|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
45-497 |
0e+00 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 670.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 45 LNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERMRTVNQLKAFASALRENpeS 124
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREG--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 125 PLGLkVVDEADVTRAPLPKPHTELNYLPLGPVAVFGASNFPYAFSTLGGDTAAALAAGCPVIVKNHTAHPGTGELMARAA 204
Cdd:cd07129 79 WLDA-RIDPADPDRQPLPRPDLRRMLVPLGPVAVFGASNFPLAFSVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 205 LAAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIPFYGELGSINPQVILPNKAI 284
Cdd:cd07129 158 RAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEPIPFYAELGSVNPVFILPGALA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 285 EQSKEMAQSLCQSMLMGNGQFCTSPGLWLVPTG--CDELEAHITACINDAPSDTLLTPGIVKTFKQQVEER-SQFAQLSV 361
Cdd:cd07129 238 ERGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAGpaGDAFIAALAEALAAAPAQTMLTPGIAEAYRQGVEALaAAPGVRVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 362 LGKGKLEQAFHANAHVFACNADDYLTTPTLHEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGTEADLNKADSVIE 441
Cdd:cd07129 318 AGGAAAEGGNQAAPTLFKVDAAAFLADPALQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHGEEDDLALARELLP 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1887644984 442 ALQYKVGRLIKNQMPTGVEVCGSMNHGGPFPSSTDVRSTSVGTNAMLRFMRPICYQ 497
Cdd:cd07129 398 VLERKAGRLLFNGWPTGVEVCPAMVHGGPYPATTDPRFTSVGTAAIERFLRPVCYQ 453
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
45-498 |
3.03e-66 |
|
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: 220.19 E-value: 3.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 45 LNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPlARLQGERMRTVNQLKAFASALRenpes 124
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG-WMFAENICGDQVQLRARAFVIY----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 125 plGLKVVDEADVTRAPLPKPHTELNYLPLGPVAVFGASNFPyaFSTLGGDTAAALAAGCPVIVKNHTAHPGTGELMARAA 204
Cdd:cd07084 75 --SYRIPHEPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFP--LWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 205 LAAIKecaMPLGVFAMVQSKAYdISHQLVAAPGIKAVGFTGSFNVASKLQETIAKreepIPFYGELGSINPQVILPNkaI 284
Cdd:cd07084 151 HYAGL---LPPEDVTLINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALDAKQ----ARIYLELAGFNWKVLGPD--A 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 285 EQSKEMAQSLCQSMLMGNGQFCTSPGLWLVPTGcDELEAHITACINDA----PSDTLLTPGIVKTFKQQVEERSQFAQLS 360
Cdd:cd07084 221 QAVDYVAWQCVQDMTACSGQKCTAQSMLFVPEN-WSKTPLVEKLKALLarrkLEDLLLGPVQTFTTLAMIAHMENLLGSV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 361 VLGKGKLEQAFHANA--------HVFACNADDYLTTPTLHEEVFGPAALVVRY--DSEQQLMILINKLQGQLTASVHGTE 430
Cdd:cd07084 300 LLFSGKELKNHSIPSiygacvasALFVPIDEILKTYELVTEEIFGPFAIVVEYkkDQLALVLELLERMHGSLTAAIYSND 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 431 ADLnkADSVIEALQyKVGRLIK-NQMPTGVEVcgSMNHGGPFPSSTdvRSTSVGT-NAMLRFMRPICYQA 498
Cdd:cd07084 380 PIF--LQELIGNLW-VAGRTYAiLRGRTGVAP--NQNHGGGPAADP--RGAGIGGpEAIKLVWRCHAEQA 442
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
48-469 |
1.50e-57 |
|
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: 197.05 E-value: 1.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 48 AIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERMRTVNQLKAFASALRENpesplg 127
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 128 lkvvdEADVTRAPLPKPHTELNYLPLGPVAVFGASNFPyaFSTLGGDTAAALAAGCPVIVKNHTAHPGTGELMARAalaa 207
Cdd:cd07078 77 -----HGEVIPSPDPGELAIVRREPLGVVGAITPWNFP--LLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAEL---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 208 IKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKReePIPFYGELGSINPQVILPNKAIEQs 287
Cdd:cd07078 146 LAEAGLPPGVLNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAEN--LKRVTLELGGKSPLIVFDDADLDA- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 288 keMAQSLCQSMLMGNGQFCTSPGLWLVPTGC-DELEAHITACI------NDAPSDTLLTPGI----VKTFKQQVEE-RSQ 355
Cdd:cd07078 223 --AVKGAVFGAFGNAGQVCTAASRLLVHESIyDEFVERLVERVkalkvgNPLDPDTDMGPLIsaaqLDRVLAYIEDaKAE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 356 FAQLSVLGK--GKLEQAFHAnAHVFACNADDyltTPTLHEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGTeaDL 433
Cdd:cd07078 301 GAKLLCGGKrlEGGKGYFVP-PTVLTDVDPD---MPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTR--DL 374
|
410 420 430
....*....|....*....|....*....|....*.
gi 1887644984 434 NKADSVIEALQykVGRLIKNQMPTGVEvcGSMNHGG 469
Cdd:cd07078 375 ERALRVAERLE--AGTVWINDYSVGAE--PSAPFGG 406
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-469 |
1.57e-52 |
|
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: 184.56 E-value: 1.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 1 MTL-TGQSLVAGQWIGDSANGEFHAFSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQIL 79
Cdd:COG1012 1 MTTpEYPLFIGGEWVAAASGETFDVINPATGEVL-ARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 80 VLGDELIEQTQQETNLPLARLQGERMRTVNQLKAFASALRENpesplglkvvdEADVTRAPLPKPHTELNYLPLGPVAVF 159
Cdd:COG1012 80 ERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRL-----------YGETIPSDAPGTRAYVRREPLGVVGAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 160 GASNFPyaFSTLGGDTAAALAAGCPVIVKNHTAHPGTGELMARaalaAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIK 239
Cdd:COG1012 149 TPWNFP--LALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAE----LLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 240 AVGFTGSFNVASKLQETIAKReePIPFYGELGSINPQVILPNKAIEQskeMAQSLCQSMLMGNGQFCTSPGLWLVPTGC- 318
Cdd:COG1012 223 KISFTGSTAVGRRIAAAAAEN--LKRVTLELGGKNPAIVLDDADLDA---AVEAAVRGAFGNAGQRCTAASRLLVHESIy 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 319 DELEAHITACIND----APSDT------LLTPGIVKTFKQQVEE-RSQFAQLsVLGKGKLEqafhanahvfacNADDYLT 387
Cdd:COG1012 298 DEFVERLVAAAKAlkvgDPLDPgtdmgpLISEAQLERVLAYIEDaVAEGAEL-LTGGRRPD------------GEGGYFV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 388 TPTL-----------HEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGTeaDLNKADSVIEALQykVGRLIKNQMP 456
Cdd:COG1012 365 EPTVladvtpdmriaREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTR--DLARARRVARRLE--AGMVWINDGT 440
|
490
....*....|...
gi 1887644984 457 TGVEvcGSMNHGG 469
Cdd:COG1012 441 TGAV--PQAPFGG 451
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
50-489 |
1.94e-52 |
|
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: 181.66 E-value: 1.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 50 EAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERMRTVNQLKAFASALRENPEsplglk 129
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGG------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 130 vvdeaDVTRAPLPKPHTELNYLPLGPVAVFGASNFPyaFSTLGGDTAAALAAGCPVIVKNHTAHPGTGELMARaalaAIK 209
Cdd:cd06534 75 -----PELPSPDPGGEAYVRREPLGVVGVITPWNFP--LLLAAWKLAPALAAGNTVVLKPSELTPLTALALAE----LLQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 210 ECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKReePIPFYGELGSINPQVILPNKAIEQske 289
Cdd:cd06534 144 EAGLPPGVVNVVPGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAEN--LKPVTLELGGKSPVIVDEDADLDA--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 290 MAQSLCQSMLMGNGQFCTSPGLWLVPTGC-DELEAHITacindapsdTLLTPgivktfkqqVEERSQFAqlsvlgkgkle 368
Cdd:cd06534 219 AVEGAVFGAFFNAGQICTAASRLLVHESIyDEFVEKLV---------TVLVD---------VDPDMPIA----------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 369 qafhanahvfacnaddylttptlHEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGTeaDLNKADSVIEALQykVG 448
Cdd:cd06534 270 -----------------------QEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTR--DLNRALRVAERLR--AG 322
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1887644984 449 RLIKNQMPTGVEVcgSMNHGGPFPSSTDVRSTSVGTNAMLR 489
Cdd:cd06534 323 TVYINDSSIGVGP--EAPFGGVKNSGIGREGGPYGLEEYTR 361
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
13-469 |
2.03e-46 |
|
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: 167.71 E-value: 2.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 13 WIgDSANGEFHAFSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQE 92
Cdd:pfam00171 1 WV-DSESETIEVINPATGEVI-ATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 93 TNLPLARLQGERMRTVNQLKAFASALRE-NPESplglkvvdeadvtrapLPKPHTELNYL---PLGPVAVFGASNFPyaF 168
Cdd:pfam00171 79 NGKPLAEARGEVDRAIDVLRYYAGLARRlDGET----------------LPSDPGRLAYTrrePLGVVGAITPWNFP--L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 169 STLGGDTAAALAAGCPVIVKNHTAHPGTGELMARAalaaIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFN 248
Cdd:pfam00171 141 LLPAWKIAPALAAGNTVVLKPSELTPLTALLLAEL----FEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 249 VASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQskeMAQSLCQSMLMGNGQFCTSPGLWLVPTGC-DELEAHITA 327
Cdd:pfam00171 217 VGRHIAEAAAQNLKRVTL--ELGGKNPLIVLEDADLDA---AVEAAVFGAFGNAGQVCTATSRLLVHESIyDEFVEKLVE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 328 CI------NDAPSDTLLTPGI----VKTFKQQVEE-RSQFAQLSVLGKGKLEQAFHANAHVFA-CNADDYLttptLHEEV 395
Cdd:pfam00171 292 AAkklkvgDPLDPDTDMGPLIskaqLERVLKYVEDaKEEGAKLLTGGEAGLDNGYFVEPTVLAnVTPDMRI----AQEEI 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887644984 396 FGPAALVVRYDSEQQLMILINKLQGQLTASVHGTeaDLNKADSVIEALQykVGRLIKNQMPTGVEVcgSMNHGG 469
Cdd:pfam00171 368 FGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTS--DLERALRVARRLE--AGMVWINDYTTGDAD--GLPFGG 435
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
7-460 |
2.41e-31 |
|
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: 126.21 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 7 SLVAGQWIGDSANGEfhAFSPARNEALPTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELI 86
Cdd:cd07097 3 NYIDGEWVAGGDGEE--NRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 87 EQTQQETNLPLARLQGERMRTVNQLKAFAS-ALRenpespLGLKVVDEADvtraplpkPHTELNYL--PLGPVAVFGASN 163
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGeALR------LSGETLPSTR--------PGVEVETTrePLGVVGLITPWN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 164 FPyaFSTLGGDTAAALAAGCPVIVKNHTAHPGTGelmarAALA-AIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVG 242
Cdd:cd07097 147 FP--IAIPAWKIAPALAYGNTVVFKPAELTPASA-----WALVeILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 243 FTGSFNVASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQSKEMAqslCQSMLMGNGQFCTspglwlvptgcdele 322
Cdd:cd07097 220 FTGSTAVGRRIAAAAAARGARVQL--EMGGKNPLVVLDDADLDLAVECA---VQGAFFSTGQRCT--------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 323 ahitacindAPSDTLLTPGIVKTFKQQVEER----------------------SQFAQ-LSVLGKGKLEQAFHA-NAHVF 378
Cdd:cd07097 280 ---------ASSRLIVTEGIHDRFVEALVERtkalkvgdaldegvdigpvvseRQLEKdLRYIEIARSEGAKLVyGGERL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 379 ACNADDYLTTPTL-----------HEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGTeaDLNKADSVIEALQykV 447
Cdd:cd07097 351 KRPDEGYYLAPALfagvtndmriaREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTT--SLKHATHFKRRVE--A 426
|
490
....*....|....
gi 1887644984 448 GrLIKNQMPT-GVE 460
Cdd:cd07097 427 G-VVMVNLPTaGVD 439
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
25-445 |
4.55e-29 |
|
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: 119.07 E-value: 4.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 25 FSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGER 104
Cdd:cd07103 2 INPATGEVI-GEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 105 MRTVNQLKAFAsalrenpesplglkvvDEA-----DVTRAPLPKPHTELNYLPLGPVAVFGASNFPYAFST--LggdtAA 177
Cdd:cd07103 81 DYAASFLEWFA----------------EEArriygRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITrkI----AP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 178 ALAAGCPVIVKNHTAHPGTGELMARAALaaikECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETI 257
Cdd:cd07103 141 ALAAGCTVVLKPAEETPLSALALAELAE----EAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 258 AKREEPIPFygELGSINPQVILPNKAIEQSkemAQSLCQSMLMGNGQFCTSPGLWLVPTGC-DELEAHITACI------N 330
Cdd:cd07103 217 ADTVKRVSL--ELGGNAPFIVFDDADLDKA---VDGAIASKFRNAGQTCVCANRIYVHESIyDEFVEKLVERVkklkvgN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 331 DAPSDTLLTPGI----VKTFKQQVEE-RSQFAQLsVLGKGKLEQA--FHAnahvfacnaddylttPTL-----------H 392
Cdd:cd07103 292 GLDEGTDMGPLIneraVEKVEALVEDaVAKGAKV-LTGGKRLGLGgyFYE---------------PTVltdvtddmlimN 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1887644984 393 EEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGTeaDLNKADSVIEALQY 445
Cdd:cd07103 356 EETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTR--DLARAWRVAEALEA 406
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
7-448 |
1.71e-28 |
|
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: 117.83 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 7 SLVAGQWIGDSANGEFHAFSPARNEALPTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELI 86
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 87 EQTQQETNLPLARLQGERMRTVNQLKAFASALREnpesPLGlkvvdeaDVTRAPLPKPHTELNYLPLGPVAVFGASNFPY 166
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRR----LFG-------ETVPSELPNKDAMTRRQPIGVVALITPWNFPV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 167 AFStlGGDTAAALAAGCPVIVKNHTAHPGTGELMARAALAAikecAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGS 246
Cdd:cd07131 150 AIP--SWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEA----GLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 247 FNVASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQSKEMAqslcqsmLMG----NGQFCTSPGLWLVPTGC-DEL 321
Cdd:cd07131 224 TEVGERIGETCARPNKRVAL--EMGGKNPIIVMDDADLDLALEGA-------LWSafgtTGQRCTATSRLIVHESVyDEF 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 322 EAHITACINDAP------SDTLLTPGIVKTFKQQVEERSQFAQL---------SVLGKGKLEQAFHANAHVFacnADDYL 386
Cdd:cd07131 295 LKRFVERAKRLRvgdgldEETDMGPLINEAQLEKVLNYNEIGKEegatlllggERLTGGGYEKGYFVEPTVF---TDVTP 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1887644984 387 TTPTLHEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHgTEaDLNKADSVIEALQYKVG 448
Cdd:cd07131 372 DMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIY-TE-DVNKAFRARRDLEAGIT 431
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
9-445 |
4.33e-28 |
|
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: 116.60 E-value: 4.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 9 VAGQWIGDSANGEFHAFSPArNEALPTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQ 88
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPA-TGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 89 TQQETNLPLARLQGERMRTVNQLKAFASALRenpesplglkvVDEADVTRAPLPKPHTELNYLPLGPVAVFGASNFPyaF 168
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWAR-----------RIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFP--F 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 169 STLGGDTAAALAAGCPVIVKNHTAHPGTGELMARAALAAikecAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFN 248
Cdd:cd07088 148 FLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEA----GLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 249 VASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQSkemAQSLCQSMLMGNGQFCTSPGLWLV-----PTGCDELEA 323
Cdd:cd07088 224 AGQKIMEAAAENITKVSL--ELGGKAPAIVMKDADLDLA---VKAIVDSRIINCGQVCTCAERVYVhediyDEFMEKLVE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 324 HITA--CINDAPSDTLLTPGIVKTFKQQVEERSQFAQLS----VLGKGKLEQafhANAHVFAcnaddylttPTL------ 391
Cdd:cd07088 299 KMKAvkVGDPFDAATDMGPLVNEAALDKVEEMVERAVEAgatlLTGGKRPEG---EKGYFYE---------PTVltnvrq 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1887644984 392 -----HEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHgTEaDLNKADSVIEALQY 445
Cdd:cd07088 367 dmeivQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIY-TE-NLNTAMRATNELEF 423
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
6-445 |
2.85e-27 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 114.40 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 6 QSLVAGQWIGDSANGEFHAFSPARNEALPTRFFnLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDEL 85
Cdd:PLN02278 26 QGLIGGKWTDAYDGKTFPVYNPATGEVIANVPC-MGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 86 IEQTQQETNLPLARLQGERMRTVNQLKAFAS-ALRENpesplglkvvdeADVTRAPLPKPHTELNYLPLGPVAVFGASNF 164
Cdd:PLN02278 105 AQLMTLEQGKPLKEAIGEVAYGASFLEYFAEeAKRVY------------GDIIPSPFPDRRLLVLKQPVGVVGAITPWNF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 165 PYAFSTlgGDTAAALAAGCPVIVKNHTAHPGTGelMARAALAaiKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFT 244
Cdd:PLN02278 173 PLAMIT--RKVGPALAAGCTVVVKPSELTPLTA--LAAAELA--LQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 245 GSFNVASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQSkemAQSLCQSMLMGNGQFCTSPGLWLVPTGC-DELEA 323
Cdd:PLN02278 247 GSTAVGKKLMAGAAATVKRVSL--ELGGNAPFIVFDDADLDVA---VKGALASKFRNSGQTCVCANRILVQEGIyDKFAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 324 HITACIN----------DAPSDTLLTPGIVKTFKQQVEER-SQFAQLSVLGK-GKLEQAFHANAHVFACNADDYLttptL 391
Cdd:PLN02278 322 AFSKAVQklvvgdgfeeGVTQGPLINEAAVQKVESHVQDAvSKGAKVLLGGKrHSLGGTFYEPTVLGDVTEDMLI----F 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1887644984 392 HEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHgTEaDLNKADSVIEALQY 445
Cdd:PLN02278 398 REEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIF-TR-DLQRAWRVSEALEY 449
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
41-444 |
1.75e-26 |
|
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: 111.47 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 41 STAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERMRTVNQLKAFASaLRE 120
Cdd:cd07106 17 SEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTAS-LDL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 121 NPEsplglkVVDEADVTRaplpkphTELNYLPLGPVAVFGASNFPyaFSTLGGDTAAALAAGCPVIVKnhtAHPGT---- 196
Cdd:cd07106 96 PDE------VIEDDDTRR-------VELRRKPLGVVAAIVPWNFP--LLLAAWKIAPALLAGNTVVLK---PSPFTplct 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 197 ---GELMARaalaaikecAMPLGVFAMVqSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIPFygELGSI 273
Cdd:cd07106 158 lklGELAQE---------VLPPGVLNVV-SGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTL--ELGGN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 274 NPQVILPNKAIeqsKEMAQSLCQSMLMGNGQFCTSPGLWLVPTG-----CDELEAHITACI--NDAPSDTLLTPgivktf 346
Cdd:cd07106 226 DAAIVLPDVDI---DAVAPKLFWGAFINSGQVCAAIKRLYVHESiydefCEALVALAKAAVvgDGLDPGTTLGP------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 347 kqqVEERSQFAQLsvlgKGKLEQAFHANAHVFA----CNADDYLTTPTL-----------HEEVFGPAALVVRYDSEQQL 411
Cdd:cd07106 297 ---VQNKMQYDKV----KELVEDAKAKGAKVLAggepLDGPGYFIPPTIvddppegsrivDEEQFGPVLPVLKYSDEDEV 369
|
410 420 430
....*....|....*....|....*....|...
gi 1887644984 412 MILINKLQGQLTASVHGteADLNKADSVIEALQ 444
Cdd:cd07106 370 IARANDSEYGLGASVWS--SDLERAEAVARRLE 400
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
48-433 |
4.76e-26 |
|
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: 110.05 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 48 AIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERMRTVNQLKAFASALRENpespLG 127
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHER----TG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 128 LKVVDEADVTRAplpkphteLNYLPLGPVAVFGASNFPYAFSTlgGDTAAALAAGCPVIVKNHTAHPGTGELMARAALAA 207
Cdd:cd07095 81 ERATPMAQGRAV--------LRHRPHGVMAVFGPFNFPGHLPN--GHIVPALLAGNTVVFKPSELTPAVAELMVELWEEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 208 ikecAMPLGVFAMVQSkAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIpFYGELGSINPQVILPNKAIEQs 287
Cdd:cd07095 151 ----GLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI-LALEMGGNNPLVVWDVADIDA- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 288 keMAQSLCQSMLMGNGQFCTSPGLWLVPTGC--DELEAHITACIN----DAP--SDTLLTPGIVktfkQQVEERSQFAQL 359
Cdd:cd07095 224 --AAYLIVQSAFLTAGQRCTCARRLIVPDGAvgDAFLERLVEAAKrlriGAPdaEPPFMGPLII----AAAAARYLLAQQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 360 SVLGKGKleQAFHANAHVfacNADDYLTTPTLH----------EEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGT 429
Cdd:cd07095 298 DLLALGG--EPLLAMERL---VAGTAFLSPGIIdvtdaadvpdEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSD 372
|
....
gi 1887644984 430 EADL 433
Cdd:cd07095 373 DEAL 376
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
8-456 |
1.16e-25 |
|
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: 109.58 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 8 LVAGQWIGdsANGEFHA-FSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKT-SFAQRADFLTCIAEQILVLGDEL 85
Cdd:cd07082 5 LINGEWKE--SSGKTIEvYSPIDGEVI-GSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 86 IEQTQQETNLPLARLQGERMRTVNQLKAFASALRE-------NPESPLGLKVvdEADVTRAPLpkphtelnylplGPVAV 158
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRldgdslpGDWFPGTKGK--IAQVRREPL------------GVVLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 159 FGASNFPY--AFSTLggdtAAALAAGCPVIVKNHTAHPGTGELMARAAlaaiKECAMPLGVFAMVQSKAYDISHQLVAAP 236
Cdd:cd07082 148 IGPFNYPLnlTVSKL----IPALIMGNTVVFKPATQGVLLGIPLAEAF----HDAGFPKGVVNVVTGRGREIGDPLVTHG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 237 GIKAVGFTGSFNVASKLQEtIAKReepIPFYGELGSINPQVILPNKAIEqskEMAQSLCQSMLMGNGQFCTSPGLWLV-P 315
Cdd:cd07082 220 RIDVISFTGSTEVGNRLKK-QHPM---KRLVLELGGKDPAIVLPDADLE---LAAKEIVKGALSYSGQRCTAIKRVLVhE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 316 TGCDELEAHITACIN--------DAPSDtlLTPGIVKTFKQQVEE-----RSQFAQLSVLGKGKLEQAFHAnAHVFACNA 382
Cdd:cd07082 293 SVADELVELLKEEVAklkvgmpwDNGVD--ITPLIDPKSADFVEGliddaVAKGATVLNGGGREGGNLIYP-TLLDPVTP 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887644984 383 DDYLTtptlHEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGTeaDLNKADSVIEALQykVGRLIKNQMP 456
Cdd:cd07082 370 DMRLA----WEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTK--DINKARKLADALE--VGTVNINSKC 435
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
25-444 |
9.86e-24 |
|
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: 103.80 E-value: 9.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 25 FSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGER 104
Cdd:cd07093 2 FNPATGEVL-AKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 105 M-RTVNQLKAFASALRENPEsplglkvvdEAdvtrapLPKPHTELNYL---PLGPVAVFGASNFPYAFSTLggDTAAALA 180
Cdd:cd07093 81 IpRAAANFRFFADYILQLDG---------ES------YPQDGGALNYVlrqPVGVAGLITPWNLPLMLLTW--KIAPALA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 181 AGCPVIVKNHTAHPGTGELMARAALAAikecAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKR 260
Cdd:cd07093 144 FGNTVVLKPSEWTPLTAWLLAELANEA----GLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 261 EEPIPFygELGSINPQVILPNKAIEqskEMAQSLCQSMLMGNGQFCTSPGLWLVPTGC-DELEAHITA-----CINDaPS 334
Cdd:cd07093 220 LKPVSL--ELGGKNPNIVFADADLD---RAVDAAVRSSFSNNGEVCLAGSRILVQRSIyDEFLERFVErakalKVGD-PL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 335 D--TLLTPGIvktFKQQVEERSQFAQLS-------VLGKGKLEQAFHANAH-----VFAcNADDylTTPTLHEEVFGPAA 400
Cdd:cd07093 294 DpdTEVGPLI---SKEHLEKVLGYVELAraegatiLTGGGRPELPDLEGGYfveptVIT-GLDN--DSRVAQEEIFGPVV 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1887644984 401 LVVRYDSEQQLMILINKLQGQLTASVHgTEaDLNKADSVIEALQ 444
Cdd:cd07093 368 TVIPFDDEEEAIELANDTPYGLAAYVW-TR-DLGRAHRVARRLE 409
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
22-444 |
1.28e-22 |
|
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: 100.10 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 22 FHAFSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQ 101
Cdd:cd07150 1 FDDLNPADGSVY-ARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 102 GERMRTVNQLKAFASALREnpesPLGlkvvdeaDVTRAPLPKPHTELNYLPLGPVAVFGASNFPYAFSTlgGDTAAALAA 181
Cdd:cd07150 80 FETTFTPELLRAAAGECRR----VRG-------ETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILAT--KKVAFALAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 182 GCPVIVKNHTAHPGTGELMARAalaaIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKRE 261
Cdd:cd07150 147 GNTVVLKPSEETPVIGLKIAEI----MEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 262 EPIPFygELGSINPQVILPNKAIEQSKEMAqslCQSMLMGNGQFCTSPGLWLVP-TGCDELEAHITACI------NDAPS 334
Cdd:cd07150 223 KKITL--ELGGKNPLIVLADADLDYAVRAA---AFGAFMHQGQICMSASRIIVEePVYDEFVKKFVARAsklkvgDPRDP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 335 DTLLTPGI----VKTFKQQVEE-RSQFAQLsvLGKGKLEQAFHAnAHVFACNADDYLttpTLHEEVFGPAALVVRYDSEQ 409
Cdd:cd07150 298 DTVIGPLIsprqVERIKRQVEDaVAKGAKL--LTGGKYDGNFYQ-PTVLTDVTPDMR---IFREETFGPVTSVIPAKDAE 371
|
410 420 430
....*....|....*....|....*....|....*
gi 1887644984 410 QLMILINKLQGQLTASVHGTeaDLNKADSVIEALQ 444
Cdd:cd07150 372 EALELANDTEYGLSAAILTN--DLQRAFKLAERLE 404
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
7-471 |
1.34e-22 |
|
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: 100.33 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 7 SLVAGQWIGdSANGEFHAFSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRAdfltciaEQILVLGDELI 86
Cdd:cd07086 1 GVIGGEWVG-SGGETFTSRNPANGEPI-ARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRG-------EIVRQIGEALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 87 EQTQqetnlPLARLQGERMRtvnqlKAFASALRENPEsplGLKVVDEA---------DVTRAPLPKPHTELNYLPLGPVA 157
Cdd:cd07086 72 KKKE-----ALGRLVSLEMG-----KILPEGLGEVQE---MIDICDYAvglsrmlygLTIPSERPGHRLMEQWNPLGVVG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 158 VFGASNFPYAfsTLGGDTAAALAAGCPVIVKNHTAHPGTGELMARAALAAIKECAMPLGVFAMVQSKAyDISHQLVAAPG 237
Cdd:cd07086 139 VITAFNFPVA--VPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGG-DGGELLVHDPR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 238 IKAVGFTGSFNVASKLQETIAKREEPIPFygELGSINPQVILPNKAIeqskEMAqslCQSMLMG----NGQFCTSPGLWL 313
Cdd:cd07086 216 VPLVSFTGSTEVGRRVGETVARRFGRVLL--ELGGNNAIIVMDDADL----DLA---VRAVLFAavgtAGQRCTTTRRLI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 314 VPTGC-DELEAHITAC-----INDaPSD--TLLTPGIVKTFKQQVEERSQFAQLS---VLGKGK----LEQAFHANAHVF 378
Cdd:cd07086 287 VHESVyDEFLERLVKAykqvrIGD-PLDegTLVGPLINQAAVEKYLNAIEIAKSQggtVLTGGKridgGEPGNYVEPTIV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 379 ACNADDyltTPTLHEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHgTEaDLNKADSVIEALQYKVGrlIKN-QMPT 457
Cdd:cd07086 366 TGVTDD---ARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIF-TE-DLREAFRWLGPKGSDCG--IVNvNIPT 438
|
490
....*....|....*
gi 1887644984 458 -GVEVcgsmnhGGPF 471
Cdd:cd07086 439 sGAEI------GGAF 447
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
40-456 |
1.50e-22 |
|
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: 100.20 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 40 LSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERMRTVNQLKAFASALR 119
Cdd:cd07094 18 DDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRLAAEEAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 120 EN--PESPLGLKVVDEadvTRAPLPKPHtelnylPLGPVAVFGASNFPYAFSTLggDTAAALAAGCPVIVKNHTAHPgtg 197
Cdd:cd07094 98 RIrgEEIPLDATQGSD---NRLAWTIRE------PVGVVLAITPFNFPLNLVAH--KLAPAIATGCPVVLKPASKTP--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 198 eLMARAALAAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIpfygELGSINPQV 277
Cdd:cd07094 164 -LSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIAL----ELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 278 ILPNKAIEQSkemAQSLCQSMLMGNGQFCTSPGLWLVPtgcDEL-EAHITACINDAPS---------DTLLTPGIVKTFK 347
Cdd:cd07094 239 VDRDADLDAA---IEALAKGGFYHAGQVCISVQRIYVH---EELyDEFIEAFVAAVKKlkvgdpldeDTDVGPLISEEAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 348 QQVE---ERSQFAQLSVLGKGKLEQA-FHAnahvfACNADDYLTTPTLHEEVFGPAALVVRYDSEQQLMILINKLQGQLT 423
Cdd:cd07094 313 ERVErwvEEAVEAGARLLCGGERDGAlFKP-----TVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQ 387
|
410 420 430
....*....|....*....|....*....|...
gi 1887644984 424 ASVHgTEaDLNKADSVIEALQykVGRLIKNQMP 456
Cdd:cd07094 388 AGIF-TR-DLNVAFKAAEKLE--VGGVMVNDSS 416
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
25-444 |
1.57e-22 |
|
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: 100.12 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 25 FSPArNEALPTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQ--- 101
Cdd:cd07110 2 INPA-TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwdv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 102 GERMRTVNQLKAFASALRENPESPLGLKVVDEADVTRaplpkphtelnYLPLGPVAVFGASNFPYAFSTLggDTAAALAA 181
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARVR-----------REPVGVVGLITPWNFPLLMAAW--KVAPALAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 182 GCPVIVKNHTAHPGTgELmaraALAAI-KECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKR 260
Cdd:cd07110 148 GCTVVLKPSELTSLT-EL----ELAEIaAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 261 EEPIPFygELGSINPQVILPNKAIEQSKEMAQSLCqsmLMGNGQFCTSPGLWLVPTGCDE-----LEAHITACINDAP-- 333
Cdd:cd07110 223 IKPVSL--ELGGKSPIIVFDDADLEKAVEWAMFGC---FWNNGQICSATSRLLVHESIADaflerLATAAEAIRVGDPle 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 334 SDTLLTPGIVKTFKQQVEE-----RSQFAQLSVLGK--GKLEQAFHANAHVFA-CNADDYLTTptlhEEVFGPAALVVRY 405
Cdd:cd07110 298 EGVRLGPLVSQAQYEKVLSfiargKEEGARLLCGGRrpAHLEKGYFIAPTVFAdVPTDSRIWR----EEIFGPVLCVRSF 373
|
410 420 430
....*....|....*....|....*....|....*....
gi 1887644984 406 DSEQQLMILINKLQGQLTASVhgTEADLNKADSVIEALQ 444
Cdd:cd07110 374 ATEDEAIALANDSEYGLAAAV--ISRDAERCDRVAEALE 410
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
26-426 |
2.78e-22 |
|
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: 99.37 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 26 SPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERM 105
Cdd:cd07107 3 NPATGQVL-ARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 106 RTVNQLKAFASalrenpespLGLkvvdeaDVTRAPLPKPHTELNYL---PLGPVAVFGASNFPYAFStlGGDTAAALAAG 182
Cdd:cd07107 82 VAAALLDYFAG---------LVT------ELKGETIPVGGRNLHYTlrePYGVVARIVAFNHPLMFA--AAKIAAPLAAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 183 CPVIVKNhtahPGTGELMArAALAAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREE 262
Cdd:cd07107 145 NTVVVKP----PEQAPLSA-LRLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 263 PIPFygELGSINPQVILPNKAIEQskeMAQSLCQSMLMG-NGQFCTSPGLWLVPTGC-DELEAHI-TACINDAPSDtllt 339
Cdd:cd07107 220 HVTL--ELGGKNALIVFPDADPEA---AADAAVAGMNFTwCGQSCGSTSRLFVHESIyDEVLARVvERVAAIKVGD---- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 340 PGIVKTFKQQVEERSQFAQ-LSVLGKGKLEQA------FHANAHVFacnADDYLTTPTL-----------HEEVFGPAAL 401
Cdd:cd07107 291 PTDPATTMGPLVSRQQYDRvMHYIDSAKREGArlvtggGRPEGPAL---EGGFYVEPTVfadvtpgmriaREEIFGPVLS 367
|
410 420
....*....|....*....|....*
gi 1887644984 402 VVRYDSEQQLMILINKLQGQLTASV 426
Cdd:cd07107 368 VLRWRDEAEMVAQANGVEYGLTAAI 392
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
8-468 |
3.71e-22 |
|
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: 99.07 E-value: 3.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 8 LVAGQWIGDSANGEFHAFSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDEL-- 85
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETL-SEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLam 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 86 ---------IEQTQQeTNLPLArlqgermrtVNQLKAFASALRENPESplgLKVVDEadvtraplpkphTELNYLPLGPV 156
Cdd:cd07117 83 vetldngkpIRETRA-VDIPLA---------ADHFRYFAGVIRAEEGS---ANMIDE------------DTLSIVLREPI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 157 AVFGAS---NFPYAFSTLggDTAAALAAGCPVIVknhtaHPGTGELMARAALAAIKECAMPLGVFAMVQSKAYDISHQLV 233
Cdd:cd07117 138 GVVGQIipwNFPFLMAAW--KLAPALAAGNTVVI-----KPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 234 AAPGIKAVGFTGSFNVASKLQETIAKReePIPFYGELGSINPQVILPNKAIEQSKEMAQslcQSMLMGNGQFCTSPGLWL 313
Cdd:cd07117 211 NHPGLDKLAFTGSTEVGRDVAIAAAKK--LIPATLELGGKSANIIFDDANWDKALEGAQ---LGILFNQGQVCCAGSRIF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 314 VPTGC-DELEAHITACINDAPSDTLLTPGIV---KTFKQQVEErsqfaQLSVLGKGKLEQA-FHANAHVFACNADD--YL 386
Cdd:cd07117 286 VQEGIyDEFVAKLKEKFENVKVGNPLDPDTQmgaQVNKDQLDK-----ILSYVDIAKEEGAkILTGGHRLTENGLDkgFF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 387 TTPTL-----------HEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHgtEADLNKADSVIEALQykVGRL---IK 452
Cdd:cd07117 361 IEPTLivnvtndmrvaQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVF--TKDINRALRVARAVE--TGRVwvnTY 436
|
490
....*....|....*.
gi 1887644984 453 NQMPTGVEVCGSMNHG 468
Cdd:cd07117 437 NQIPAGAPFGGYKKSG 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
48-445 |
6.13e-22 |
|
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: 98.03 E-value: 6.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 48 AIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQET---------NLPLArlqgermrtVNQLKAFASAL 118
Cdd:cd07105 5 AVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETgataawagfNVDLA---------AGMLREAASLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 119 RENPEsplGLKVVDEADvTRAPLPKPhtelnylPLGPVAVFGASNFPYafsTLGGDT-AAALAAGCPVIVKNHTAHPGTG 197
Cdd:cd07105 76 TQIIG---GSIPSDKPG-TLAMVVKE-------PVGVVLGIAPWNAPV---ILGTRAiAYPLAAGNTVVLKASELSPRTH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 198 ELMARAALAAikecAMPLGVFAMVQSKAYD---ISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIPFygELGSIN 274
Cdd:cd07105 142 WLIGRVFHEA----GLPKGVLNVVTHSPEDapeVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLL--ELGGKA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 275 PQVILPNKAIEQSkemAQSLCQSMLMGNGQFCTSPGLWLVPTG-CDELEAHITACINDAPSD-----TLLTPGIVKTFKQ 348
Cdd:cd07105 216 PAIVLEDADLDAA---ANAALFGAFLNSGQICMSTERIIVHESiADEFVEKLKAAAEKLFAGpvvlgSLVSAAAADRVKE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 349 QVEersqfaqlSVLGKG-KLEQAFHAnahvfACNADDYLTTPTL-----------HEEVFGPAALVVRYDSEQQLMILIN 416
Cdd:cd07105 293 LVD--------DALSKGaKLVVGGLA-----DESPSGTSMPPTIldnvtpdmdiySEESFGPVVSIIRVKDEEEAVRIAN 359
|
410 420
....*....|....*....|....*....
gi 1887644984 417 KLQGQLTASVHGteADLNKADSVIEALQY 445
Cdd:cd07105 360 DSEYGLSAAVFT--RDLARALAVAKRIES 386
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
26-444 |
6.50e-22 |
|
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: 98.20 E-value: 6.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 26 SPARNEALPTRFFNlSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETnlplarlqGERM 105
Cdd:cd07108 3 NPATGQVIGEVPRS-RAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALET--------GNAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 106 RTvnQLKAFASALrenpesplglkvvdeADVTR-----AP------LPKPHTELNYLPLGPVAVFGAS---NFPYAFSTL 171
Cdd:cd07108 74 RT--QARPEAAVL---------------ADLFRyfgglAGelkgetLPFGPDVLTYTVREPLGVVGAIlpwNAPLMLAAL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 172 ggDTAAALAAGCPVIVKNHTAHPgtgelMARAALAAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVAS 251
Cdd:cd07108 137 --KIAPALVAGNTVVLKAAEDAP-----LAVLLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 252 KLQETIAKREEPIPFygELGSINPQVILPNKAIEQSkeMAQSLCQSMLMGNGQFCT-SPGLWLVPTGCDELEAHITACIN 330
Cdd:cd07108 210 IIYRAAADRLIPVSL--ELGGKSPMIVFPDADLDDA--VDGAIAGMRFTRQGQSCTaGSRLFVHEDIYDAFLEKLVAKLS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 331 --------DAPSD--TLLTPGIVKTFKQQVEERSQFAQLSVLGKGKLEQAFHanahvfacNADDYLTTPTL--------- 391
Cdd:cd07108 286 klkigdplDEATDigAIISEKQFAKVCGYIDLGLSTSGATVLRGGPLPGEGP--------LADGFFVQPTIfsgvdnewr 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1887644984 392 --HEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGTeaDLNKADSVIEALQ 444
Cdd:cd07108 358 laREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR--DLGRALRAAHALE 410
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
24-444 |
7.98e-22 |
|
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: 97.76 E-value: 7.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 24 AFSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRAdfltciaeQILVLGDELIEQTQQEtnlpLARLQge 103
Cdd:cd07090 1 VIEPATGEVL-ATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERG--------RILRKAADLLRERNDE----IARLE-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 104 rmrTVNQLKAFASALrenpesplgLKVVDEADVTR------APLPKPHTELN-----Y---LPLGPVAVFGASNFPyaFS 169
Cdd:cd07090 66 ---TIDNGKPIEEAR---------VDIDSSADCLEyyaglaPTLSGEHVPLPggsfaYtrrEPLGVCAGIGAWNYP--IQ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 170 TLGGDTAAALAAGCPVIVKNHTAHPGTGELMARAalaaIKECAMPLGVFAMVQSKAyDISHQLVAAPGIKAVGFTGSFNV 249
Cdd:cd07090 132 IASWKSAPALACGNAMVYKPSPFTPLTALLLAEI----LTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 250 ASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQSkemaqslCQSMLMGN----GQFCTSPGLWLVPTGC-DELEAH 324
Cdd:cd07090 207 GKKVMSAAAKGIKHVTL--ELGGKSPLIIFDDADLENA-------VNGAMMANflsqGQVCSNGTRVFVQRSIkDEFTER 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 325 I---TACI---NDAPSDTLLTPGIVKTFKQQVEE-----RSQFAQL-----SVLGKGKLEQAFHANAHVFACNADDyltT 388
Cdd:cd07090 278 LverTKKIrigDPLDEDTQMGALISEEHLEKVLGyiesaKQEGAKVlcggeRVVPEDGLENGFYVSPCVLTDCTDD---M 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1887644984 389 PTLHEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHgtEADLNKADSVIEALQ 444
Cdd:cd07090 355 TIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVF--TRDLQRAHRVIAQLQ 408
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
15-427 |
1.14e-21 |
|
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: 98.04 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 15 GDSANGEFHA-FSPARNEALPTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAeqilvlgDELIEQTqqet 93
Cdd:cd07125 40 EETETGEGAPvIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAA-------DLLEANR---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 94 nlplARLQGERMRTVNqlKAFASALRENPESplglkvVD---------EADVTRAPLPKPHTELN---YLPLGPVAVFGA 161
Cdd:cd07125 109 ----GELIALAAAEAG--KTLADADAEVREA------IDfcryyaaqaRELFSDPELPGPTGELNgleLHGRGVFVCISP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 162 SNFPYAFSTlgGDTAAALAAGCPVIVK--NHTAhpgtgeLMARAALAAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIK 239
Cdd:cd07125 177 WNFPLAIFT--GQIAAALAAGNTVIAKpaEQTP------LIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 240 AVGFTGSFNVASKLQETIAKREEPI-PFYGELGSINPQVILPNKAIEQskeMAQSLCQSMLMGNGQFCTSPGLWLVPtgc 318
Cdd:cd07125 249 GVIFTGSTETAKLINRALAERDGPIlPLIAETGGKNAMIVDSTALPEQ---AVKDVVQSAFGSAGQRCSALRLLYLQ--- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 319 DELEAHITACINDA--------PSD--TLLTPGI----VKTFKQQVEERSQFAQLsvLGKGKLEQafhANAHVFACNADD 384
Cdd:cd07125 323 EEIAERFIEMLKGAmaslkvgdPWDlsTDVGPLIdkpaGKLLRAHTELMRGEAWL--IAPAPLDD---GNGYFVAPGIIE 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1887644984 385 YLTTPTLHEEVFGPAALVVRYDSEQ--QLMILINKLQGQLTASVH 427
Cdd:cd07125 398 IVGIFDLTTEVFGPILHVIRFKAEDldEAIEDINATGYGLTLGIH 442
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
9-444 |
5.99e-21 |
|
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: 95.26 E-value: 5.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 9 VAGQWIGDSANGEFHAFSPARNEALPTrfFNLSTAE-LNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIE 87
Cdd:cd07138 3 IDGAWVAPAGTETIDVINPATEEVIGT--VPLGTAAdVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 88 QTQQETNLPL---ARLQGERmrTVNQLKAFASALRENP-ESPLGlkvvdEADVTRAPLpkphtelnylplGPVAVFGASN 163
Cdd:cd07138 81 AITLEMGAPItlaRAAQVGL--GIGHLRAAADALKDFEfEERRG-----NSLVVREPI------------GVCGLITPWN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 164 FPyaFSTLGGDTAAALAAGCPVIVKNHTAHPGTGELMARAalaaIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGF 243
Cdd:cd07138 142 WP--LNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEI----LDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 244 TGSFNVASKLQETIA---KReepipFYGELGSINPQVILPNKAIEQSKEMAqslCQSMLMGNGQFCTSPGLWLVPTGC-D 319
Cdd:cd07138 216 TGSTRAGKRVAEAAAdtvKR-----VALELGGKSANIILDDADLEKAVPRG---VAACFANSGQSCNAPTRMLVPRSRyA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 320 ELEAHITACIN----DAPSDTLLTPGIVKTFKQQ----------VEERsqfAQLSVLGKGK---LEQAFHANAHVFacnA 382
Cdd:cd07138 288 EAEEIAAAAAEayvvGDPRDPATTLGPLASAAQFdrvqgyiqkgIEEG---ARLVAGGPGRpegLERGYFVKPTVF---A 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887644984 383 DDyltTP--TLH-EEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGteADLNKADSVIEALQ 444
Cdd:cd07138 362 DV---TPdmTIArEEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWS--ADPERARAVARRLR 421
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
9-407 |
2.26e-20 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 93.87 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 9 VAGQWIgdSANGE-FHAFSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIE 87
Cdd:PRK09457 5 INGDWI--AGQGEaFESRNPVSGEVL-WQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 88 QTQQETNLPLARLQGERMRTVNQLKAFASALRENPesplGLKVVDEADVTRAPLPKPHtelnylplGPVAVFGASNFPYA 167
Cdd:PRK09457 82 VIARETGKPLWEAATEVTAMINKIAISIQAYHERT----GEKRSEMADGAAVLRHRPH--------GVVAVFGPYNFPGH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 168 FSTlgGDTAAALAAGCPVIVKNHTAHPGTGELMARAALAAikecAMPLGVFAMVQSkAYDISHQLVAAPGIKAVGFTGSF 247
Cdd:PRK09457 150 LPN--GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQA----GLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 248 NVASKLQETIAKREEPIpFYGELGSINPQVIlpnKAIEQSKEMAQSLCQSMLMGNGQFCTSPGLWLVPTGC--DELEAHI 325
Cdd:PRK09457 223 NTGYLLHRQFAGQPEKI-LALEMGGNNPLVI---DEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqgDAFLARL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 326 TACIN-------DAPSDTLLTPGIVKTFKQQVEErsqfAQLSVLGKGKleQAFHANAHVfacNADDYLTTPTL------- 391
Cdd:PRK09457 299 VAVAKrltvgrwDAEPQPFMGAVISEQAAQGLVA----AQAQLLALGG--KSLLEMTQL---QAGTGLLTPGIidvtgva 369
|
410
....*....|....*....
gi 1887644984 392 ---HEEVFGPAALVVRYDS 407
Cdd:PRK09457 370 elpDEEYFGPLLQVVRYDD 388
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
45-444 |
2.66e-20 |
|
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: 92.91 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 45 LNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGErmrtVNqlKAfASALR---EN 121
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAE----VE--KC-AWICRyyaEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 122 PESPLglkvvdeADVTRaPLPKPHTELNYLPLGPvaVFGAS--NFPY--AFSTLggdtAAALAAGCPVIVKnHTAH-PGT 196
Cdd:cd07100 74 AEAFL-------ADEPI-ETDAGKAYVRYEPLGV--VLGIMpwNFPFwqVFRFA----APNLMAGNTVLLK-HASNvPGC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 197 GELMARaalaAIKECAMPLGVFAMVQSKAYDIShQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIPFygELGSINPQ 276
Cdd:cd07100 139 ALAIEE----LFREAGFPEGVFQNLLIDSDQVE-AIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVL--ELGGSDPF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 277 VILPNKAIEQSKEMAqslCQSMLMGNGQFCTSPGLWLVPTGC-DELEAHITACINDA----PSD--TLLTP----GIVKT 345
Cdd:cd07100 212 IVLDDADLDKAVKTA---VKGRLQNAGQSCIAAKRFIVHEDVyDEFLEKFVEAMAALkvgdPMDedTDLGPlarkDLRDE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 346 FKQQVEE-RSQFAQLsVLGKGKLEQ--AFHANAHVfacnADDYLTTPTLHEEVFGPAALVVRYDSEQQLMILINKLQGQL 422
Cdd:cd07100 289 LHEQVEEaVAAGATL-LLGGKRPDGpgAFYPPTVL----TDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGL 363
|
410 420
....*....|....*....|..
gi 1887644984 423 TASVHGTeaDLNKADSVIEALQ 444
Cdd:cd07100 364 GGSVFTT--DLERAERVARRLE 383
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
11-456 |
3.16e-20 |
|
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: 93.14 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 11 GQWIGDSANGEFHAFSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQ 90
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETL-AEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 91 QETNlplarlqGERMRTVNQLKAFASALRENPESPLGLkvvdEADVTRAPLPKPHTELNYLPLGPVAVFGASNFPYAFST 170
Cdd:cd07151 80 RESG-------STRIKANIEWGAAMAITREAATFPLRM----EGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 171 LGgdTAAALAAGCPVIVKNHTAHPGTGELMaraaLAAIKECA-MPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNV 249
Cdd:cd07151 149 RS--VAPALALGNAVVLKPASDTPITGGLL----LAKIFEEAgLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 250 ASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQSKEMAqslcqsmLMG----NGQFCTSPGLWLVPTGC-DE---- 320
Cdd:cd07151 223 GRHIGELAGRHLKKVAL--ELGGNNPFVVLEDADIDAAVNAA-------VFGkflhQGQICMAINRIIVHEDVyDEfvek 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 321 LEAHITACINDAPSD--TLLTPGIvktfkqqveERSQFAQLsvlgKGKLEQAFHANA---------------HVFA-CNA 382
Cdd:cd07151 294 FVERVKALPYGDPSDpdTVVGPLI---------NESQVDGL----LDKIEQAVEEGAtllvggeaegnvlepTVLSdVTN 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887644984 383 DdyltTPTLHEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGteADLNKADSVieALQYKVGRLIKNQMP 456
Cdd:cd07151 361 D----MEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFT--SDLERGVQF--ARRIDAGMTHINDQP 426
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
6-445 |
3.68e-20 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 93.05 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 6 QSLVAGQWIgDSANGEFHAFS-PARNEALPTrFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDE 84
Cdd:PRK11241 12 QALINGEWL-DANNGEVIDVTnPANGDKLGS-VPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 85 LIEQTQQETNLPLARLQGERMRTVNQLKAFAsalrENPESPLGlkvvdeaDVTRAPLPKPHTELNYLPLGPVAVFGASNF 164
Cdd:PRK11241 90 LARLMTLEQGKPLAEAKGEISYAASFIEWFA----EEGKRIYG-------DTIPGHQADKRLIVIKQPIGVTAAITPWNF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 165 PYAFSTLggDTAAALAAGCPVIVKnhtahPGTGELMARAALAAIKECA-MPLGVFAMVQSKAYDISHQLVAAPGIKAVGF 243
Cdd:PRK11241 159 PAAMITR--KAGPALAAGCTMVLK-----PASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVGGELTSNPLVRKLSF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 244 TGSFNVASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQSKEMAQSlcqSMLMGNGQFCTSPGLWLVPTGC-DELE 322
Cdd:PRK11241 232 TGSTEIGRQLMEQCAKDIKKVSL--ELGGNAPFIVFDDADLDKAVEGALA---SKFRNAGQTCVCANRLYVQDGVyDRFA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 323 AHITACI------NDAPSDTLLTPGIVKTFKQQVEERSQFA---QLSVLGKGKLeQAFHANAHVFACNADDYLTTPTLHE 393
Cdd:PRK11241 307 EKLQQAVsklhigDGLEKGVTIGPLIDEKAVAKVEEHIADAlekGARVVCGGKA-HELGGNFFQPTILVDVPANAKVAKE 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1887644984 394 EVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGTeaDLNKADSVIEALQY 445
Cdd:PRK11241 386 ETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYAR--DLSRVFRVGEALEY 435
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
26-444 |
5.02e-20 |
|
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: 92.50 E-value: 5.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 26 SPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPL-ARLQGER 104
Cdd:cd07115 3 NPATGELI-ARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIrAARRLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 105 MRTVNQLKAFASALREnpespLGLKVVdeadvtraPLPKPHteLNYLPLGPVAVFGAS---NFPYAFSTLggDTAAALAA 181
Cdd:cd07115 82 PRAADTFRYYAGWADK-----IEGEVI--------PVRGPF--LNYTVREPVGVVGAIvpwNFPLMFAAW--KVAPALAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 182 GCPVIVKNHTAHPGTGELMARAALaaikECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKRE 261
Cdd:cd07115 145 GNTVVLKPAELTPLSALRIAELMA----EAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 262 EPIPFygELGSINPQVILPNKAIEQSKEMAQSlcqSMLMGNGQFCTSPGLWLVPTGC-DELEAHITACINDA----PSD- 335
Cdd:cd07115 221 KRVSL--ELGGKSANIVFADADLDAAVRAAAT---GIFYNQGQMCTAGSRLLVHESIyDEFLERFTSLARSLrpgdPLDp 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 336 -TLLTPGIVKTFKQQVEE-----RSQFAQLSVLGKGKLEQAFHANAHVFACNADDYLTTptlHEEVFGPAALVVRYDSEQ 409
Cdd:cd07115 296 kTQMGPLVSQAQFDRVLDyvdvgREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIA---QEEIFGPVVSVMRFRDEE 372
|
410 420 430
....*....|....*....|....*....|....*
gi 1887644984 410 QLMILINKLQGQLTASVHgtEADLNKADSVIEALQ 444
Cdd:cd07115 373 EALRIANGTEYGLAAGVW--TRDLGRAHRVAAALK 405
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
25-458 |
6.31e-20 |
|
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: 92.03 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 25 FSPARNEALPTrFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGER 104
Cdd:cd07145 4 RNPANGEVIDT-VPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 105 MRTVNQLKAFASALREnpespLGLKV--VDEADVTRAPLPKPHTElnylPLGPVAVFGASNFPyaFSTLGGDTAAALAAG 182
Cdd:cd07145 83 ERTIRLFKLAAEEAKV-----LRGETipVDAYEYNERRIAFTVRE----PIGVVGAITPFNFP--ANLFAHKIAPAIAVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 183 CPVIVKNHTAHPGTGELMARAalaaIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREE 262
Cdd:cd07145 152 NSVVVKPSSNTPLTAIELAKI----LEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 263 PIPFygELGSINPQVILPNKAIEQSkemAQSLCQSMLMGNGQFCTSPGLWLVPtgcDELEAHITACINDA--------PS 334
Cdd:cd07145 228 KVAL--ELGGSDPMIVLKDADLERA---VSIAVRGRFENAGQVCNAVKRILVE---EEVYDKFLKLLVEKvkklkvgdPL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 335 D------TLLTPGIVKTFKQQVEER-SQFAQLSVLGKGKlEQAFHANAHVfacnADDYLTTPTLHEEVFGPAALVVRYDS 407
Cdd:cd07145 300 DestdlgPLISPEAVERMENLVNDAvEKGGKILYGGKRD-EGSFFPPTVL----ENDTPDMIVMKEEVFGPVLPIAKVKD 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1887644984 408 EQQLMILINKLQGQLTASVHgTEaDLNKADSVIEALQY------KVGRLIKNQMPTG 458
Cdd:cd07145 375 DEEAVEIANSTEYGLQASVF-TN-DINRALKVARELEAggvvinDSTRFRWDNLPFG 429
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
44-436 |
8.95e-20 |
|
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: 91.44 E-value: 8.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 44 ELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERMRTVNQLKAFASALREnpe 123
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 124 sPLGLKVvdeadvtraPLPKPHTElNY---LPLGPVAVFGASNFPYAFSTLGgdTAAALAAGCPVIVKNHTAHPGTGELM 200
Cdd:cd07104 78 -PEGEIL---------PSDVPGKE-SMvrrVPLGVVGVISPFNFPLILAMRS--VAPALALGNAVVLKPDSRTPVTGGLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 201 araaLAAIKECA-MPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIPFygELGSINPQVIL 279
Cdd:cd07104 145 ----IAEIFEEAgLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVAL--ELGGNNPLIVL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 280 PNKAIEQSkemAQSLCQSMLMGNGQFCTSPGLWLVPTGC-DELEAHITACI------NDAPSDTLLTPGI----VKTFKQ 348
Cdd:cd07104 219 DDADLDLA---VSAAAFGAFLHQGQICMAAGRILVHESVyDEFVEKLVAKAkalpvgDPRDPDTVIGPLInerqVDRVHA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 349 QVEE-RSQFAQlsVLGKGKLEQAFHAnAHVFA-CNADdyltTPTLHEEVFGPAALVVRYDSEQQLMILINKLQGQLTASV 426
Cdd:cd07104 296 IVEDaVAAGAR--LLTGGTYEGLFYQ-PTVLSdVTPD----MPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAV 368
|
410
....*....|
gi 1887644984 427 HGteADLNKA 436
Cdd:cd07104 369 FT--RDLERA 376
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
26-308 |
3.89e-19 |
|
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: 89.59 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 26 SPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERM 105
Cdd:cd07099 2 NPATGEVL-GEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 106 RTVNQLKAFASalreNPESPLGlkvvDEADVTRAPLPKPHTELNYLPLGPVAVFGASNFPyaFSTLGGDTAAALAAGCPV 185
Cdd:cd07099 81 LALEAIDWAAR----NAPRVLA----PRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYP--LLTPMGDIIPALAAGNAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 186 IVKNHTAHPGTGELMARaalaAIKECAMPLGVFAMVQSKAyDISHQLVAApGIKAVGFTGSFNVASKLQETIAKReePIP 265
Cdd:cd07099 151 VLKPSEVTPLVGELLAE----AWAAAGPPQGVLQVVTGDG-ATGAALIDA-GVDKVAFTGSVATGRKVMAAAAER--LIP 222
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1887644984 266 FYGELGSINPQVILPNKAIEQSkemAQSLCQSMLMGNGQFCTS 308
Cdd:cd07099 223 VVLELGGKDPMIVLADADLERA---AAAAVWGAMVNAGQTCIS 262
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
41-444 |
5.29e-19 |
|
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: 89.42 E-value: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 41 STAELNGAIEAAQSAFY-QYRKTSFAQRADFLTCIAEQILVLGDEL--IEQTQQETNLPLARLQgERMRTVNQLKAFASa 117
Cdd:cd07113 35 TEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEELaqLETLCSGKSIHLSRAF-EVGQSANFLRYFAG- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 118 lrenpespLGLKVVDEadvTRAP-LPKPHTElNYL------PLGPVAVFgasnFPYAFSTLGG--DTAAALAAGCPVIVK 188
Cdd:cd07113 113 --------WATKINGE---TLAPsIPSMQGE-RYTaftrrePVGVVAGI----VPWNFSVMIAvwKIGAALATGCTIVIK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 189 NHTAHPGTgeLMARAALAaiKECAMPLGVFAMVQSKAyDISHQLVAAPGIKAVGFTGSFNVASKLQETIA---KReepip 265
Cdd:cd07113 177 PSEFTPLT--LLRVAELA--KEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQAAsdlTR----- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 266 FYGELGSINPQVILPNKAIEqskEMAQSLCQSMLMGNGQFCTSPGLWLVP-TGCDELEAHITACINDAPSDTLLTPGivk 344
Cdd:cd07113 247 VTLELGGKNAAAFLKDADID---WVVEGLLTAGFLHQGQVCAAPERFYVHrSKFDELVTKLKQALSSFQVGSPMDES--- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 345 TFKQQVEERSQFAQLsvlgKGKLEQAFHANAHVF----ACNADDYLTTPTL-----------HEEVFGPAALVVRYDSEQ 409
Cdd:cd07113 321 VMFGPLANQPHFDKV----CSYLDDARAEGDEIVrggeALAGEGYFVQPTLvlarsadsrlmREETFGPVVSFVPYEDEE 396
|
410 420 430
....*....|....*....|....*....|....*
gi 1887644984 410 QLMILINKLQGQLTASVHgTEaDLNKADSVIEALQ 444
Cdd:cd07113 397 ELIQLINDTPFGLTASVW-TN-NLSKALRYIPRIE 429
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
41-471 |
5.54e-19 |
|
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: 89.22 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 41 STAELNGAIEAAQSAFYQY-RKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGerMRTVNQLKAFASALR 119
Cdd:cd07089 17 GAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA--MQVDGPIGHLRYFAD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 120 enpespLGLKVVDEADVTRAPLPKP--HTELNYLPLGPVAVFGASNFPyaFSTLGGDTAAALAAGCPVIVKNHTAHPGTG 197
Cdd:cd07089 95 ------LADSFPWEFDLPVPALRGGpgRRVVRREPVGVVAAITPWNFP--FFLNLAKLAPALAAGNTVVLKPAPDTPLSA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 198 ELMARAALAAikecAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIPFygELGSINPQV 277
Cdd:cd07089 167 LLLGEIIAET----DLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLL--ELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 278 ILPNKAIEQskemAQSLCQSMLMGN-GQFCTSPGLWLVPTGC-DELEAHITAC-----INDaPSD--TLLTPGIVKTFKQ 348
Cdd:cd07089 241 VLDDADLAA----AAPAAVGVCMHNaGQGCALTTRLLVPRSRyDEVVEALAAAfealpVGD-PADpgTVMGPLISAAQRD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 349 QVEE-----RSQFAQLsVLGKGK---LEQAFHANAHVFAcnadDYLTTPTLH-EEVFGPAALVVRYDSEQQLMILINKLQ 419
Cdd:cd07089 316 RVEGyiargRDEGARL-VTGGGRpagLDKGFYVEPTLFA----DVDNDMRIAqEEIFGPVLVVIPYDDDDEAVRIANDSD 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1887644984 420 GQLTASVHGteADLNKAdsviealqYKVGRLIKNQMpTGVEVCGSMNHGGPF 471
Cdd:cd07089 391 YGLSGGVWS--ADVDRA--------YRVARRIRTGS-VGINGGGGYGPDAPF 431
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
26-444 |
8.07e-19 |
|
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: 88.84 E-value: 8.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 26 SPARNEALPTRFFnLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGErm 105
Cdd:cd07102 2 SPIDGSVIAERPL-ASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 106 rtVNQLKAFASALRENPESPLglkvvdeADVTRAPLPKPHTELNYLPLGPVAVFGASNFPYAfsTLGGDTAAALAAGCPV 185
Cdd:cd07102 79 --IRGMLERARYMISIAEEAL-------ADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYL--TAVNAVIPALLAGNAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 186 IVKNHTAHPGTGELMARAALAAikecAMPLGVFAMVQSKAYDISHqLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIP 265
Cdd:cd07102 148 ILKHSPQTPLCGERFAAAFAEA----GLPEGVFQVLHLSHETSAA-LIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 266 FygELGSINPQVILPNKAIEQSkemAQSLCQSMLMGNGQFCtspglwlvptgC------------DELEAHITACIN--- 330
Cdd:cd07102 223 L--ELGGKDPAYVRPDADLDAA---AESLVDGAFFNSGQSC-----------CsieriyvhesiyDAFVEAFVAVVKgyk 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 331 ----DAPSDTLltpGIVKTFKQQVEERSQFAQlsVLGKG-KLeqafHANAHVFA-CNADDYLTTPTL-----H------E 393
Cdd:cd07102 287 lgdpLDPSTTL---GPVVSARAADFVRAQIAD--AIAKGaRA----LIDGALFPeDKAGGAYLAPTVltnvdHsmrvmrE 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1887644984 394 EVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGTeaDLNKADSVIEALQ 444
Cdd:cd07102 358 ETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK--DIARAEALGEQLE 406
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
26-427 |
2.19e-18 |
|
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: 87.66 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 26 SPARNEALPTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEqilvlgdeLIEQTQQETNLPLARLQGerm 105
Cdd:TIGR01238 57 NPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLAD--------LLELHMPELMALCVREAG--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 106 rtvnqlKAFASALRENPESplglkvVD----EADVTRAPLPKPHTElnylPLGPVAVFGASNFPYAFSTlgGDTAAALAA 181
Cdd:TIGR01238 126 ------KTIHNAIAEVREA------VDfcryYAKQVRDVLGEFSVE----SRGVFVCISPWNFPLAIFT--GQISAALAA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 182 GCPVIVKNHTAHPgtgeLMARAALAAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKRE 261
Cdd:TIGR01238 188 GNTVIAKPAEQTS----LIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 262 E-PIPFYGELGSINPQVILPNKAIEQskeMAQSLCQSMLMGNGQFCTSPGLWLVPtgcDELEAHITACINDAPSD----- 335
Cdd:TIGR01238 264 DaPVPLIAETGGQNAMIVDSTALPEQ---VVRDVLRSAFDSAGQRCSALRVLCVQ---EDVADRVLTMIQGAMQElkvgv 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 336 -----TLLTPGIVKTFKQQVEERSQfaQLSVLGKgKLEQAFHANAHvfACNADDYLtTPT---------LHEEVFGPAAL 401
Cdd:TIGR01238 338 phlltTDVGPVIDAEAKQNLLAHIE--HMSQTQK-KIAQLTLDDSR--ACQHGTFV-APTlfelddiaeLSEEVFGPVLH 411
|
410 420
....*....|....*....|....*...
gi 1887644984 402 VVRYDSEQ--QLMILINKLQGQLTASVH 427
Cdd:TIGR01238 412 VVRYKAREldQIVDQINQTGYGLTMGVH 439
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
25-444 |
2.27e-18 |
|
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: 87.29 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 25 FSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQ-YRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGE 103
Cdd:cd07109 2 FDPSTGEVF-ARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 104 RMRTVNQLKAFASALR--ENPESPLGlkvVDEADVTRaplpkphtelnYLPLGPVAVFGASNFPyaFSTLGGDTAAALAA 181
Cdd:cd07109 81 VEAAARYFEYYGGAADklHGETIPLG---PGYFVYTV-----------REPHGVTGHIIPWNYP--LQITGRSVAPALAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 182 GCPVIVKNHTAHPGTGELMARAALAAikecAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKRE 261
Cdd:cd07109 145 GNAVVVKPAEDAPLTALRLAELAEEA----GLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 262 epIPFYGELGSINPQVILPNKAIEQSkemAQSLCQSMLMGNGQFCTSPGLWLVPTGC-DELEAHITAC-----INDAPSD 335
Cdd:cd07109 221 --VPVTLELGGKSPQIVFADADLEAA---LPVVVNAIIQNAGQTCSAGSRLLVHRSIyDEVLERLVERfralrVGPGLED 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 336 TLLTPGIVKTFKQQVEERSQFAQLS---VLGKGKLEQAFHANAHVFA------CNADDylttPTLHEEVFGPAALVVRYD 406
Cdd:cd07109 296 PDLGPLISAKQLDRVEGFVARARARgarIVAGGRIAEGAPAGGYFVAptllddVPPDS----RLAQEEIFGPVLAVMPFD 371
|
410 420 430
....*....|....*....|....*....|....*...
gi 1887644984 407 SEQQLMILINKLQGQLTASVHgtEADLNKADSVIEALQ 444
Cdd:cd07109 372 DEAEAIALANGTDYGLVAGVW--TRDGDRALRVARRLR 407
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
43-493 |
2.50e-18 |
|
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: 87.63 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 43 AELNGAIEAAQSAFYQYRKTSFAQRAdfltciaeQILVLGDELIEQTQQETNLPLARLQGERMrtVNQLKAFASAL---R 119
Cdd:cd07083 55 AEAEAALEAAWAAFKTWKDWPQEDRA--------RLLLKAADLLRRRRRELIATLTYEVGKNW--VEAIDDVAEAIdfiR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 120 ENPESPLGLKVVDEADVtraPLPKPHTELNYLPLGPVAVFGASNFPYAFstLGGDTAAALAAGCPVIVKnhtahPGTGEL 199
Cdd:cd07083 125 YYARAALRLRYPAVEVV---PYPGEDNESFYVGLGAGVVISPWNFPVAI--FTGMIVAPVAVGNTVIAK-----PAEDAV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 200 MARAALAAI-KECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEP----IPFYGELGSIN 274
Cdd:cd07083 195 VVGYKVFEIfHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPGqtwfKRLYVETGGKN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 275 PQVILPNKAIEQskeMAQSLCQSMLMGNGQFCTSPGLWLVPTGCDE------LEAHITACINDAPSD-TLLTPGIVKTFK 347
Cdd:cd07083 275 AIIVDETADFEL---VVEGVVVSAFGFQGQKCSAASRLILTQGAYEpvlerlLKRAERLSVGPPEENgTDLGPVIDAEQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 348 QQVEERSQFAQ--LSVLGKGKLEQafhANAHVFACNA--DDYLTTPTLHEEVFGPAALVVRY--DSEQQLMILINKLQGQ 421
Cdd:cd07083 352 AKVLSYIEHGKneGQLVLGGKRLE---GEGYFVAPTVveEVPPKARIAQEEIFGPVLSVIRYkdDDFAEALEVANSTPYG 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1887644984 422 LTASVHGTeadlnKADSVIEAL-QYKVGRLIKNQMPTGvEVCGSMNHGGPFPSSTDVRSTsvGTNAMLRFMRP 493
Cdd:cd07083 429 LTGGVYSR-----KREHLEEARrEFHVGNLYINRKITG-ALVGVQPFGGFKLSGTNAKTG--GPHYLRRFLEM 493
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
6-444 |
2.48e-17 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 84.40 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 6 QSLVAGQWIGDSANGEFHAFSPARNE---ALPTrffnlSTAE-LNGAIEAAQSAFYQYR-----KTSFAQRADFLTCIAE 76
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEEtigDIPA-----ATAEdVDAAVEAARKAFKRNKgkdwaRTTGAVRAKYLRAIAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 77 QILVLGDELIEQTQQETNLPLARLQGERMRTVNQLKAFAS---ALRENPESPLGLkvvdeadvtraPLPKPHTELNYLPL 153
Cdd:PLN02467 84 KITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADlaeALDAKQKAPVSL-----------PMETFKGYVLKEPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 154 GPVAVFGASNFPYAFSTLggDTAAALAAGCPVIVKnhtahPGTGELMARAALAAI-KECAMPLGVFAMVQSKAYDISHQL 232
Cdd:PLN02467 153 GVVGLITPWNYPLLMATW--KVAPALAAGCTAVLK-----PSELASVTCLELADIcREVGLPPGVLNVVTGLGTEAGAPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 233 VAAPGIKAVGFTGSFNVASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQSKEMAQSLCqsmLMGNGQFCTSPGLW 312
Cdd:PLN02467 226 ASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSL--ELGGKSPIIVFDDVDLDKAVEWAMFGC---FWTNGQICSATSRL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 313 LVPTGCDE--LEAHITACINDAPSDTL-----LTP----GIVKTFKQQVEE-RSQFAQLSVLGK--GKLEQAFHANAHVF 378
Cdd:PLN02467 301 LVHERIASefLEKLVKWAKNIKISDPLeegcrLGPvvseGQYEKVLKFISTaKSEGATILCGGKrpEHLKKGFFIEPTII 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1887644984 379 ACnaddylTTPTLH---EEVFGPAALVVRYDSEQQLMILINKLQGQLTASVhgTEADLNKADSVIEALQ 444
Cdd:PLN02467 381 TD------VTTSMQiwrEEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAV--ISNDLERCERVSEAFQ 441
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
8-493 |
4.21e-17 |
|
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: 83.81 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 8 LVAGQWIGDSanGEFHAFSPARNEALPTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIE 87
Cdd:cd07124 36 VIGGKEVRTE--EKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 88 QTQQETNLPLARLQGERMRTVNQLKAFASALRENPESPLGlkvvdeadvtraPLPKPHTELNYLPLGPVAVFGASNFPYA 167
Cdd:cd07124 114 WMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVE------------MVPGEDNRYVYRPLGVGAVISPWNFPLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 168 FSTlgGDTAAALAAGCPVIVKNHTAHPGTGELMARaalaAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSF 247
Cdd:cd07124 182 ILA--GMTTAALVTGNTVVLKPAEDTPVIAAKLVE----ILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 248 NVASKLQETIAKREE----PIPFYGELGSINPQVILPNKAIEQSkemAQSLCQSMLMGNGQFCTSpglwlvptgCDELEA 323
Cdd:cd07124 256 EVGLRIYERAAKVQPgqkwLKRVIAEMGGKNAIIVDEDADLDEA---AEGIVRSAFGFQGQKCSA---------CSRVIV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 324 H-------------ITACINDAPS---DTLLTPGI----VKTFKQQVEERSQFAQLsVLGKGKLE---QAFHANAHVFac 380
Cdd:cd07124 324 HesvydeflerlveRTKALKVGDPedpEVYMGPVIdkgaRDRIRRYIEIGKSEGRL-LLGGEVLElaaEGYFVQPTIF-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 381 nADDYLTTPTLHEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHG-TEADLNKADSVIEalqykVGRLIKNQMPTGV 459
Cdd:cd07124 401 -ADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSrSPEHLERARREFE-----VGNLYANRKITGA 474
|
490 500 510
....*....|....*....|....*....|....
gi 1887644984 460 EVcGSMNHGGPFPSSTDvrSTSVGTNAMLRFMRP 493
Cdd:cd07124 475 LV-GRQPFGGFKMSGTG--SKAGGPDYLLQFMQP 505
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
25-444 |
5.97e-17 |
|
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: 83.16 E-value: 5.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 25 FSPARNEALpTRFFNLSTAELNGAIEAAQSAFyqyRKTSFAQ----RADFLTCIAEQILVLGDELIEQTQQETNLPLARL 100
Cdd:cd07120 2 IDPATGEVI-GTYADGGVAEAEAAIAAARRAF---DETDWAHdprlRARVLLELADAFEANAERLARLLALENGKILGEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 101 QGERMRTVNQLKAFASALRENPEsplglKVVDeadvtraPLPKPHTELNYLPLGPVAVFGASNFPYAFstLGGDTAAALA 180
Cdd:cd07120 78 RFEISGAISELRYYAGLARTEAG-----RMIE-------PEPGSFSLVLREPMGVAGIIVPWNSPVVL--LVRSLAPALA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 181 AGCPVIVKNHTAHPGTGELMARAaLAAIKecAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKR 260
Cdd:cd07120 144 AGCTVVVKPAGQTAQINAAIIRI-LAEIP--SLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 261 EEPIPFygELGSINPQVILPNKAIEQskeMAQSLCQSMLMGNGQFCTSPGLWLVPTG-CDELEAHITACI--------ND 331
Cdd:cd07120 221 LKRLGL--ELGGKTPCIVFDDADLDA---ALPKLERALTIFAGQFCMAGSRVLVQRSiADEVRDRLAARLaavkvgpgLD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 332 APSDtlLTPGIVKTFKQQVEER-----SQFAQLSVLGKGKLEQ----AFHANAHVfacnADDYLTTPTLHEEVFGPAALV 402
Cdd:cd07120 296 PASD--MGPLIDRANVDRVDRMveraiAAGAEVVLRGGPVTEGlakgAFLRPTLL----EVDDPDADIVQEEIFGPVLTL 369
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1887644984 403 VRYDSEQQLMILINKLQGQLTASVHGTeaDLNKADSVIEALQ 444
Cdd:cd07120 370 ETFDDEAEAVALANDTDYGLAASVWTR--DLARAMRVARAIR 409
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
16-474 |
7.33e-17 |
|
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: 82.76 E-value: 7.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 16 DSANGEFHAFSPARnealptrffnlSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNL 95
Cdd:cd07092 3 DPATGEEIATVPDA-----------SAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 96 PLA-RLQGERMRTVNQLKAFASALRENPESPLGLKVVDEADVTRAPlpkphtelnylPLGPVAVFGASNFPYAFSTLggD 174
Cdd:cd07092 72 PLHlVRDDELPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRRE-----------PIGVVAQIAPWNYPLMMAAW--K 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 175 TAAALAAGCPVIVKnhtahPGTGELMARAALAAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQ 254
Cdd:cd07092 139 IAPALAAGNTVVLK-----PSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 255 ETIA---KReepipFYGELGSINPQVILPNKAIEqskEMAQSLCQSMLMGNGQFCTSPGLWLVPTGC-DELEAHITAC-- 328
Cdd:cd07092 214 RAAAdtlKR-----VHLELGGKAPVIVFDDADLD---AAVAGIATAGYYNAGQDCTAACRVYVHESVyDEFVAALVEAvs 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 329 ---IND-APSDTLLTPGIVKTFKQQV----EERSQFAQLSVLGKGKLEQAFHANAHVFA-CNADDYLTTptlhEEVFGPA 399
Cdd:cd07092 286 airVGDpDDEDTEMGPLNSAAQRERVagfvERAPAHARVLTGGRRAEGPGYFYEPTVVAgVAQDDEIVQ----EEIFGPV 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887644984 400 ALVVRYDSEQQLMILINKLQGQLTASVHGTeaDLNKADSVIEALQYKVgRLIKNQMPTGVEvcgsMNHGGpFPSS 474
Cdd:cd07092 362 VTVQPFDDEDEAIELANDVEYGLASSVWTR--DVGRAMRLSARLDFGT-VWVNTHIPLAAE----MPHGG-FKQS 428
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
40-444 |
9.74e-17 |
|
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: 82.35 E-value: 9.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 40 LSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPL--ARLqGERMRTVNQLKAFAS- 116
Cdd:cd07098 15 DTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMvdASL-GEILVTCEKIRWTLKh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 117 ---ALRenPESplglkvvdeadvTRAPLPKPH--TELNYLPLGPVAVFGASNFPyaFSTLGGDTAAALAAGCPVIVK--N 189
Cdd:cd07098 94 gekALR--PES------------RPGGLLMFYkrARVEYEPLGVVGAIVSWNYP--FHNLLGPIIAALFAGNAIVVKvsE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 190 HTAHpgTGELMARAALAAIKECAMPLGVFAMVQSKAYDISHqLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIPFygE 269
Cdd:cd07098 158 QVAW--SSGFFLSIIRECLAACGHDPDLVQLVTCLPETAEA-LTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVL--E 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 270 LGSINPQVILPNKAIEQskeMAQSLCQSMLMGNGQFCTSPGLWLVPTG-----CDELEAHITACINDAPSD------TLL 338
Cdd:cd07098 233 LGGKDPAIVLDDADLDQ---IASIIMRGTFQSSGQNCIGIERVIVHEKiydklLEILTDRVQALRQGPPLDgdvdvgAMI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 339 TPGIVKTFKQQVEER-SQFAQLsvLGKGKLEQAF-HANAHVFacnaddyltTPTL-----------HEEVFGPAALVVRY 405
Cdd:cd07098 310 SPARFDRLEELVADAvEKGARL--LAGGKRYPHPeYPQGHYF---------PPTLlvdvtpdmkiaQEEVFGPVMVVMKA 378
|
410 420 430
....*....|....*....|....*....|....*....
gi 1887644984 406 DSEQQLMILINKLQGQLTASVHGteADLNKADSVIEALQ 444
Cdd:cd07098 379 SDDEEAVEIANSTEYGLGASVFG--KDIKRARRIASQLE 415
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
6-472 |
1.54e-16 |
|
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: 81.93 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 6 QSLVAGQWIG---------DSANGEFHAFspARNEALPTRffnlstAELNGAIEAAQSAFyqyRKTSFAQRADFLTCIAE 76
Cdd:cd07128 2 QSYVAGQWHAgtgdgrtlhDAVTGEVVAR--VSSEGLDFA------AAVAYAREKGGPAL---RALTFHERAAMLKALAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 77 QILVLGDELIEqtqqetnlpLARLQGERMRT--------VNQLKAFASALRENPESPlglKVVDEADVTraPLPKPHTEL 148
Cdd:cd07128 71 YLMERKEDLYA---------LSAATGATRRDswididggIGTLFAYASLGRRELPNA---HFLVEGDVE--PLSKDGTFV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 149 N---YLPLGPVAVF-GASNFPyAFSTLGgDTAAALAAGCPVIVKNHTAhpgTGELmARAALAAIKECA-MPLGVFAMVQS 223
Cdd:cd07128 137 GqhiLTPRRGVAVHiNAFNFP-VWGMLE-KFAPALLAGVPVIVKPATA---TAYL-TEAVVKDIVESGlLPEGALQLICG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 224 KAYDISHQLvaaPGIKAVGFTGSFNVASKLQETIAKREEPIPFYGELGSINPQVILPnKAIEQSKEMA---QSLCQSMLM 300
Cdd:cd07128 211 SVGDLLDHL---GEQDVVAFTGSAATAAKLRAHPNIVARSIRFNAEADSLNAAILGP-DATPGTPEFDlfvKEVAREMTV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 301 GNGQFCTSPGLWLVPTG-CDELEAHITACINDA----PSDTLLTPGIVKTFKQQVEERSQFAQLS--------------V 361
Cdd:cd07128 287 KAGQKCTAIRRAFVPEArVDAVIEALKARLAKVvvgdPRLEGVRMGPLVSREQREDVRAAVATLLaeaevvfggpdrfeV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 362 LGKGKLEQAFHAnAHVFACnaDDYLTTPTLHE-EVFGPAALVVRYDSEQQLMILINKLQGQLTASVHgTEADLNKADSVI 440
Cdd:cd07128 367 VGADAEKGAFFP-PTLLLC--DDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVV-TNDPAFARELVL 442
|
490 500 510
....*....|....*....|....*....|..
gi 1887644984 441 EALQYkVGRLIKNQMPTGVEvcgSMNHGGPFP 472
Cdd:cd07128 443 GAAPY-HGRLLVLNRDSAKE---STGHGSPLP 470
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
48-457 |
1.91e-16 |
|
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: 81.49 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 48 AIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERMRTVNQLKaFAS--ALRENPE-- 123
Cdd:cd07149 26 AIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLR-LSAeeAKRLAGEti 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 124 ----SPLGLKVVdeADVTRAPLpkphtelnylplGPVAVFGASNFPyaFSTLGGDTAAALAAGCPVIVKNHTAHPGTGEL 199
Cdd:cd07149 105 pfdaSPGGEGRI--GFTIREPI------------GVVAAITPFNFP--LNLVAHKVGPAIAAGNAVVLKPASQTPLSALK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 200 MARAALaaikECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIpfygELGSINPQVIL 279
Cdd:cd07149 169 LAELLL----EAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLKKVTL----ELGSNAAVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 280 PNKAIEQSkemAQSLCQSMLMGNGQFCTSPGLWLVPTG-----CDELEAHITACINDAPSD--TLLTPGIVKTFKQQVEE 352
Cdd:cd07149 241 ADADLEKA---VERCVSGAFANAGQVCISVQRIFVHEDiydefLERFVAATKKLVVGDPLDedTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 353 RSQFAQLS---VLGKGKLEQAFHANAHVFACNADDYLTtptlHEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGT 429
Cdd:cd07149 318 WVEEAVEGgarLLTGGKRDGAILEPTVLTDVPPDMKVV----CEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTN 393
|
410 420
....*....|....*....|....*...
gi 1887644984 430 eaDLNKADSVIEALQykVGRLIKNQMPT 457
Cdd:cd07149 394 --DLQKALKAARELE--VGGVMINDSST 417
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
41-444 |
1.93e-16 |
|
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: 81.44 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 41 STAELNGAIEAAQSAFYQ--YRKTSFAQRADFLTCIAEQILVLGDELIE-QTQQEtnlplARLQGErmrTVNQLKAFASA 117
Cdd:cd07114 17 SAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAElETRDN-----GKLIRE---TRAQVRYLAEW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 118 LRENPesplGLKVVDEADVTraPLPKPHTeLNYL---PLGPVAVFGASNFPYAFSTLggDTAAALAAGCPVIVKNHTAHP 194
Cdd:cd07114 89 YRYYA----GLADKIEGAVI--PVDKGDY-LNFTrrePLGVVAAITPWNSPLLLLAK--KLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 195 GTGELMARAALAAikecAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIPFygELGSIN 274
Cdd:cd07114 160 ASTLELAKLAEEA----GFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTL--ELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 275 PQVILPNKAIEQSkemAQSLCQSMLMGNGQFCTSPGLWLVPTGC-DE-LEAHITAC----INDaPSDTLLTPGIVKTFKQ 348
Cdd:cd07114 234 PNIVFDDADLDAA---VNGVVAGIFAAAGQTCVAGSRLLVQRSIyDEfVERLVARArairVGD-PLDPETQMGPLATERQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 349 --QVEE-----RSQFAQLsVLGKGKLEQAFHANAH-----VFACNADDYlttPTLHEEVFGPAALVVRYDSEQQLMILIN 416
Cdd:cd07114 310 leKVERyvaraREEGARV-LTGGERPSGADLGAGYffeptILADVTNDM---RIAQEEVFGPVLSVIPFDDEEEAIALAN 385
|
410 420
....*....|....*....|....*...
gi 1887644984 417 KLQGQLTASVHgTEaDLNKADSVIEALQ 444
Cdd:cd07114 386 DSEYGLAAGIW-TR-DLARAHRVARAIE 411
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
41-427 |
2.06e-16 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 82.71 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 41 STAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEqilvlgdeLIE-QTQQETNLpLARLQGermrtvnqlKAFASALR 119
Cdd:PRK11809 680 TPAEVEQALESAVNAAPIWFATPPAERAAILERAAD--------LMEaQMQTLMGL-LVREAG---------KTFSNAIA 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 120 ENPESplglkvVD----EADVTRAPLpkphTELNYLPLGPVAVFGASNFPYAFSTlgGDTAAALAAGCPVIVKNHTAHPg 195
Cdd:PRK11809 742 EVREA------VDflryYAGQVRDDF----DNDTHRPLGPVVCISPWNFPLAIFT--GQVAAALAAGNSVLAKPAEQTP- 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 196 tgeLMARAALAAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREE----PIPFYGELG 271
Cdd:PRK11809 809 ---LIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDpqgrPIPLIAETG 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 272 SINPQVILPNKAIEQskeMAQSLCQSMLMGNGQFCTSpgLWLVptgC--DELEAHITACINDAPS-------DTLLT--- 339
Cdd:PRK11809 886 GQNAMIVDSSALTEQ---VVADVLASAFDSAGQRCSA--LRVL---ClqDDVADRTLKMLRGAMAecrmgnpDRLSTdig 957
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 340 PGIVKTFKQQVEERSQfaqlSVLGKG-KLEQAFHANAhvfacnADDYLTT---PTLHE---------EVFGPAALVVRYD 406
Cdd:PRK11809 958 PVIDAEAKANIERHIQ----AMRAKGrPVFQAARENS------EDWQSGTfvpPTLIEldsfdelkrEVFGPVLHVVRYN 1027
|
410 420
....*....|....*....|...
gi 1887644984 407 SEQ--QLMILINKLQGQLTASVH 427
Cdd:PRK11809 1028 RNQldELIEQINASGYGLTLGVH 1050
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
26-458 |
6.51e-16 |
|
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: 79.69 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 26 SPArNEALPTRFFNLSTAELNGAIEAAQSAFYQ--YRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGE 103
Cdd:cd07118 3 SPA-HGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 104 RMRTVNQLKAFASALR-------EN-PESPLGLkVVDEadvtraplpkphtelnylPLGPVAVFGASNFPyaFSTLGGDT 175
Cdd:cd07118 82 IEGAADLWRYAASLARtlhgdsyNNlGDDMLGL-VLRE------------------PIGVVGIITPWNFP--FLILSQKL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 176 AAALAAGCPVIVKNHTAHPGT----GELMARAALaaikecamPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVAS 251
Cdd:cd07118 141 PFALAAGCTVVVKPSEFTSGTtlmlAELLIEAGL--------PAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 252 KLQETIAKREEPIPFygELGSINPQVILPNKAIEQSKEMAqslcqsmLMG----NGQFCTSPGLWLV------------- 314
Cdd:cd07118 213 AIAAAAARNLKKVSL--ELGGKNPQIVFADADLDAAADAV-------VFGvyfnAGECCNSGSRLLVhesiadafvaavv 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 315 ------PTGcDEL--EAHITACINDAPSDTLLtpGIVKtfkqqvEERSQFAQLsVLGKGKLEqafHANAHVFAcnaddyl 386
Cdd:cd07118 284 arsrkvRVG-DPLdpETKVGAIINEAQLAKIT--DYVD------AGRAEGATL-LLGGERLA---SAAGLFYQ------- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 387 ttPTL-----------HEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGTeaDLNKADSVIEALqyKVGRLIKN-- 453
Cdd:cd07118 344 --PTIftdvtpdmaiaREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSK--DIDTALTVARRI--RAGTVWVNtf 417
|
490
....*....|
gi 1887644984 454 -----QMPTG 458
Cdd:cd07118 418 ldgspELPFG 427
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
43-457 |
3.68e-14 |
|
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: 74.59 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 43 AELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERMRTVNQLKAFASALRENP 122
Cdd:cd07147 21 DDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATRIY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 123 ESPLGLKVVDEADVTRAPLPKphtelnyLPLGPVAVFGASNFPyaFSTLGGDTAAALAAGCPVIVKNHTAHPGTGELMAR 202
Cdd:cd07147 101 GEVLPLDISARGEGRQGLVRR-------FPIGPVSAITPFNFP--LNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 203 aalaAIKECAMPLGVFAMVQSKAyDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIpfygELGSINPQVILPN- 281
Cdd:cd07147 172 ----VLAETGLPKGAFSVLPCSR-DDADLLVTDERIKLLSFTGSPAVGWDLKARAGKKKVVL----ELGGNAAVIVDSDa 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 282 ---KAIEQSKEMAQSLCqsmlmgnGQFCTSPGLWLVPTGC-----DELEAHITACINDAPSD--TLLTPGIVKTFKQQVE 351
Cdd:cd07147 243 dldFAAQRIIFGAFYQA-------GQSCISVQRVLVHRSVydefkSRLVARVKALKTGDPKDdaTDVGPMISESEAERVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 352 ersqfaqlsvlgkGKLEQAFHANAHVFACNA-DDYLTTPTL-----------HEEVFGPAALVVRYDSEQQLMILINKLQ 419
Cdd:cd07147 316 -------------GWVNEAVDAGAKLLTGGKrDGALLEPTIledvppdmevnCEEVFGPVVTVEPYDDFDEALAAVNDSK 382
|
410 420 430
....*....|....*....|....*....|....*...
gi 1887644984 420 GQLTASVHgtEADLNKADSVIEALQykVGRLIKNQMPT 457
Cdd:cd07147 383 FGLQAGVF--TRDLEKALRAWDELE--VGGVVINDVPT 416
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
27-306 |
3.87e-14 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 74.39 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 27 PARNEALPTrFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERMR 106
Cdd:PRK09406 8 PATGETVKT-FTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 107 TVNQLKAFAsalrENPESPLGLKVVDEADV--TRAplpkphtELNYLPLGPVAVFGASNFPY----AFStlggdtAAALA 180
Cdd:PRK09406 87 CAKGFRYYA----EHAEALLADEPADAAAVgaSRA-------YVRYQPLGVVLAVMPWNFPLwqvvRFA------APALM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 181 AGCPVIVKNHTAHPGT----GELMARAALaaikecamPLGVFA--MVQSKAYDishQLVAAPGIKAVGFTGSfNVASKLQ 254
Cdd:PRK09406 150 AGNVGLLKHASNVPQTalylADLFRRAGF--------PDGCFQtlLVGSGAVE---AILRDPRVAAATLTGS-EPAGRAV 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1887644984 255 ETIAKREEPiPFYGELGSINPQVILPNKAIEQSKEMA-QSLCQSmlmgNGQFC 306
Cdd:PRK09406 218 AAIAGDEIK-KTVLELGGSDPFIVMPSADLDRAAETAvTARVQN----NGQSC 265
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
41-443 |
4.15e-14 |
|
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: 74.25 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 41 STAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERMRTVNQLKAfASALre 120
Cdd:cd07152 11 DAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHE-AAGL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 121 nPESPLGLKvvdeadvtrapLPKPHTELNY---LPLGPVAVFGASNFPYAFSTLGgdTAAALAAGCPVIVKNHTAHPGTG 197
Cdd:cd07152 88 -PTQPQGEI-----------LPSAPGRLSLarrVPLGVVGVISPFNFPLILAMRS--VAPALALGNAVVLKPDPRTPVSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 198 ELMaraaLAAIKECA-MPLGVFAMVQSKAyDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIPFygELGSINPQ 276
Cdd:cd07152 154 GVV----IARLFEEAgLPAGVLHVLPGGA-DAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSL--ELGGKNAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 277 VILPNKAIEQSkemAQSLCQSMLMGNGQFCTSPGLWLVPTG-CDELEAHITACI------NDAPSDTLLTPGIVKTFKQQ 349
Cdd:cd07152 227 IVLDDADLDLA---ASNGAWGAFLHQGQICMAAGRHLVHESvADAYTAKLAAKAkhlpvgDPATGQVALGPLINARQLDR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 350 VE---ERSQFAQLSVLGKGKLEQAFHAN---AHVFACNaddylttPTLHEEVFGPAALVVRYDSEQQLMILINKLQGQLT 423
Cdd:cd07152 304 VHaivDDSVAAGARLEAGGTYDGLFYRPtvlSGVKPGM-------PAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLS 376
|
410 420
....*....|....*....|
gi 1887644984 424 ASVHGteADLNKADSVIEAL 443
Cdd:cd07152 377 AGIIS--RDVGRAMALADRL 394
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
9-443 |
1.72e-13 |
|
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: 72.34 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 9 VAGQWIgDSANGEFHA-FSPArNEALPTRFFNLSTAELNGAIEAAQSAFYQ--YRKTSFAQRADFLTCIAEQILVLGDEL 85
Cdd:cd07119 2 IDGEWV-EAASGKTRDiINPA-NGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 86 IEQTQQETNLPLARLQGERMRTVNQLKAFAsalrenpesplGLKVVDEADVTRAPlpkPHTELNYL--PLGPVAVFGASN 163
Cdd:cd07119 80 ARLETLNTGKTLRESEIDIDDVANCFRYYA-----------GLATKETGEVYDVP---PHVISRTVrePVGVCGLITPWN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 164 FPYAFSTLggDTAAALAAGCPVIVKNHTAHPgtgeLMARAALAAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGF 243
Cdd:cd07119 146 YPLLQAAW--KLAPALAAGNTVVIKPSEVTP----LTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 244 TGSFNVASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQSKEMAQSlcqSMLMGNGQFCTSPGLWLVP-TGCDELE 322
Cdd:cd07119 220 TGGTATGRSIMRAAAGNVKKVAL--ELGGKNPNIVFADADFETAVDQALN---GVFFNAGQVCSAGSRLLVEeSIHDKFV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 323 AHITACI------NDAPSDTLLTPGIVKTFKQQVEE-----RSQFAQLSVLGKGKLEQAFhanahvfacnADDYLTTPTL 391
Cdd:cd07119 295 AALAERAkkiklgNGLDADTEMGPLVSAEHREKVLSyiqlgKEEGARLVCGGKRPTGDEL----------AKGYFVEPTI 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1887644984 392 -----------HEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHgtEADLNKADSVIEAL 443
Cdd:cd07119 365 fddvdrtmrivQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVW--TKDIARANRVARRL 425
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
9-444 |
2.67e-13 |
|
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: 71.79 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 9 VAGQWIGDSANGEFHAFSPArNEALPTRFFNLSTAELNGAIEAAQSAFYQY--RKTSFAQRADFLTCIAEqilvlgdeLI 86
Cdd:cd07143 11 INGEFVDSVHGGTVKVYNPS-TGKLITKIAEATEADVDIAVEVAHAAFETDwgLKVSGSKRGRCLSKLAD--------LM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 87 EQTQQEtnlpLARLQgermrTVNQLKAFASALRenpesplgLKVVDEADVTR---APLPKPH--------TELNYLPLGP 155
Cdd:cd07143 82 ERNLDY----LASIE-----ALDNGKTFGTAKR--------VDVQASADTFRyygGWADKIHgqvietdiKKLTYTRHEP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 156 VAVFGAS---NFPyaFSTLGGDTAAALAAGCPVIVKNHTAHPgtgeLMARAALAAIKECAMPLGVFAMVQSKAYDISHQL 232
Cdd:cd07143 145 IGVCGQIipwNFP--LLMCAWKIAPALAAGNTIVLKPSELTP----LSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 233 VAAPGIKAVGFTGSFNVASKLQETIAKRE-EPIPFygELGSINPQVILPNKAIEQSKEMAQslcQSMLMGNGQFCTSPGL 311
Cdd:cd07143 219 SSHMDIDKVAFTGSTLVGRKVMEAAAKSNlKKVTL--ELGGKSPNIVFDDADLESAVVWTA---YGIFFNHGQVCCAGSR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 312 WLVPTGCdeLEAHITACINDAPSDTLLTPGIVKTFKQQVEERSQFAQ-LSVLGKGKLEQafhANAHVFA--CNADDYLTT 388
Cdd:cd07143 294 IYVQEGI--YDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERiMSYIESGKAEG---ATVETGGkrHGNEGYFIE 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1887644984 389 PTL-----------HEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHgtEADLNKADSVIEALQ 444
Cdd:cd07143 369 PTIftdvtedmkivKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVF--TNNINNAIRVANALK 433
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
48-274 |
3.22e-13 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 72.59 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 48 AIEAAQSAFYQYRKTSFAQRADFLTCIAEqilvlgdeLIEQTQQETNLPLARLQGermrtvnqlKAFASALRENPESplg 127
Cdd:PRK11905 595 ALAAAQAAFPEWSATPAAERAAILERAAD--------LMEAHMPELFALAVREAG---------KTLANAIAEVREA--- 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 128 lkvVD-----EADVTRAPLPKPHtelnyLPLGPVAVFGASNFPYAFSTlgGDTAAALAAGCPVIVKNHTAHPgtgeLMAR 202
Cdd:PRK11905 655 ---VDflryyAAQARRLLNGPGH-----KPLGPVVCISPWNFPLAIFT--GQIAAALVAGNTVLAKPAEQTP----LIAA 720
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1887644984 203 AALAAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKR-EEPIPFYGELGSIN 274
Cdd:PRK11905 721 RAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRsGPPVPLIAETGGQN 793
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
12-274 |
7.14e-13 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 71.38 E-value: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 12 QWIG---DSANGEFHA-FSPA--RNEALPTRFFNLSTAELngAIEAAQSAFYQYRKTSFAQRADFLTCIAEqilvlgdeL 85
Cdd:PRK11904 550 QWQAgpiINGEGEARPvVSPAdrRRVVGEVAFADAEQVEQ--ALAAARAAFPAWSRTPVEERAAILERAAD--------L 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 86 IEQTQQETnlpLARLQGERMRTVnqlkafASALREnpesplglkvVDEA-DVTR-----------AP--LPKPHTELNYL 151
Cdd:PRK11904 620 LEANRAEL---IALCVREAGKTL------QDAIAE----------VREAvDFCRyyaaqarrlfgAPekLPGPTGESNEL 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 152 PLGPVAVFGA-S--NFPYAFSTlgGDTAAALAAGCPVIVKnhtahPG--TGeLMARAALAAIKECAMPLGVFAMVQSKAY 226
Cdd:PRK11904 681 RLHGRGVFVCiSpwNFPLAIFL--GQVAAALAAGNTVIAK-----PAeqTP-LIAAEAVKLLHEAGIPKDVLQLLPGDGA 752
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1887644984 227 DISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPI-PFYGELGSIN 274
Cdd:PRK11904 753 TVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIvPLIAETGGQN 801
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
46-456 |
2.64e-12 |
|
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: 68.54 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 46 NGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERMRTVNQLKAFASALRENPESP 125
Cdd:cd07146 21 EALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRDDGES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 126 LGLKVVDEADVTRA-PLPKphtelnylPLGPVAVFGASNFPyaFSTLGGDTAAALAAGCPVIVKNHTAHPgtgeLMARAA 204
Cdd:cd07146 101 FSCDLTANGKARKIfTLRE--------PLGVVLAITPFNHP--LNQVAHKIAPAIAANNRIVLKPSEKTP----LSAIYL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 205 LAAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIpfygELGSINPQVILPNKAI 284
Cdd:cd07146 167 ADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQLL----ELGGNDPLIVMDDADL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 285 EQSKEMAQSLCQSmlmGNGQFCTSPGLWLVPTGC-----DELEAHITACINDAP--SDTLLTPGIVKTFKQQVE---ERS 354
Cdd:cd07146 243 ERAATLAVAGSYA---NSGQRCTAVKRILVHESVadefvDLLVEKSAALVVGDPmdPATDMGTVIDEEAAIQIEnrvEEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 355 QFAQLSVLGKGKLEQAFHANA---HVfacNADDYLTTptlhEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVhgTEA 431
Cdd:cd07146 320 IAQGARVLLGNQRQGALYAPTvldHV---PPDAELVT----EETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV--CTN 390
|
410 420
....*....|....*....|....*
gi 1887644984 432 DLNKADSVIEALqyKVGRLIKNQMP 456
Cdd:cd07146 391 DLDTIKRLVERL--DVGTVNVNEVP 413
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
15-274 |
2.73e-12 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 69.58 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 15 GDSANGEFHA-FSPA-RNEALPTRFFnLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEqilvlgdeLIEQTQQE 92
Cdd:COG4230 564 GEAASGEARPvRNPAdHSDVVGTVVE-ATAADVEAALAAAQAAFPAWSATPVEERAAILERAAD--------LLEAHRAE 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 93 tnLpLARLQGERMRTvnqlkaFASAL---REnpesplglkVVD-------EAdvtRAPLPKPHTelnYLPLGPVAVFGAS 162
Cdd:COG4230 635 --L-MALLVREAGKT------LPDAIaevRE---------AVDfcryyaaQA---RRLFAAPTV---LRGRGVFVCISPW 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 163 NFPYAFSTlgGDTAAALAAGCPVIVKnhtahPGtgE---LMARAALAAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIK 239
Cdd:COG4230 691 NFPLAIFT--GQVAAALAAGNTVLAK-----PA--EqtpLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIA 761
|
250 260 270
....*....|....*....|....*....|....*.
gi 1887644984 240 AVGFTGSFNVASKLQETIAKRE-EPIPFYGELGSIN 274
Cdd:COG4230 762 GVAFTGSTETARLINRTLAARDgPIVPLIAETGGQN 797
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
11-444 |
4.54e-12 |
|
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: 68.20 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 11 GQWIGDSANGEFHAFSPArNEALPTRFFNLSTAELNGAIEAAQSAFYQ-YRKTSFAQRADFLTCIAEqilvlgdeLIEQt 89
Cdd:cd07144 14 NEFVKSSDGETIKTVNPS-TGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLAD--------LVEK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 90 QQETnlpLARLQgermrTVNQLKAFASALRENpesplglkvVDE-----------AD-VTRAPLPKPHTELNYL---PLG 154
Cdd:cd07144 84 NRDL---LAAIE-----ALDSGKPYHSNALGD---------LDEiiaviryyagwADkIQGKTIPTSPNKLAYTlhePYG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 155 PVAVFGASNFPYAFstLGGDTAAALAAGCPVIVKnhTAHPGTGELMARAALaaIKECAMPLGVFAMVQSKAYDISHQLVA 234
Cdd:cd07144 147 VCGQIIPWNYPLAM--AAWKLAPALAAGNTVVIK--PAENTPLSLLYFANL--VKEAGFPPGVVNIIPGYGAVAGSALAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 235 APGIKAVGFTGSFNVASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQskemAQSLCQSMLMGN-GQFCTSPGLWL 313
Cdd:cd07144 221 HPDVDKIAFTGSTATGRLVMKAAAQNLKAVTL--ECGGKSPALVFEDADLDQ----AVKWAAAGIMYNsGQNCTATSRIY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 314 VPTGC-DELEAHITACINDA-------PSDTLLTPGIVKTFKQQV-----EERSQFAQLSVLGKGK---LEQAFHANAHV 377
Cdd:cd07144 295 VQESIyDKFVEKFVEHVKQNykvgspfDDDTVVGPQVSKTQYDRVlsyieKGKKEGAKLVYGGEKApegLGKGYFIPPTI 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887644984 378 FA-CNADDYLttptLHEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHgTEaDLNKADSVIEALQ 444
Cdd:cd07144 375 FTdVPQDMRI----VKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVF-TK-DIRRAHRVARELE 436
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
27-259 |
6.96e-12 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 67.65 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 27 PARNEALPTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARLQGERMR 106
Cdd:PRK03137 57 PANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 107 TVNQLKAFA-SALRENPESPLglkvvdeadvtrAPLPKPHTELNYLPLGPVAVFGASNFPYAFSTlgGDTAAALAAGCPV 185
Cdd:PRK03137 137 AIDFLEYYArQMLKLADGKPV------------ESRPGEHNRYFYIPLGVGVVISPWNFPFAIMA--GMTLAAIVAGNTV 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887644984 186 IVKNHTAHPGTGELMARaalaAIKECAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAK 259
Cdd:PRK03137 203 LLKPASDTPVIAAKFVE----VLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAK 272
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
8-260 |
7.13e-12 |
|
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: 67.23 E-value: 7.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 8 LVAGQWIGDSanGEFHAFSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADfltcIAEQIlvlGDELIE 87
Cdd:cd07130 2 VYDGEWGGGG--GVVTSISPANGEPI-ARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGE----IVRQI---GDALRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 88 QTQqetnlPLARLQGERMRtvnqlKAFASALRENPEsplglkVVDEAD----VTRA------PLPKP-HTEL-NYLPLGP 155
Cdd:cd07130 72 KKE-----ALGKLVSLEMG-----KILPEGLGEVQE------MIDICDfavgLSRQlygltiPSERPgHRMMeQWNPLGV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 156 VAVFGASNFPYAfsTLGGDTAAALAAGCPVIVKNHTAHPGTGELMARAALAAIKECAMPLGVFAMVQSKAyDISHQLVAA 235
Cdd:cd07130 136 VGVITAFNFPVA--VWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGA-DVGEALVKD 212
|
250 260
....*....|....*....|....*
gi 1887644984 236 PGIKAVGFTGSFNVASKLQETIAKR 260
Cdd:cd07130 213 PRVPLVSFTGSTAVGRQVGQAVAAR 237
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
152-444 |
1.24e-11 |
|
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: 66.73 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 152 PLGPVAVFGASNFPyafsTLGGDTA--AALAAGCPVIVKnhtAHPGTGELMA---RAALAAIKECAM-PLGVFAMVQSKA 225
Cdd:cd07127 193 PRGVALVIGCSTFP----TWNGYPGlfASLATGNPVIVK---PHPAAILPLAitvQVAREVLAEAGFdPNLVTLAADTPE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 226 YDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREepipFYGELGSINPQVIlpnKAIEQSKEMAQSLCQSMLMGNGQF 305
Cdd:cd07127 266 EPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ----VYTEKAGVNTVVV---DSTDDLKAMLRNLAFSLSLYSGQM 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 306 CTSPGLWLVP----------TGCDELEAHITACINDAPSD----TLLTPGIV-KTFKQQVEERSQFAQLSVLGKgKLEQA 370
Cdd:cd07127 339 CTTPQNIYVPrdgiqtddgrKSFDEVAADLAAAIDGLLADparaAALLGAIQsPDTLARIAEARQLGEVLLASE-AVAHP 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 371 FHANAHV-----FACNADDyltTPTLHEEVFGPAALVVRYDSEQQLMILINKL---QGQLTASVHGTEADlnkadsVIEA 442
Cdd:cd07127 418 EFPDARVrtpllLKLDASD---EAAYAEERFGPIAFVVATDSTDHSIELARESvreHGAMTVGVYSTDPE------VVER 488
|
..
gi 1887644984 443 LQ 444
Cdd:cd07127 489 VQ 490
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
152-470 |
1.51e-11 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 66.65 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 152 PLGPVAVF-GASNFPyAFStLGGDTAAALAAGCPVIVKNHTAhpgTGELMARAALAAIKECAMPLGVFAMVQSKAYDISH 230
Cdd:PRK11903 147 PTRGVALFiNAFNFP-AWG-LWEKAAPALLAGVPVIVKPATA---TAWLTQRMVKDVVAAGILPAGALSVVCGSSAGLLD 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 231 QLvaaPGIKAVGFTGSFNVASKLQETIAKREEPIPFYGELGSINPQVILPNKA--IEQSKEMAQSLCQSMLMGNGQFCTS 308
Cdd:PRK11903 222 HL---QPFDVVSFTGSAETAAVLRSHPAVVQRSVRVNVEADSLNSALLGPDAApgSEAFDLFVKEVVREMTVKSGQKCTA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 309 PGLWLVPTG-----CDELEAHITACINDAPSDTLLTPGIVKTFKQQVEERSQFAQLS----VLGKGKLEQAFHANAHVFA 379
Cdd:PRK11903 299 IRRIFVPEAlydavAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRaqaeVLFDGGGFALVDADPAVAA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 380 C------NADDYLTTPTLHE-EVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGTEAD------LNKADS-----VIE 441
Cdd:PRK11903 379 CvgptllGASDPDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAflaaaaLELADShgrvhVIS 458
|
330 340 350
....*....|....*....|....*....|..
gi 1887644984 442 AlqyKVGRLIK---NQMPTGVevcgsmnHGGP 470
Cdd:PRK11903 459 P---DVAALHTghgNVMPQSL-------HGGP 480
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
3-259 |
3.73e-11 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 64.93 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 3 LTGQSLVAGQWIgDSANGEFHAFSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLG 82
Cdd:PRK13473 1 MQTKLLINGELV-AGEGEKQPVYNPATGEVL-AEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 83 DELIEQTQQETNLPL-ARLQGERMRTVNQLKAFASALRENPESPLGLKVVDeadvtraplpkpHTelNYL---PLGPVAV 158
Cdd:PRK13473 79 DEFARLESLNCGKPLhLALNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEG------------HT--SMIrrdPVGVVAS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 159 FGASNFPYAFSTLggDTAAALAAGCPVIVKNHTAHPGTGELMARAAlaaiKEcAMPLGVFAMVQSKAYDISHQLVAAPGI 238
Cdd:PRK13473 145 IAPWNYPLMMAAW--KLAPALAAGNTVVLKPSEITPLTALKLAELA----AD-ILPPGVLNVVTGRGATVGDALVGHPKV 217
|
250 260
....*....|....*....|.
gi 1887644984 239 KAVGFTGSFNVASKLQETIAK 259
Cdd:PRK13473 218 RMVSLTGSIATGKHVLSAAAD 238
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
41-308 |
9.08e-11 |
|
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: 63.87 E-value: 9.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 41 STAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNlplarlqgermrtvnqlKAFASALRE 120
Cdd:cd07101 16 TPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETG-----------------KARRHAFEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 121 npesplglkVVDEADVTR-----AP-LPKPH-----------TELNYLPLGPVAVFGASNFPYAFSTlgGDTAAALAAGC 183
Cdd:cd07101 79 ---------VLDVAIVARyyarrAErLLKPRrrrgaipvltrTTVNRRPKGVVGVISPWNYPLTLAV--SDAIPALLAGN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 184 PVIVKNHTAHPGTGELMARAALaaikECAMPLGVFAMVQSKAYDISHQLVAapGIKAVGFTGSFNVASKLQETIAKREep 263
Cdd:cd07101 148 AVVLKPDSQTALTALWAVELLI----EAGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRRL-- 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1887644984 264 IPFYGELGSINPQVILPNKAIEQSKEMAQSLCQSmlmGNGQFCTS 308
Cdd:cd07101 220 IGCSLELGGKNPMIVLEDADLDKAAAGAVRACFS---NAGQLCVS 261
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
11-444 |
8.39e-10 |
|
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: 60.69 E-value: 8.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 11 GQWIgDSANGE-FHAFSPArNEALPTRFFNLSTAELNGAIEAAQSAFYQ--YRKTSFAQRADFLTCIAEqilvlgdeLIE 87
Cdd:cd07091 10 NEFV-DSVSGKtFPTINPA-TEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLAD--------LIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 88 QTQQEtnlpLARLQgermrTVNQLKAFASALRenpesplglkvVDEADVTRA----------------PLPKPHteLNYL 151
Cdd:cd07091 80 RDRDE----LAALE-----SLDNGKPLEESAK-----------GDVALSIKClryyagwadkiqgktiPIDGNF--LAYT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 152 PLGPVAVFGAS---NFP---YAFSTlggdtAAALAAGCPVIVKNHTAHPGTGELMARaalaAIKECAMPLGVFAMVQSKA 225
Cdd:cd07091 138 RREPIGVCGQIipwNFPllmLAWKL-----APALAAGNTVVLKPAEQTPLSALYLAE----LIKEAGFPPGVVNIVPGFG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 226 YDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKRE-EPIPFygELGSINPQVILPNKAIEQSKEMAQslcQSMLMGNGQ 304
Cdd:cd07091 209 PTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNlKKVTL--ELGGKSPNIVFDDADLDKAVEWAA---FGIFFNQGQ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 305 FCTSPGLWLVPTGC-DELEAHITACINDA----PSDTlltpgivKTFKQQVEERSQFAQ-LSVLGKGKLEQA--FHANAH 376
Cdd:cd07091 284 CCCAGSRIFVQESIyDEFVEKFKARAEKRvvgdPFDP-------DTFQGPQVSKAQFDKiLSYIESGKKEGAtlLTGGER 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1887644984 377 VfacNADDYLTTPTL-----------HEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHgTEaDLNKADSVIEALQ 444
Cdd:cd07091 357 H---GSKGYFIQPTVftdvkddmkiaKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVF-TK-DINKALRVSRALK 430
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
23-426 |
2.34e-09 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 59.49 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 23 HAFS--PARNEALPTRFFnLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNLPLARL 100
Cdd:PRK13968 8 HAISvnPATGEQLSVLPW-AGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 101 QGERMRTVNQLKAFAS---ALReNPESPLglkVVDEADVtraplpkphteLNYLPLGPVAVFGASNFPYaFSTLGGdTAA 177
Cdd:PRK13968 87 RAEVAKSANLCDWYAEhgpAML-KAEPTL---VENQQAV-----------IEYRPLGTILAIMPWNFPL-WQVMRG-AVP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 178 ALAAGCPVIVKNHTAHPGTGELMARAalaaIKECAMPLGVFAMVQSKAYDIShQLVAAPGIKAVGFTGSFNVASKL--QE 255
Cdd:PRK13968 150 ILLAGNGYLLKHAPNVMGCAQLIAQV----FKDAGIPQGVYGWLNADNDGVS-QMINDSRIAAVTVTGSVRAGAAIgaQA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 256 TIAKREEPIpfygELGSINPQVILPNKAIEQSKEMAQSlcqSMLMGNGQFCTSPGLWLVPTG-----CDELEAHITACIN 330
Cdd:PRK13968 225 GAALKKCVL----ELGGSDPFIVLNDADLELAVKAAVA---GRYQNTGQVCAAAKRFIIEEGiasafTERFVAAAAALKM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 331 DAPSDTLLTPGIVKTFK------QQVEER-SQFAQLsVLGKGKLEQAFHANAHVFACNADDYLTTptLHEEVFGP-AALV 402
Cdd:PRK13968 298 GDPRDEENALGPMARFDlrdelhHQVEATlAEGARL-LLGGEKIAGAGNYYAPTVLANVTPEMTA--FREELFGPvAAIT 374
|
410 420
....*....|....*....|....
gi 1887644984 403 VRYDSEQQLMiLINKLQGQLTASV 426
Cdd:PRK13968 375 VAKDAEHALE-LANDSEFGLSATI 397
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
150-407 |
2.45e-09 |
|
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: 59.42 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 150 YLPLGPVAVFGASNFPY--AFSTLggdtAAALAAGCPVIVKNHTAHPGTGELMARAALAAIKEcamplGVFAMVQSKAyD 227
Cdd:cd07133 99 YQPLGVVGIIVPWNYPLylALGPL----IAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDE-----DEVAVVTGGA-D 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 228 ISHQLVAAPGIKAVgFTGSFNVASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQSkemAQSLCQSMLMGNGQFCT 307
Cdd:cd07133 169 VAAAFSSLPFDHLL-FTGSTAVGRHVMRAAAENLTPVTL--ELGGKSPAIIAPDADLAKA---AERIAFGKLLNAGQTCV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 308 SPGLWLVPTGC-DELEAHITACINDAPSDTLLTP---GIVktfkqqvEERsQFAQLsvlgKGKLEQAFHANAHVFACNAD 383
Cdd:cd07133 243 APDYVLVPEDKlEEFVAAAKAAVAKMYPTLADNPdytSII-------NER-HYARL----QGLLEDARAKGARVIELNPA 310
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1887644984 384 DY------LTTPTL-----------HEEVFGPAALVVRYDS 407
Cdd:cd07133 311 GEdfaatrKLPPTLvlnvtddmrvmQEEIFGPILPILTYDS 351
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
41-308 |
2.72e-09 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 59.51 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 41 STAE-LNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEQTQQETNlplarlqgermrtvnqlKAFASALR 119
Cdd:PRK09407 51 STAAdVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG-----------------KARRHAFE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 120 EnpesplglkVVDEADVTR-----AP-LPKPH-----------TELNYLPLGPVAVFGASNFPYafsTLG-GDTAAALAA 181
Cdd:PRK09407 114 E---------VLDVALTARyyarrAPkLLAPRrragalpvltkTTELRQPKGVVGVISPWNYPL---TLAvSDAIPALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 182 GCPVIVKNHTAHPGTgelmaraALAAIK---ECAMPLGVFAMVQSKAYDISHQLVAapGIKAVGFTGSFNVASKLQETIA 258
Cdd:PRK09407 182 GNAVVLKPDSQTPLT-------ALAAVEllyEAGLPRDLWQVVTGPGPVVGTALVD--NADYLMFTGSTATGRVLAEQAG 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1887644984 259 KREepIPFYGELGSINPQVILPNKAIEQSKEMAQSLCQSmlmGNGQFCTS 308
Cdd:PRK09407 253 RRL--IGFSLELGGKNPMIVLDDADLDKAAAGAVRACFS---NAGQLCIS 297
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
133-445 |
7.44e-09 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 57.82 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 133 EADVTRAPLPKPHTELNYLPLGPVAVFGASNFPyaFSTLGGDTAAALAAGCPVIVKNHTAHPGTGELMARAalaaIKECA 212
Cdd:PRK10090 52 EGEIIQSDRPGENILLFKRALGVTTGILPWNFP--FFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKI----VDEIG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 213 MPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQSKEmaq 292
Cdd:PRK10090 126 LPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCL--ELGGKAPAIVMDDADLDLAVK--- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 293 SLCQSMLMGNGQFCTSPGLWLVPTGC-DELEAHITACI------NDAPSDTL-LTPGIVKTFKQQVEErsqfaqlsvlgk 364
Cdd:PRK10090 201 AIVDSRVINSGQVCNCAERVYVQKGIyDQFVNRLGEAMqavqfgNPAERNDIaMGPLINAAALERVEQ------------ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 365 gKLEQAFHANAHVF----ACNADDYLTTPTL-----------HEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHGT 429
Cdd:PRK10090 269 -KVARAVEEGARVAlggkAVEGKGYYYPPTLlldvrqemsimHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQ 347
|
330
....*....|....*.
gi 1887644984 430 eaDLNKADSVIEALQY 445
Cdd:PRK10090 348 --NLNVAMKAIKGLKF 361
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
83-426 |
6.68e-08 |
|
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: 54.73 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 83 DELIEQTQQETNLPLARLQGERMRTVNQLKAFASALR--ENPESPLGLKVVDE---ADVTRAPLpkphtelnylplGPVA 157
Cdd:cd07148 62 DELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGqlGGREIPMGLTPASAgriAFTTREPI------------GVVV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 158 VFGASNFPyaFSTLGGDTAAALAAGCPVIVKNHTAHPgtgeLMARAALAAIKECAMPLGVFAMVQSKAyDISHQLVAAPG 237
Cdd:cd07148 130 AISAFNHP--LNLIVHQVAPAIAAGCPVIVKPALATP----LSCLAFVDLLHEAGLPEGWCQAVPCEN-AVAEKLVTDPR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 238 IKAVGFTGSFNVASKLQETIAKreepipfyG-----ELGSINPQVILPNKAIEqskEMAQSLCQSMLMGNGQFCTSPGLW 312
Cdd:cd07148 203 VAFFSFIGSARVGWMLRSKLAP--------GtrcalEHGGAAPVIVDRSADLD---AMIPPLVKGGFYHAGQVCVSVQRV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 313 LVPTG-CDELEAHITACI------NDAPSDT----LLTPGIVKTFKQQVEE-RSQFAQLsVLGKGKLEQAFHANAHVFAC 380
Cdd:cd07148 272 FVPAEiADDFAQRLAAAAeklvvgDPTDPDTevgpLIRPREVDRVEEWVNEaVAAGARL-LCGGKRLSDTTYAPTVLLDP 350
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1887644984 381 NADDYLTTptlhEEVFGPAALVVRYDSEQQLMILINKLQGQLTASV 426
Cdd:cd07148 351 PRDAKVST----QEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAV 392
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
6-444 |
1.34e-07 |
|
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: 54.04 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 6 QSLVAGQWIGDSANGEFHAFSPArNEALPTRFFNLSTAELNGAIEAAQSAFY--QYRKTSFAQRADFLTCIAEqilvlgd 83
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPT-DGSVICKVSLATVEDVDRAVAAAKEAFEngEWGKMNARDRGRLMYRLAD------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 84 eLIEQTQQEtnlpLARLQgermrTVNQLKAFASALRENpespLGLKV---------VDEADVTRAPL--PKPHTELNYL- 151
Cdd:cd07140 79 -LMEEHQEE----LATIE-----SLDSGAVYTLALKTH----VGMSIqtfryfagwCDKIQGKTIPInqARPNRNLTLTk 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 152 --PLGPVAVFGASNFPyaFSTLGGDTAAALAAGCPVIVKNHTAHPGTG----ELMARAALaaikecamPLGVFAMVQSKA 225
Cdd:cd07140 145 rePIGVCGIVIPWNYP--LMMLAWKMAACLAAGNTVVLKPAQVTPLTAlkfaELTVKAGF--------PKGVINILPGSG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 226 YDISHQLVAAPGIKAVGFTGSFNVASKLQETIAKRE-EPIPFygELGSINPQVILPNKAIEQSKEMAqslCQSMLMGNGQ 304
Cdd:cd07140 215 SLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSNlKKVSL--ELGGKSPLIIFADCDMDKAVRMG---MSSVFFNKGE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 305 FCTSPG-LWLVPTGCDELEAHI-----TACINDaPSDTLLTPG----------IVKTFKQQVEERsqfAQLSVLGKGKLE 368
Cdd:cd07140 290 NCIAAGrLFVEESIHDEFVRRVveevkKMKIGD-PLDRSTDHGpqnhkahldkLVEYCERGVKEG---ATLVYGGKQVDR 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887644984 369 QAFHANAHVFACNADDYLTTptlHEEVFGPAALVVRYDSE--QQLMILINKLQGQLTASVHgtEADLNKADSVIEALQ 444
Cdd:cd07140 366 PGFFFEPTVFTDVEDHMFIA---KEESFGPIMIISKFDDGdvDGVLQRANDTEYGLASGVF--TKDINKALYVSDKLE 438
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
152-417 |
1.44e-07 |
|
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: 53.76 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 152 PLGPVAVFGASNFPyaFSTLGGDTAAALAAGCPVIVKNHTAHPGTGELMARaalaaIKECAMPLGVFAMVQSkaydishq 231
Cdd:cd07135 108 PLGVVLIIGPWNYP--VLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE-----LVPKYLDPDAFQVVQG-------- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 232 lvAAPGIKA--------VGFTGSFNVASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQSkemAQSLCQSMLMGNG 303
Cdd:cd07135 173 --GVPETTAlleqkfdkIFYTGSGRVGRIIAEAAAKHLTPVTL--ELGGKSPVIVTKNADLELA---AKRILWGKFGNAG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 304 QFCTSPGLWLVPTgcDELEAHITACI--------NDAPSDTLLTPgIV--KTFKQQVE--ERSQfAQLSVLGKGKLEQAF 371
Cdd:cd07135 246 QICVAPDYVLVDP--SVYDEFVEELKkvldefypGGANASPDYTR-IVnpRHFNRLKSllDTTK-GKVVIGGEMDEATRF 321
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1887644984 372 HANAHVFACNADDylttPTLHEEVFGPAALVVRYDSEQQLMILINK 417
Cdd:cd07135 322 IPPTIVSDVSWDD----SLMSEELFGPVLPIIKVDDLDEAIKVINS 363
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
22-444 |
2.09e-07 |
|
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: 53.37 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 22 FHAFSPARNEALpTRFFNLSTAELNGAIEAAQSAFY--QYRKTSFAQRADFLTCIAEqilvlgdeLIEQTQQEtnlpLAR 99
Cdd:cd07112 4 FATINPATGRVL-AEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLAD--------LIEAHRDE----LAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 100 LQgermrTVNQLKAFASALREN-PESPLGL--------KVVDEAdvtrapLPKPHTELNYLPLGPVAVFGAS---NFPya 167
Cdd:cd07112 71 LE-----TLDMGKPISDALAVDvPSAANTFrwyaeaidKVYGEV------APTGPDALALITREPLGVVGAVvpwNFP-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 168 FSTLGGDTAAALAAGCPVIVKNHTAHPGTGELMARAALAAikecAMPLGVFAMVQSKAYDISHQLVAAPGIKAVGFTGSF 247
Cdd:cd07112 138 LLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEA----GLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGST 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 248 NVASKLQETIA----KReepipFYGELGSINPQVILPN-KAIEQSKEMAQSlcqSMLMGNGQFCTSPGLWLVPTGC-DEL 321
Cdd:cd07112 214 EVGRRFLEYSGqsnlKR-----VWLECGGKSPNIVFADaPDLDAAAEAAAA---GIFWNQGEVCSAGSRLLVHESIkDEF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 322 EAHITACIND-APSDTL-----LTPGIVKTFKQQVEE-----RSQFAQLSVLGKGKLEQA--FHANAHVFACNADDYltt 388
Cdd:cd07112 286 LEKVVAAAREwKPGDPLdpatrMGALVSEAHFDKVLGyiesgKAEGARLVAGGKRVLTETggFFVEPTVFDGVTPDM--- 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1887644984 389 pTLH-EEVFGPAALVVRYDSEQQLMILINKLQGQLTASVHgtEADLNKADSVIEALQ 444
Cdd:cd07112 363 -RIArEEIFGPVLSVITFDSEEEAVALANDSVYGLAASVW--TSDLSRAHRVARRLR 416
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
46-416 |
2.68e-07 |
|
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: 53.00 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 46 NGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIEqtqqetnlplarlqgermrtvnqlkAFASALREnPESP 125
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIA-------------------------ALAADFRK-PAAE 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 126 LGLK----VVDEADVTRAPLP---KP------------HTELNYLPLGPVAVFGASNFPyaFSTLGGDTAAALAAGCPVI 186
Cdd:cd07134 55 VDLTeilpVLSEINHAIKHLKkwmKPkrvrtplllfgtKSKIRYEPKGVCLIISPWNYP--FNLAFGPLVSAIAAGNTAI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 187 VKNHTAHPGTGELMARaalaaIKECAMPLGVFAMVQSkAYDISHQLVAAPgIKAVGFTGSFNVASKLQETIAKREEPIPF 266
Cdd:cd07134 133 LKPSELTPHTSAVIAK-----IIREAFDEDEVAVFEG-DAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 267 ygELGSINPQVILPNKAIEQSkemAQSLCQSMLMGNGQFCTSPG-LWLVPTGCDELEAHITACINDAPSDTLLTPGiVKT 345
Cdd:cd07134 206 --ELGGKSPTIVDETADLKKA---AKKIAWGKFLNAGQTCIAPDyVFVHESVKDAFVEHLKAEIEKFYGKDAARKA-SPD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 346 FKQQVEERsQFAQLsvlgKGKLEQAFHANAHVFA---CNADDYLTTPTL-----------HEEVFGPAALVVRYDSEQQL 411
Cdd:cd07134 280 LARIVNDR-HFDRL----KGLLDDAVAKGAKVEFggqFDAAQRYIAPTVltnvtpdmkimQEEIFGPVLPIITYEDLDEV 354
|
....*
gi 1887644984 412 MILIN 416
Cdd:cd07134 355 IEYIN 359
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
6-444 |
4.39e-07 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 52.19 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 6 QSLVAGQWIGDSANGEFHAFSPARNEALpTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRAdfltciaeQILVLGDEL 85
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVL-ATVQAATPADVEAAVASAKQGQKIWAAMTAMERS--------RILRRAVDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 86 IeqtqQETNLPLARLQgermrTVNQLKAFASALrenpesplglkVVD---EADVTR-----AP------LPKPHTELNYL 151
Cdd:PRK13252 79 L----RERNDELAALE-----TLDTGKPIQETS-----------VVDivtGADVLEyyaglAPalegeqIPLRGGSFVYT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 152 ---PLGPVAVFGASNFPYAFSTLGGdtAAALAAGCPVIVKNHTAHPgtgeLMArAALAAI-KECAMPLGVFAMVQSkAYD 227
Cdd:PRK13252 139 rrePLGVCAGIGAWNYPIQIACWKS--APALAAGNAMIFKPSEVTP----LTA-LKLAEIyTEAGLPDGVFNVVQG-DGR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 228 ISHQLVAAPGIKAVGFTGSF--------NVASKLQE-TIakreepipfygELGSINPQVILPNKAIEQSKEMAqslcqsm 298
Cdd:PRK13252 211 VGAWLTEHPDIAKVSFTGGVptgkkvmaAAAASLKEvTM-----------ELGGKSPLIVFDDADLDRAADIA------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 299 LMGN----GQFCTSPGLWLVPTGC-DELEAHITAC-----INDaPSDTLLTPGIVKTFKQQ------VEE-RSQFAQLSV 361
Cdd:PRK13252 273 MLANfyssGQVCTNGTRVFVQKSIkAAFEARLLERverirIGD-PMDPATNFGPLVSFAHRdkvlgyIEKgKAEGARLLC 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 362 LGKGKLEQAFHANAHV----FACNADDyltTPTLHEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVhgTEADLNKAD 437
Cdd:PRK13252 352 GGERLTEGGFANGAFVaptvFTDCTDD---MTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGV--FTADLSRAH 426
|
....*..
gi 1887644984 438 SVIEALQ 444
Cdd:PRK13252 427 RVIHQLE 433
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
152-416 |
2.45e-06 |
|
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: 49.83 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 152 PLGPVAVFGASNFP--YAFSTLggdtAAALAAGCPVIVK--NHTAHpgTGELMARaalaAIKEcAMPLGVFAMVQSKAyD 227
Cdd:cd07087 100 PLGVVLIIGPWNYPlqLALAPL----IGAIAAGNTVVLKpsELAPA--TSALLAK----LIPK-YFDPEAVAVVEGGV-E 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 228 ISHQLVAAPgIKAVGFTGSFNVASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQSkemAQSLCQSMLMGNGQFCT 307
Cdd:cd07087 168 VATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTL--ELGGKSPCIVDKDANLEVA---ARRIAWGKFLNAGQTCI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 308 SPGLWLVPTGC-DELEAHITACIND-APSDTLLTPG---IVKtfKQQVEERSQF-AQLSVLGKGKLEQAFHANAHVFACN 381
Cdd:cd07087 242 APDYVLVHESIkDELIEELKKAIKEfYGEDPKESPDygrIIN--ERHFDRLASLlDDGKVVIGGQVDKEERYIAPTILDD 319
|
250 260 270
....*....|....*....|....*....|....*
gi 1887644984 382 ADdyLTTPTLHEEVFGPAALVVRYDSEQQLMILIN 416
Cdd:cd07087 320 VS--PDSPLMQEEIFGPILPILTYDDLDEAIEFIN 352
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
152-439 |
5.13e-06 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 49.05 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 152 PLGPVAVFGASNFPYAFSTLggDTAAALAAGCPVIVKNHTAHPGTGELMARAAlaaiKECAMPLGVFAMVQSKAYDISHQ 231
Cdd:PLN02766 158 PIGVVGHIIPWNFPSTMFFM--KVAPALAAGCTMVVKPAEQTPLSALFYAHLA----KLAGVPDGVINVVTGFGPTAGAA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 232 LVAAPGIKAVGFTGSFNVASKLQETiAKREEPIPFYGELGSINPQVILPNKAIEQSKEMAQSLCqsmLMGNGQFCTSPGL 311
Cdd:PLN02766 232 IASHMDVDKVSFTGSTEVGRKIMQA-AATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGI---FYNKGEICVASSR 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 312 WLVPTGC-DELEAHITACINDA----PSDTLLTPGiVKTFKQQVEE--------RSQFAQLSVLGKGKLEQAFHANAHVF 378
Cdd:PLN02766 308 VYVQEGIyDEFVKKLVEKAKDWvvgdPFDPRARQG-PQVDKQQFEKilsyiehgKREGATLLTGGKPCGDKGYYIEPTIF 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887644984 379 ACNADDYLTTptlHEEVFGPAALVVRYDSEQQLMILINKLQGQLTASVhgTEADLNKADSV 439
Cdd:PLN02766 387 TDVTEDMKIA---QDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGI--VTKDLDVANTV 442
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
8-314 |
2.86e-05 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 46.67 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 8 LVAGQWIGDSANGEFHAFSPARNEAlPTRFFNLSTAELNGAIEAAQSAFYQYRKTSFAQRADFLTCIAEQILVLGDELIE 87
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKT-QYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 88 QTQQETNLPLARLQGERMRTVNQLKAFASAlrenpesplGLKVVDEADVTRAPlPKPHTELNYL------PLGPVAVFGA 161
Cdd:PLN00412 98 CLVKEIAKPAKDAVTEVVRSGDLISYTAEE---------GVRILGEGKFLVSD-SFPGNERNKYcltskiPLGVVLAIPP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 162 SNFP--YAFSTLggdtAAALAAGCPVIVKNHTAHPGTGELMARAALAAikecAMPLGVFAMVQSKAYDISHQLVAAPGIK 239
Cdd:PLN00412 168 FNYPvnLAVSKI----APALIAGNAVVLKPPTQGAVAALHMVHCFHLA----GFPKGLISCVTGKGSEIGDFLTMHPGVN 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887644984 240 AVGFTGSfnvasklqET---IAKREEPIPFYGELGSINPQVILPNKAIEQSkemAQSLCQSMLMGNGQFCTSPGLWLV 314
Cdd:PLN00412 240 CISFTGG--------DTgiaISKKAGMVPLQMELGGKDACIVLEDADLDLA---AANIIKGGFSYSGQRCTAVKVVLV 306
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
152-417 |
9.97e-04 |
|
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: 41.72 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 152 PLGPVAVFGASNFPY--AFSTLGGdtaaALAAGCPVIVK--NHTAHpgTGELMARAalaaIKECaMPLGVFAMVQSkAYD 227
Cdd:cd07136 100 PYGVVLIIAPWNYPFqlALAPLIG----AIAAGNTAVLKpsELTPN--TSKVIAKI----IEET-FDEEYVAVVEG-GVE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 228 ISHQLVAAPGIKaVGFTGSFNVASKLQETIAKREEPIPFygELGSINPQVILPNKAIEQSkemAQSLCQSMLMGNGQFCT 307
Cdd:cd07136 168 ENQELLDQKFDY-IFFTGSVRVGKIVMEAAAKHLTPVTL--ELGGKSPCIVDEDANLKLA---AKRIVWGKFLNAGQTCV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 308 SPGLWLVPTGC-DELEAHITACINDA-PSDTLLTPGIVKTfkqqVEERsQFAQLS-VLGKGKLeqafhanahVFA--CNA 382
Cdd:cd07136 242 APDYVLVHESVkEKFIKELKEEIKKFyGEDPLESPDYGRI----INEK-HFDRLAgLLDNGKI---------VFGgnTDR 307
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1887644984 383 DDYLTTPTL-----------HEEVFGPAALVVRYDSEQQLMILINK 417
Cdd:cd07136 308 ETLYIEPTIldnvtwddpvmQEEIFGPILPVLTYDTLDEAIEIIKS 353
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
152-260 |
8.11e-03 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 38.66 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887644984 152 PLGPVAVFGASNFPYAfsTLGGDTAAALAAGCPVIVKNHTAHPGTGELMARAALAAIKECAMPLGVFAMVQSKAyDISHQ 231
Cdd:PLN02315 154 PLGIVGVITAFNFPCA--VLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGA-EIGEA 230
|
90 100
....*....|....*....|....*....
gi 1887644984 232 LVAAPGIKAVGFTGSFNVASKLQETIAKR 260
Cdd:PLN02315 231 IAKDTRIPLVSFTGSSKVGLMVQQTVNAR 259
|
|
| |
