNTVVIKPSSTTSLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 241 SYAVYRILREAgLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLdrfrtFPRLAgECGGKNFH 320
Cdd:cd07117 179 LLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL-----IPATL-ELGGKSAN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 321 FVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIK 400
Cdd:cd07117 252 IIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDP-DTQMGAQVNKDQLDKIL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 401 KWLEHARSSPSlSILAGGQ----CNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYG 476
Cdd:cd07117 331 SYVDIAKEEGA-KILTGGHrlteNGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTED--EVIDMAND-SEYG 406
|
....*....
gi 568930882 477 LTGAVFAQD 485
Cdd:cd07117 407 LGGGVFTKD 415
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
90-485 |
9.45e-38 |
|
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: 144.20 E-value: 9.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 90 VAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMV-GQGKTVIQA--EIDAAAELI 166
Cdd:cd07085 29 IARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLE--ENLDELARLITlEHGKTLADArgDVLRGLEVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 167 DffrFNAKFAVELEGEQPISVPPSTNHTVYRGLEGFVAAISPFNFTAIggnlagAPALM-------GNVVLWKPSDTAML 239
Cdd:cd07085 107 E---FACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAM------IPLWMfpmaiacGNTFVLKPSERVPG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 240 ASYAVYRILREAGLPPNIIQFVPADgptfGDTVtssEHLC------GINFTGSVPTFKHLWRQVAQNLDRFRTFprlage 313
Cdd:cd07085 178 AAMRLAELLQEAGLPDGVLNVVHGG----KEAV---NALLdhpdikAVSFVGSTPVGEYIYERAAANGKRVQAL------ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 314 CGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGdPAEDFGTFFSAVIDA 393
Cdd:cd07085 245 GGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVG-AGDDPGADMGPVISP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 394 KAFARIKKWLEHArsspslsILAGGQC-----NESV-----GYYVEPCIIESKDPQEPIMKEEIFGPVLTVyVYPDDkYR 463
Cdd:cd07085 324 AAKERIEGLIESG-------VEEGAKLvldgrGVKVpgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSI-VRVDT-LD 394
|
410 420
....*....|....*....|..
gi 568930882 464 ETLQLVDStTSYGLTGAVFAQD 485
Cdd:cd07085 395 EAIAIINA-NPYGNGAAIFTRS 415
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
89-485 |
1.86e-37 |
|
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: 143.26 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 89 KVAKFCYADKALLNRAIDAALAARK---EWDLKPMADRAQVFLKAADMLSGPRRAEVLAKTMVGqGKTVIQAEIDAAAEL 165
Cdd:cd07141 34 KICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDN-GKPFSKSYLVDLPGA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 166 IDFFRFNAKFAVELEGEqpiSVPPSTNHTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASY 242
Cdd:cd07141 113 IKVLRYYAGWADKIHGK---TIPMDGDFFTYTRHEpvGVCGQIIPWNFPLLMAAWKLAPALaCGNTVVLKPAEQTPLTAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 243 AVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTfKHLWRQVA--QNLDrfrtfpRLAGECGGKNFH 320
Cdd:cd07141 190 YLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV-GKLIQQAAgkSNLK------RVTLELGGKSPN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 321 FVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIK 400
Cdd:cd07141 263 IVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDP-KTEQGPQIDEEQFKKIL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 401 KWLEHARSSPSlSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYvypddKYRETLQLVD--STTSYGLT 478
Cdd:cd07141 342 ELIESGKKEGA-KLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIF-----KFKTIDEVIEraNNTTYGLA 415
|
....*..
gi 568930882 479 GAVFAQD 485
Cdd:cd07141 416 AAVFTKD 422
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
89-490 |
2.06e-37 |
|
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: 143.31 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 89 KVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSGPRRAEVLAKTMVGqGKTVIQ---AEIDAAAEL 165
Cdd:cd07111 49 VLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDN-GKPIREsrdCDIPLVARH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 166 idfFRFNAKFAVELEGEQPISVPPstnhtvyrgleGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAV 244
Cdd:cd07111 128 ---FYHHAGWAQLLDTELAGWKPV-----------GVVGQIVPWNFPLLMLAWKICPALaMGNTVVLKPAEYTPLTALLF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 245 YRILREAGLPPNIIQFVPADGpTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQnldrfrTFPRLAGECGGKNFHFVHS 324
Cdd:cd07111 194 AEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAG------TGKKLSLELGGKSPFIVFD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 325 SADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDP---AEDFGtffsAVIDAKAFARIKK 401
Cdd:cd07111 267 DADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPldkAIDMG----AIVDPAQLKRIRE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 402 WLEHARSSPSLSILAGGQCNESvGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAV 481
Cdd:cd07111 343 LVEEGRAEGADVFQPGADLPSK-GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAK--EAVALANN-TPYGLAASV 418
|
....*....
gi 568930882 482 FAqDNHSVC 490
Cdd:cd07111 419 WS-ENLSLA 426
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
96-487 |
2.13e-37 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 143.17 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 96 ADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAkTMVGQ--GKTVIQAEIDAAAELidffrfnA 173
Cdd:PRK09457 34 ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLE--ENKEELA-EVIARetGKPLWEAATEVTAMI-------N 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 174 KFAV------ELEGEQPISVPPSTNHTVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYR 246
Cdd:PRK09457 104 KIAIsiqayhERTGEKRSEMADGAAVLRHRPH-GVVAVFGPYNFPGHLPNGHIVPALLaGNTVVFKPSELTPWVAELTVK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 247 ILREAGLPPNIIQFVPAdGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFrtfprLAGECGGKNFHFVHSSA 326
Cdd:PRK09457 183 LWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKI-----LALEMGGNNPLVIDEVA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 327 DVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQ-IKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKAFARIKKWLEH 405
Cdd:PRK09457 257 DIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWDAEPQPFMGAVISEQAAQGLVAAQAQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 406 ARSSPSLSILAGGQCNESVGyYVEPCIIESKDPQEPImKEEIFGPVLTVYVYPDdkYRETLQLVDStTSYGLTGAVFAQD 485
Cdd:PRK09457 337 LLALGGKSLLEMTQLQAGTG-LLTPGIIDVTGVAELP-DEEYFGPLLQVVRYDD--FDEAIRLANN-TRFGLSAGLLSDD 411
|
..
gi 568930882 486 NH 487
Cdd:PRK09457 412 RE 413
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
103-487 |
2.43e-35 |
|
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: 137.05 E-value: 2.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 103 RAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAK-TMVGQGKTVIQA---EIDAAAELIdffRFNAKfave 178
Cdd:cd07098 22 EAIAAARAAQREWAKTSFAERRKVLRSLLKYIL--ENQEEICRvACRDTGKTMVDAslgEILVTCEKI---RWTLK---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 179 lEGE---QPISVPPSTNhTVYRGLE------GFVAAISPFNF---TAIGGNLAgapALM-GNVVLWKPSDTAMLASYAVY 245
Cdd:cd07098 93 -HGEkalRPESRPGGLL-MFYKRARveyeplGVVGAIVSWNYpfhNLLGPIIA---ALFaGNAIVVKVSEQVAWSSGFFL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 246 RILREA----GLPPNIIQFVPADGPTfGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDrfrtfPRLAgECGGKNFHF 321
Cdd:cd07098 168 SIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLT-----PVVL-ELGGKDPAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 322 VHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAE---DFGtffsAVIDAKAFAR 398
Cdd:cd07098 241 VLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDgdvDVG----AMISPARFDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 399 IKKWLEHARSSPSlSILAGGQ----CNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTS 474
Cdd:cd07098 317 LEELVADAVEKGA-RLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDE--EAVEIANS-TE 392
|
410
....*....|...
gi 568930882 475 YGLTGAVFAQDNH 487
Cdd:cd07098 393 YGLGASVFGKDIK 405
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
103-491 |
5.52e-34 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 133.49 E-value: 5.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 103 RAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTM-VGQGKTVIQA--EIDAAAELIDFFRFNAK--FAV 177
Cdd:PRK11241 52 AAIDAANRALPAWRALTAKERANILRRWFNLMM--EHQDDLARLMtLEQGKPLAEAkgEISYAASFIEWFAEEGKriYGD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 178 ELEGEQPisvppSTNHTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPN 256
Cdd:PRK11241 130 TIPGHQA-----DKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIRAGIPAG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 257 IIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRfrtfprLAGECGGKNFHFVHSSADVDSVVSGTL 336
Cdd:PRK11241 205 VFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK------VSLELGGNAPFIVFDDADLDKAVEGAL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 337 RSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHARSSPSlSILA 416
Cdd:PRK11241 279 ASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK-GVTIGPLIDEKAVAKVEEHIADALEKGA-RVVC 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568930882 417 GGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAVFAQDNHSVCR 491
Cdd:PRK11241 357 GGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEA--DVIAQAND-TEFGLAAYFYARDLSRVFR 428
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
101-485 |
1.10e-33 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 133.39 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 101 LNRAIDAALAARKE--WDLKPMADRAQVFLKAADMLSgPRRAEVLAKTMVGQGKTVIQAeidAAAEL---IDFFRFNAKF 175
Cdd:PLN02466 97 VNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLE-KHNDELAALETWDNGKPYEQS---AKAELpmfARLFRYYAGW 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 176 AVELEGeqpISVPPSTNHTVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAG 252
Cdd:PLN02466 173 ADKIHG---LTVPADGPHHVQTLHEpiGVAGQIIPWNFPLLMFAWKVGPALAcGNTIVLKTAEQTPLSALYAAKLLHEAG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 253 LPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFRTFprlagECGGKNFHFVHSSADVDSVV 332
Cdd:PLN02466 250 LPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVTL-----ELGGKSPFIVCEDADVDKAV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 333 SGTLRSAFEYGGQKCSACSRLYVPKSLWPQI----KGRLLeehsRIKVGDPaedfgtFFSAV-----IDAKAFARIKKWL 403
Cdd:PLN02466 325 ELAHFALFFNQGQCCCAGSRTFVHERVYDEFvekaKARAL----KRVVGDP------FKKGVeqgpqIDSEQFEKILRYI 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 404 EHARSSPSlSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDdkYRETLQLVDStTSYGLTGAVFA 483
Cdd:PLN02466 395 KSGVESGA-TLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKD--LDEVIRRANN-TRYGLAAGVFT 470
|
..
gi 568930882 484 QD 485
Cdd:PLN02466 471 QN 472
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
90-485 |
1.21e-33 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 133.02 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 90 VAKFCYADKALLNRAIDAALAA--RKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAK-------TMVGQGKTViqaEID 160
Cdd:PLN02766 49 IARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIE--EHIEELAAldtidagKLFALGKAV---DIP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 161 AAAELidfFRFNAKFAVELEGEQPISVPPSTNHTVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAML 239
Cdd:PLN02766 124 AAAGL---LRYYAGAADKIHGETLKMSRQLQGYTLKEPI-GVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQTPL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 240 ASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQ-NLDRfrtfprLAGECGGKN 318
Cdd:PLN02766 200 SALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNLKQ------VSLELGGKS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 319 FHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKAFAR 398
Cdd:PLN02766 274 PLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF-DPRARQGPQVDKQQFEK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 399 IKKWLEHARSSPSlSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYvypddKYR---ETLQLVDStTSY 475
Cdd:PLN02766 353 ILSYIEHGKREGA-TLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLM-----KFKtveEAIKKANN-TKY 425
|
410
....*....|
gi 568930882 476 GLTGAVFAQD 485
Cdd:PLN02766 426 GLAAGIVTKD 435
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
81-485 |
2.39e-31 |
|
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: 125.61 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 81 LSPFNHAHkVAKFCYADKALLNRAIDAALAA---RKEWdlKPMADRAQVFLKAADMLSGprRAEVLAKTMVGQG-KTVIQ 156
Cdd:cd07148 4 VNPFDLKP-IGEVPTVDWAAIDKALDTAHALfldRNNW--LPAHERIAILERLADLMEE--RADELALLIAREGgKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 157 A--EIDAAaelIDFFRFNAKFAVELEGEQ-PISV-PPSTNHTVYRGLE--GFVAAISPFNFTAiggNLA---GAPAL-MG 226
Cdd:cd07148 79 AkvEVTRA---IDGVELAADELGQLGGREiPMGLtPASAGRIAFTTREpiGVVVAISAFNHPL---NLIvhqVAPAIaAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 227 NVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEhLCGINFTGSVPTFKHLWRQVAQNldrfrt 306
Cdd:cd07148 153 CPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPR-VAFFSFIGSARVGWMLRSKLAPG------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 307 fPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAeDFGTF 386
Cdd:cd07148 226 -TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPT-DPDTE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 387 FSAVIDAKAFARIKKWLEHARSSPSlSILAGGQCNESVGYyvEPCIIESKDPQEPIMKEEIFGPVLTVYVYpdDKYRETL 466
Cdd:cd07148 304 VGPLIRPREVDRVEEWVNEAVAAGA-RLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSY--DDLDEAI 378
|
410
....*....|....*....
gi 568930882 467 QLVDStTSYGLTGAVFAQD 485
Cdd:cd07148 379 AQANS-LPVAFQAAVFTKD 396
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
90-485 |
2.47e-30 |
|
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: 123.37 E-value: 2.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 90 VAKFCYADKALLNRAIDAALAA--RKEWDLKPMADRAQVFLKAADMLSgpRRAEVLA---------------KTMVGQGk 152
Cdd:cd07140 34 ICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLME--EHQEELAtiesldsgavytlalKTHVGMS- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 153 tviqaeidaaaelIDFFRFNAKFAVELEGEQ-PIS-VPPSTNHTVYRGLE-GFVAAISPFNFTAIGGNLAGAPALM-GNV 228
Cdd:cd07140 111 -------------IQTFRYFAGWCDKIQGKTiPINqARPNRNLTLTKREPiGVCGIVIPWNYPLMMLAWKMAACLAaGNT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 229 VLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVA-QNLDRfrtf 307
Cdd:cd07140 178 VVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAvSNLKK---- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 308 prLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDP---AEDFG 384
Cdd:cd07140 254 --VSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPldrSTDHG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 385 TffsavidAKAFARIKKWLEHARSS--PSLSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKY 462
Cdd:cd07140 332 P-------QNHKAHLDKLVEYCERGvkEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDV 404
|
410 420
....*....|....*....|...
gi 568930882 463 RETLQLVDsTTSYGLTGAVFAQD 485
Cdd:cd07140 405 DGVLQRAN-DTEYGLASGVFTKD 426
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
98-485 |
3.10e-30 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 123.08 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 98 KALLNRAIDAALAA--RKEWDLKPMADRAQVFLKAADMLSGPRRAEVLAKTMvGQGKTV---IQAEIDAAAELIdffRFN 172
Cdd:PRK09847 56 SVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETL-DTGKPIrhsLRDDIPGAARAI---RWY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 173 AKFAVELEGEqpisVPPSTNHT---VYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRIL 248
Cdd:PRK09847 132 AEAIDKVYGE----VATTSSHElamIVREPVGVIAAIVPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 249 REAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNldrfrTFPRLAGECGGKNFHFVHSSA-D 327
Cdd:PRK09847 208 KEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS-----NMKRVWLEAGGKSANIVFADCpD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 328 VDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKAFARIKKWLEHAR 407
Cdd:PRK09847 283 LQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL-DPATTMGTLIDCAHADSVHSFIREGE 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930882 408 SSPSLsiLAGGQCNESVGyYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAVFAQD 485
Cdd:PRK09847 362 SKGQL--LLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEE--QALQLAND-SQYGLGAAVWTRD 433
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
93-491 |
1.15e-27 |
|
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: 115.63 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 93 FCYA---DKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSGPRRAEVLAKTmVGQGKTV---IQAEIDAAaelI 166
Cdd:cd07116 29 FCEVprsTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET-WDNGKPVretLAADIPLA---I 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 167 DFFRFNAKFAVELEGeqpiSVPPSTNHTV-YRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASY 242
Cdd:cd07116 105 DHFRYFAGCIRAQEG----SISEIDENTVaYHFHEplGVVGQIIPWNFPLLMATWKLAPALAaGNCVVLKPAEQTPASIL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 243 AVYRILREAgLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLdrfrtFPrLAGECGGKN---- 318
Cdd:cd07116 181 VLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI-----IP-VTLELGGKSpnif 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 319 FHFVHSSAD--VDSVVSGTLRSAFEYGgQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAKAF 396
Cdd:cd07116 254 FADVMDADDafFDKALEGFVMFALNQG-EVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL-DTETMIGAQASLEQL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 397 ARIKKWLEHARSSPSlSILAGGQCNES----VGYYVEPCIIEsKDPQEPIMKEEIFGPVLTVYVYPDdkYRETLQLVDST 472
Cdd:cd07116 332 EKILSYIDIGKEEGA-EVLTGGERNELggllGGGYYVPTTFK-GGNKMRIFQEEIFGPVLAVTTFKD--EEEALEIANDT 407
|
410
....*....|....*....
gi 568930882 473 TsYGLTGAVFAQDNHSVCR 491
Cdd:cd07116 408 L-YGLGAGVWTRDGNTAYR 425
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
103-484 |
4.40e-27 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 114.16 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 103 RAIDAALAARKEWDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKFAVELEGe 182
Cdd:PLN02315 60 EGLRACEEAAKIWMQVPAPKRGEIVRQIGDALR--AKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNG- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 183 qpiSVPPST--NHT---VYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRI----LREAG 252
Cdd:PLN02315 137 ---SIIPSErpNHMmmeVWNPL-GIVGVITAFNFpCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLvaevLEKNN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 253 LPPNIIQFVpADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNldrfrtFPRLAGECGGKNFHFVHSSADVDSVV 332
Cdd:PLN02315 213 LPGAIFTSF-CGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR------FGKCLLELSGNNAIIVMDDADIQLAV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 333 SGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAKAFARIKKWLEHARSSPSl 412
Cdd:PLN02315 286 RSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK-GTLLGPLHTPESKKNFEKGIEIIKSQGG- 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568930882 413 SILAGGQCNESVGYYVEPCIIESKdPQEPIMKEEIFGPVLtvYVYPDDKYRETLQLVDSTTSyGLTGAVFAQ 484
Cdd:PLN02315 364 KILTGGSAIESEGNFVQPTIVEIS-PDADVVKEELFGPVL--YVMKFKTLEEAIEINNSVPQ-GLSSSIFTR 431
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
90-485 |
4.79e-27 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 113.29 E-value: 4.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 90 VAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSGPRRAevLAKTMVGQ-GKTVIQAEIDAAaELIDF 168
Cdd:PRK09406 14 VKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQ--VAALMTLEmGKTLASAKAEAL-KCAKG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 169 FRFNAKFAVELEGEQPI---SVPPSTNHTVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWK-PSDTAMLASYa 243
Cdd:PRK09406 91 FRYYAEHAEALLADEPAdaaAVGASRAYVRYQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGNVGLLKhASNVPQTALY- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 244 VYRILREAGLPPNIIQ--FVPADGPtfgDTVTSSEHLCGINFTGSVPTfkhlWRQVAQnldrfrtfprLAG--------E 313
Cdd:PRK09406 169 LADLFRRAGFPDGCFQtlLVGSGAV---EAILRDPRVAAATLTGSEPA----GRAVAA----------IAGdeikktvlE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 314 CGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDA 393
Cdd:PRK09406 232 LGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDP-DTDVGPLATE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 394 KAFARIKKWLEHARSSPSlSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDdkYRETLQLVDSTT 473
Cdd:PRK09406 311 QGRDEVEKQVDDAVAAGA-TILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVAD--IDEAIEIANATT 387
|
410
....*....|..
gi 568930882 474 sYGLTGAVFAQD 485
Cdd:PRK09406 388 -FGLGSNAWTRD 398
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
101-485 |
8.38e-25 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 106.55 E-value: 8.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 101 LNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSgPRRAEVLAKTMVGQGKTVIQAEiDAAAeliDFFRFNAKFAVELE 180
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLA-AKSYDIAAGAVLVTGKGWMFAE-NICG---DQVQLRARAFVIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 181 GEQPISVPPSTNHTV------YRGLEGFVAAISPFNF--TAIGGNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAG 252
Cdd:cd07084 76 YRIPHEPGNHLGQGLkqqshgYRWPYGPVLVIGAFNFplWIPLLQLAGALA-MGNPVIVKPHTAVSIVMQIMVRLLHYAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 253 -LPPNIIQFVPADGPTfGDTVTSSEHLCGINFTGSVptfkhlwrQVAQNLDRFRTFPRLAGECGGKNFHFVHSSAD-VDS 330
Cdd:cd07084 155 lLPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSS--------RVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 331 VVSGTLRSAFEYGGQKCSACSRLYVPK--SLWPQIKgRLLEEHSRIKVGDpaedfgTFFSAVIDAKAFARIkkwlEHARS 408
Cdd:cd07084 226 VAWQCVQDMTACSGQKCTAQSMLFVPEnwSKTPLVE-KLKALLARRKLED------LLLGPVQTFTTLAMI----AHMEN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 409 SPSLSILAGGQ--CNESVGYYVEPCI-------IESKDPQEPIMKEEIFGPVLTVYVYPDDKYRETLQLVDSTTSYgLTG 479
Cdd:cd07084 295 LLGSVLLFSGKelKNHSIPSIYGACVasalfvpIDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGS-LTA 373
|
....*.
gi 568930882 480 AVFAQD 485
Cdd:cd07084 374 AIYSND 379
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
153-459 |
2.50e-24 |
|
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: 104.92 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 153 TVIQAEIDAAAELIDffRFNAKFAVELegeqPISVPPSTNHTVYRGLeGFVAAISPFNF---TAIGgNLAGAPAlMGNVV 229
Cdd:cd07087 61 AVVLGEIDHALKHLK--KWMKPRRVSV----PLLLQPAKAYVIPEPL-GVVLIIGPWNYplqLALA-PLIGAIA-AGNTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 230 LWKPSDTAMLASYAVYRILREAgLPPNIIQFVPADGPTfgdtvtsSEHLCG-----INFTGSVPTFKHLWRQVAQNLdrf 304
Cdd:cd07087 132 VLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEV-------ATALLAepfdhIFFTGSPAVGKIVMEAAAKHL--- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 305 rTFPRLagECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSlwpqIKGRLLEEHSR-IKV---GDPA 380
Cdd:cd07087 201 -TPVTL--ELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHES----IKDELIEELKKaIKEfygEDPK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 381 E--DFGtffsAVIDAKAFARIKKWLEHARsspslsILAGGQCNESvGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYP 458
Cdd:cd07087 274 EspDYG----RIINERHFDRLASLLDDGK------VVIGGQVDKE-ERYIAPTILDDVSPDSPLMQEEIFGPILPILTYD 342
|
.
gi 568930882 459 D 459
Cdd:cd07087 343 D 343
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
94-485 |
1.99e-22 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 100.22 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 94 CYADKalLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSGPRR--AEVLAKTMVGQGKTVIqAEIDAAAELIDFfrf 171
Cdd:PLN00412 50 CTQEE--VNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKApiAECLVKEIAKPAKDAV-TEVVRSGDLISY--- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 172 NAKFAVELEGEQPISVP---PSTNHTVY----RGLEGFVAAISPFNFTAiggNLAG---APALM-GNVVLWKPSDTAMLA 240
Cdd:PLN00412 124 TAEEGVRILGEGKFLVSdsfPGNERNKYcltsKIPLGVVLAIPPFNYPV---NLAVskiAPALIaGNAVVLKPPTQGAVA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 241 SYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSvptfkhlwrqvaqnlDRFRTFPRLAG------EC 314
Cdd:PLN00412 201 ALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG---------------DTGIAISKKAGmvplqmEL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 315 GGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfgTFFSAVIDAK 394
Cdd:PLN00412 266 GGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDD--CDITPVVSES 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 395 AFARIKKWLEHARSSpslsilAGGQCNE--SVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDSt 472
Cdd:PLN00412 344 SANFIEGLVMDAKEK------GATFCQEwkREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVE--EGIHHCNA- 414
|
410
....*....|...
gi 568930882 473 TSYGLTGAVFAQD 485
Cdd:PLN00412 415 SNFGLQGCVFTRD 427
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
81-485 |
7.26e-21 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 94.93 E-value: 7.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 81 LSPFNHA--------HKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQvflKAADMLSGPR-RAEVLAKTMVGQ- 150
Cdd:PRK13968 3 ITPATHAisvnpatgEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQ---KLRDIGKALRaRSEEMAQMITREm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 151 GKTVIQA--EIDAAAELIDFFrfnAKFAVELEGEQPISVPPSTNHTVYRGLeGFVAAISPFNFtAIGGNLAGA-PALM-G 226
Cdd:PRK13968 80 GKPINQAraEVAKSANLCDWY---AEHGPAMLKAEPTLVENQQAVIEYRPL-GTILAIMPWNF-PLWQVMRGAvPILLaG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 227 NVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEhLCGINFTGSVPTFKHLWRQVAQNLDRfrt 306
Cdd:PRK13968 155 NGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIGAQAGAALKK--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 307 fprLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDFGtf 386
Cdd:PRK13968 231 ---CVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEEN-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 387 fsaviDAKAFARIKKWLE-HARSSPSLS----ILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDK 461
Cdd:PRK13968 306 -----ALGPMARFDLRDElHHQVEATLAegarLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAE 380
|
410 420
....*....|....*....|....
gi 568930882 462 YreTLQLVDStTSYGLTGAVFAQD 485
Cdd:PRK13968 381 H--ALELAND-SEFGLSATIFTTD 401
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
182-487 |
2.77e-20 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 93.55 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 182 EQPISVPPSTNHTVYRGLeGFVAAISPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAgLPPNII 258
Cdd:PTZ00381 93 DTVGVFGPGKSYIIPEPL-GVVLVIGAWNYplnLTLI-PLAGAIA-AGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 259 QFVPADgptfgdtVTSSEHLCG-----INFTGSVPTFKHLWRQVAQNLdrfrTFPRLagECGGKNFHFVHSSADVDSVVS 333
Cdd:PTZ00381 169 RVIEGG-------VEVTTELLKepfdhIFFTGSPRVGKLVMQAAAENL----TPCTL--ELGGKSPVIVDKSCNLKVAAR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 334 GTLRSAFEYGGQKCSACSRLYVPKSlwpqIKGRLLEE--HSRIKV--GDP--AEDFgtffSAVIDAKAFARIKKWLEHAR 407
Cdd:PTZ00381 236 RIAWGKFLNAGQTCVAPDYVLVHRS----IKDKFIEAlkEAIKEFfgEDPkkSEDY----SRIVNEFHTKRLAELIKDHG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 408 SSpslsILAGGQCNESvGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKyrETLQLVDStTSYGLTGAVFAQDNH 487
Cdd:PTZ00381 308 GK----VVYGGEVDIE-NKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENID--EVLEFINS-RPKPLALYYFGEDKR 379
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
201-459 |
2.84e-20 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 93.06 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 201 GFVAAISPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAglppniiqFVPADGPTF-GDTVTSSE 276
Cdd:cd07134 102 GVCLIISPWNYpfnLAFG-PLVSAIA-AGNTAILKPSELTPHTSAVIAKIIREA--------FDEDEVAVFeGDAEVAQA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 277 -------HlcgINFTGSVPTFKHLWRQVAQNLdrfrTFPRLagECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSA 349
Cdd:cd07134 172 llelpfdH---IFFTGSPAVGKIVMAAAAKHL----ASVTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 350 CSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKAFARIKKWLEHARSSPSlSILAGGQCNESvGYYVE 429
Cdd:cd07134 243 PDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGA-KVEFGGQFDAA-QRYIA 320
|
250 260 270
....*....|....*....|....*....|
gi 568930882 430 PCIIESKDPQEPIMKEEIFGPVLTVYVYPD 459
Cdd:cd07134 321 PTVLTNVTPDMKIMQEEIFGPVLPIITYED 350
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
201-489 |
3.10e-20 |
|
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: 93.05 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 201 GFVAAISPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAgLPPNIIQFVPADGPTFGDTVTSS-E 276
Cdd:cd07135 110 GVVLIIGPWNYpvlLALS-PLVGAIA-AGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQKfD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 277 HlcgINFTGSVPTFKHLWRQVAQNLDrfrtfPrLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVP 356
Cdd:cd07135 187 K---IFYTGSGRVGRIIAEAAAKHLT-----P-VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 357 KSLWPQIKGRLLEEHSRIKVGDPAEDfgTFFSAVIDAKAFARIKKWLEHARSSpslsILAGGQCNESVgYYVEPCIIESK 436
Cdd:cd07135 258 PSVYDEFVEELKKVLDEFYPGGANAS--PDYTRIVNPRHFNRLKSLLDTTKGK----VVIGGEMDEAT-RFIPPTIVSDV 330
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568930882 437 DPQEPIMKEEIFGPVLTVYVYPDDkyRETLQLVDS--TTsygLTGAVFAQDNHSV 489
Cdd:cd07135 331 SWDDSLMSEELFGPVLPIIKVDDL--DEAIKVINSrdTP---LALYIFTDDKSEI 380
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
102-482 |
9.90e-20 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 92.12 E-value: 9.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 102 NRAIDAALAARKE----WDLKPMADRAQVFLKAADMLSgpRRAEVLAKTMVG-QGKTVIQAEIDAAAELiDFFRFNAKFA 176
Cdd:PLN02419 150 NEEFKAAVSAAKQafplWRNTPITTRQRVMLKFQELIR--KNMDKLAMNITTeQGKTLKDSHGDIFRGL-EVVEHACGMA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 177 VELEGEQPISVPPSTNHTVYRGLEGFVAAISPFNFTAIggnlagAPALM-------GNVVLWKPSDTAMLASYAVYRILR 249
Cdd:PLN02419 227 TLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAM------IPLWMfpvavtcGNTFILKPSEKDPGASVILAELAM 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 250 EAGLPPNIIQFVPADGPTFgDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFRTfprlagECGGKNFHFVHSSADVD 329
Cdd:PLN02419 301 EAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQS------NMGAKNHGLVLPDANID 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 330 SVVSGTLRSAFEYGGQKCSACSRLYV---PKSlWpqiKGRLLEEHSRIKV---GDPAEDFGtffsAVIDAKAFARIKKWL 403
Cdd:PLN02419 374 ATLNALLAAGFGAAGQRCMALSTVVFvgdAKS-W---EDKLVERAKALKVtcgSEPDADLG----PVISKQAKERICRLI 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 404 EHARSSPSLSILAGGQC---NESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTvyVYPDDKYRETLQLVDStTSYGLTGA 480
Cdd:PLN02419 446 QSGVDDGAKLLLDGRDIvvpGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLV--CMQANSFDEAISIINK-NKYGNGAA 522
|
..
gi 568930882 481 VF 482
Cdd:PLN02419 523 IF 524
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
201-457 |
2.26e-18 |
|
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: 87.17 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 201 GFVAAISPFN--FTAIGGNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAgLPPNIIQFVPadgptfGDTVTSSEHL 278
Cdd:cd07136 102 GVVLIIAPWNypFQLALAPLIGAIA-AGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVE------GGVEENQELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 279 CG----INFTGSVPTFKHLWRQVAQNLdrfrTFPRLagECGGKNFHFVHSSADVD----SVVSGTLRSAfeygGQKCSAC 350
Cdd:cd07136 174 DQkfdyIFFTGSVRVGKIVMEAAAKHL----TPVTL--ELGGKSPCIVDEDANLKlaakRIVWGKFLNA----GQTCVAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 351 SRLYVPKSlwpqIKGRLLEE---HSRIKVGDPA---EDFGTffsaVIDAKAFARIKKWLEHARsspslsILAGGQCNESv 424
Cdd:cd07136 244 DYVLVHES----VKEKFIKElkeEIKKFYGEDPlesPDYGR----IINEKHFDRLAGLLDNGK------IVFGGNTDRE- 308
|
250 260 270
....*....|....*....|....*....|...
gi 568930882 425 GYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVY 457
Cdd:cd07136 309 TLYIEPTILDNVTWDDPVMQEEIFGPILPVLTY 341
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
199-459 |
5.13e-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: 71.15 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 199 LEGFVAAISPFNFTAIGGNLAGAPALMGNV-VLWKP-SDTAMLAsYAVYRILREAG-LPPNIIQFVPADGPTFGDTVTSS 275
Cdd:cd07128 144 RRGVAVHINAFNFPVWGMLEKFAPALLAGVpVIVKPaTATAYLT-EAVVKDIVESGlLPEGALQLICGSVGDLLDHLGEQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 276 EHlcgINFTGSVPTFKHLwrqvaqnldrfRTFPRLAGEcgGKNFhfvhsSADVDSV-------------------VSGTL 336
Cdd:cd07128 223 DV---VAFTGSAATAAKL-----------RAHPNIVAR--SIRF-----NAEADSLnaailgpdatpgtpefdlfVKEVA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 337 RSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAED---FGTFFSAVIDAKAFARIKKWLEHA---RSSP 410
Cdd:cd07128 282 REMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEgvrMGPLVSREQREDVRAAVATLLAEAevvFGGP 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568930882 411 SLSILAGGQCNEsvGYYVEPCIIESKDPQEP--IMKEEIFGPVLTVYVYPD 459
Cdd:cd07128 362 DRFEVVGADAEK--GAFFPPTLLLCDDPDAAtaVHDVEAFGPVATLMPYDS 410
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
189-478 |
9.39e-13 |
|
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: 69.82 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 189 PSTNHTVYRGLeGFVAAISPFNF---TAIGGnLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAgLPPNIIQFV---P 262
Cdd:cd07133 92 PAKAEVEYQPL-GVVGIIVPWNYplyLALGP-LIAALA-AGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVtggA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 263 ADGPTFgdtvtSS---EHLCginFTGSVPTFKHLWRQVAQNLdrfrTFPRLagECGGKNFHFVHSSADVDSVVSGTLRSA 339
Cdd:cd07133 168 DVAAAF-----SSlpfDHLL---FTGSTAVGRHVMRAAAENL----TPVTL--ELGGKSPAIIAPDADLAKAAERIAFGK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 340 FEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIkvgdpaedFGTF-----FSAVIDAKAFARIKKWLEHARS--SPSL 412
Cdd:cd07133 234 LLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM--------YPTLadnpdYTSIINERHYARLQGLLEDARAkgARVI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 413 SILAGGQCNESVGYYVePCIIESKDPQEPIMKEEIFGPVLTV----------------------YVYPDDKyRETLQLVD 470
Cdd:cd07133 306 ELNPAGEDFAATRKLP-PTLVLNVTDDMRVMQEEIFGPILPIltydsldeaidyinarprplalYYFGEDK-AEQDRVLR 383
|
....*...
gi 568930882 471 STTSYGLT 478
Cdd:cd07133 384 RTHSGGVT 391
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
313-452 |
3.44e-12 |
|
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: 68.02 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 313 ECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSA-----CSrlyvpkslwPQIKGRLLEE-HSRIKV---GDPAE-- 381
Cdd:cd07132 206 ELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdyvlCT---------PEVQEKFVEAlKKTLKEfygEDPKEsp 276
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568930882 382 DFGTffsaVIDAKAFARIKKWLEharsspSLSILAGGQCNESvGYYVEPCIIESKDPQEPIMKEEIFGPVL 452
Cdd:cd07132 277 DYGR----IINDRHFQRLKKLLS------GGKVAIGGQTDEK-ERYIAPTVLTDVKPSDPVMQEEIFGPIL 336
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
197-459 |
1.52e-11 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 66.27 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 197 RGLEGFVAAispFNFTAIGGNLAGAPALMGNV-VLWKP-SDTAMLASYAVyRILREAG-LPPNIIQFV---PAD-----G 265
Cdd:PRK11903 149 RGVALFINA---FNFPAWGLWEKAAPALLAGVpVIVKPaTATAWLTQRMV-KDVVAAGiLPAGALSVVcgsSAGlldhlQ 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 266 PtfGDTVTssehlcginFTGSvptfkhlwrqvAQNLDRFRTFPRLAGecggknfHFVHSSADVDSVVSGTL-------RS 338
Cdd:PRK11903 225 P--FDVVS---------FTGS-----------AETAAVLRSHPAVVQ-------RSVRVNVEADSLNSALLgpdaapgSE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 339 AFEY------------GGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAED---FGTFFSAVIDAKAFARIKKWL 403
Cdd:PRK11903 276 AFDLfvkevvremtvkSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDgvrMGPLVSRAQLAAVRAGLAALR 355
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568930882 404 EHArsspslSILAGGQCNE------SVGYYVEPCIIESKDPQEP--IMKEEIFGPVLTVYVYPD 459
Cdd:PRK11903 356 AQA------EVLFDGGGFAlvdadpAVAACVGPTLLGASDPDAAtaVHDVEVFGPVATLLPYRD 413
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
126-487 |
1.45e-09 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 60.20 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 126 VFLKAADMLSGPRRAEVLAKTMvgqGKTVIQAEIDAAAELIDFFRFNAKFAveleGEQP------ISVPpsTNH-----T 194
Cdd:cd07126 67 VSHRVAHELRKPEVEDFFARLI---QRVAPKSDAQALGEVVVTRKFLENFA----GDQVrflarsFNVP--GDHqgqqsS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 195 VYRGLEGFVAAISPFNFT----AIggNLAGApALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGD 270
Cdd:cd07126 138 GYRWPYGPVAIITPFNFPleipAL--QLMGA-LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 271 TVTSSEHLCgINFTGSvptfkhlwRQVAQNLDRfRTFPRLAGECGGKNFHFVHSS-ADVDSVVSGTLRSAFEYGGQKCSA 349
Cdd:cd07126 215 ILLEANPRM-TLFTGS--------SKVAERLAL-ELHGKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 350 CSRLYVPKSlWPQ--IKGRLLEEHSRIKVGD----PAEDFGTffsavidakafARIKKWLEHARSSPSLSILAGG----- 418
Cdd:cd07126 285 QSILFAHEN-WVQagILDKLKALAEQRKLEDltigPVLTWTT-----------ERILDHVDKLLAIPGAKVLFGGkpltn 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568930882 419 QCNESVGYYVEPCII-----ESKDPQE-PIMKEEIFGPVLTVYVYPDDKYRETLQLVDSTTSYgLTGAVFAQDNH 487
Cdd:cd07126 353 HSIPSIYGAYEPTAVfvpleEIAIEENfELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAH-LTAAVVSNDIR 426
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
184-478 |
4.39e-09 |
|
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: 58.58 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 184 PISVPPSTNHTVYRGLeGFVAAISPFNFtAIGGNL---AGAPAlMGNVVLWKPSDTAMLASYAVYRILrEAGLPPNIIQF 260
Cdd:cd07137 87 PLTTFPAKAEIVSEPL-GVVLVISAWNF-PFLLSLepvIGAIA-AGNAVVLKPSELAPATSALLAKLI-PEYLDTKAIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 261 VPAdgptfgdTVTSSEHLC-----GINFTGSVPTFKHLWRQVAQNLDrfrtfPrLAGECGGKNFHFVHSSADVDSVVSGT 335
Cdd:cd07137 163 IEG-------GVPETTALLeqkwdKIFFTGSPRVGRIIMAAAAKHLT-----P-VTLELGGKCPVIVDSTVDLKVAVRRI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 336 LrsAFEYG---GQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDfgTFFSAVIDAKAFARIKKWLEHarSSPSL 412
Cdd:cd07137 230 A--GGKWGcnnGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKES--KDLSRIVNSHHFQRLSRLLDD--PSVAD 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 413 SILAGGQCNESvGYYVEPCIIESKDPQEPIMKEEIFGPVLT----------------------VYVYPDDKYRETlQLVD 470
Cdd:cd07137 304 KIVHGGERDEK-NLYIEPTILLDPPLDSSIMTEEIFGPLLPiitvkkieesieiinsrpkplaAYVFTKNKELKR-RIVA 381
|
....*...
gi 568930882 471 STTSYGLT 478
Cdd:cd07137 382 ETSSGGVT 389
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
174-452 |
4.08e-06 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 49.34 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 174 KFAVELEGEQPISVPPSTNHTVYRGLeGFVAAISPFNFtAIGGNL---AGAPAlMGNVVLWKPSDtamlasyavyrilre 250
Cdd:PLN02203 84 KWMAPKKAKLPLVAFPATAEVVPEPL-GVVLIFSSWNF-PIGLSLeplIGAIA-AGNAVVLKPSE--------------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 251 agLPPNIIQFVPADGPTFGDT---------VTSSEHLC-----GINFTGSVPTFKHLWRQVAQNLDrfrtfPrLAGECGG 316
Cdd:PLN02203 146 --LAPATSAFLAANIPKYLDSkavkvieggPAVGEQLLqhkwdKIFFTGSPRVGRIIMTAAAKHLT-----P-VALELGG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 317 KN---FHFVHSSADVDSVVSGTLRSAFEY-GGQKCSACSRLYVPKSLWPqIKGRLLEEHSRIKVGDPAEDFGTFfSAVID 392
Cdd:PLN02203 218 KCpciVDSLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAP-ILIELLKSTIKKFFGENPRESKSM-ARILN 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 393 AKAFARIKKWLEHARSSPSlsILAGGQCNESvGYYVEPCIIESKDPQEPIMKEEIFGPVL 452
Cdd:PLN02203 296 KKHFQRLSNLLKDPRVAAS--IVHGGSIDEK-KLFIEPTILLNPPLDSDIMTEEIFGPLL 352
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
191-357 |
7.24e-04 |
|
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: 42.08 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 191 TNHTVYRGLeGFVAAISPF----NFTAIGGNLAgapalMGNVVLWKPSDTAMLASYAVYRILR----EAGLPPNIIQFVp 262
Cdd:cd07127 188 TFTVVPRGV-ALVIGCSTFptwnGYPGLFASLA-----TGNPVIVKPHPAAILPLAITVQVARevlaEAGFDPNLVTLA- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 263 ADGPTFGDTVTSSEH--LCGINFTGSVPTFKHLWRQVAQNLdrfrtfprLAGECGGKNFHFVHSSADVDSVVSGTLRSAF 340
Cdd:cd07127 261 ADTPEEPIAQTLATRpeVRIIDFTGSNAFGDWLEANARQAQ--------VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLS 332
|
170
....*....|....*..
gi 568930882 341 EYGGQKCSACSRLYVPK 357
Cdd:cd07127 333 LYSGQMCTTPQNIYVPR 349
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
226-454 |
1.20e-03 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 41.18 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 226 GNVVLWKPSDTAMlASYAVYRILREAGLPPNIIQFVpaDGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRfr 305
Cdd:PLN02174 140 GNAVVLKPSELAP-ASSALLAKLLEQYLDSSAVRVV--EGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTP-- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930882 306 tfprLAGECGGKNFHFVHSSADVDSVVSGTLrsAFEYG---GQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAED 382
Cdd:PLN02174 215 ----VVLELGGKSPVVVDSDTDLKVTVRRII--AGKWGcnnGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMES 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568930882 383 fgTFFSAVIDAKAFARIKKWLEHARSSPSlsILAGGQcNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTV 454
Cdd:PLN02174 289 --KDMSRIVNSTHFDRLSKLLDEKEVSDK--IVYGGE-KDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPI 355
|
|
| |
