|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
25-466 |
0e+00 |
|
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: 684.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 25 TDPADGRELTIAPRAGRAEALQA-AAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWL 103
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAiDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 104 GSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAW 183
Cdd:cd07103 82 YAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 184 LIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADL 263
Cdd:cd07103 162 ALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 264 DHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTK 343
Cdd:cd07103 242 DKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 344 GAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQ 423
Cdd:cd07103 322 GAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 597799983 424 NHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07103 402 EALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYL 444
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
2-466 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 560.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 2 YPNLTLIVGGEERNKGSAGTLCLTDPADGRELTIAPRAGRAEALQA-AAAEKGFAEWSALSALERSKIMRRAADIMRERA 80
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAvAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 81 DAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKV 160
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 161 APALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGE 240
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 241 YLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQ 320
Cdd:COG1012 243 NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 321 MGPLTSQNQLETVLSMVEDALTKGAKIETGGNRI-GDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAE 399
Cdd:COG1012 323 MGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIAL 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597799983 400 SNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN-HFALALPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:COG1012 403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINdGTTGAVPQAPFGGVKQSGIGREGGREGLEEYT 470
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
16-466 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 526.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 16 KGSAGTLCLTDPADGRELTIAPRAGRA-EALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKP 94
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEdVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 95 LAEARGEWLGSADLLDWFAEEGRRVYGRIVPSrAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKP 174
Cdd:pfam00171 83 LAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 175 ASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGP 254
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 255 VIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVL 334
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 335 SMVEDALTKGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTS 414
Cdd:pfam00171 322 KYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTS 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 597799983 415 SMTTAHRVQNHLQAGMLGVNHFALALPET-PFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:pfam00171 402 DLERALRVARRLEAGMVWINDYTTGDADGlPFGGFKQSGFGREGGPYGLEEYT 454
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
52-466 |
3.52e-169 |
|
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: 483.25 E-value: 3.52e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 52 KGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNI 131
Cdd:cd07078 9 AAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDPGE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 132 QIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSD 211
Cdd:cd07078 89 LAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 212 ALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVE 291
Cdd:cd07078 169 ALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 292 ASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRI-GDTGNFYEPTILSGMT 370
Cdd:cd07078 249 ESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLeGGKGYFVPPTVLTDVD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 371 AEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN-HFALALPETPFGGVR 449
Cdd:cd07078 329 PDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINdYSVGAEPSAPFGGVK 408
|
410
....*....|....*..
gi 597799983 450 DSGFGSEGGLEGIEAYL 466
Cdd:cd07078 409 QSGIGREGGPYGLEEYT 425
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
9-466 |
4.44e-165 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 475.33 E-value: 4.44e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 9 VGGEERNKGSAGTLCLTDPADGRELTIAPRAGRAEALQAAAAEKG-FAEWSALSALERSKIMRRAADIMRERADAAARIM 87
Cdd:PLN02278 29 IGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDaFPSWSKLTASERSKILRRWYDLIIANKEDLAQLM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 88 SMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAG 167
Cdd:PLN02278 109 TLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 168 CSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTM 247
Cdd:PLN02278 189 CTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 248 ELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQ 327
Cdd:PLN02278 269 ELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 328 NQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGL 407
Cdd:PLN02278 349 AAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGL 428
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 597799983 408 GAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:PLN02278 429 AAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYL 487
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
25-466 |
3.65e-159 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 458.43 E-value: 3.65e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 25 TDPADGRELTIAPRAG-RAEALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWL 103
Cdd:TIGR01780 2 YNPATGEIIGSVPDQGvDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 104 GSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAW 183
Cdd:TIGR01780 82 YAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 184 LIGKCLLEAGLPPKAVSVIWGT-TSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADAD 262
Cdd:TIGR01780 162 ALARLAEQAGIPKGVLNVITGSrAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 263 LDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALT 342
Cdd:TIGR01780 242 LDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAVE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 343 KGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRV 422
Cdd:TIGR01780 322 KGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWRV 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 597799983 423 QNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:TIGR01780 402 AEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYL 445
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
52-464 |
4.54e-147 |
|
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: 426.88 E-value: 4.54e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 52 KGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRvYGRIVPSRAPNI 131
Cdd:cd07100 10 AAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEA-FLADEPIETDAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 132 QIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWgTTSELSD 211
Cdd:cd07100 89 KAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLL-IDSDQVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 212 ALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVE 291
Cdd:cd07100 168 AIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVH 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 292 ASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEPTILSGMTA 371
Cdd:cd07100 248 EDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPTVLTDVTP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 372 EMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDS 451
Cdd:cd07100 328 GMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGVKRS 407
|
410
....*....|...
gi 597799983 452 GFGSEGGLEGIEA 464
Cdd:cd07100 408 GYGRELGRFGIRE 420
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
54-465 |
6.74e-139 |
|
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: 407.79 E-value: 6.74e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 54 FAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQI 133
Cdd:cd07097 50 FPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 134 QVLKHPIGPVAAFTPWNFP----AWntmqKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSEL 209
Cdd:cd07097 130 ETTREPLGVVGLITPWNFPiaipAW----KIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 210 SDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFI 289
Cdd:cd07097 206 GQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 290 VEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRI--GDTGNFYEPTILS 367
Cdd:cd07097 286 VTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 368 GMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNhfalaLPET---- 443
Cdd:cd07097 366 GVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVN-----LPTAgvdy 440
|
410 420
....*....|....*....|....*
gi 597799983 444 --PFGGVRDSGFGS-EGGLEGIEAY 465
Cdd:cd07097 441 hvPFGGRKGSSYGPrEQGEAALEFY 465
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
9-466 |
3.55e-136 |
|
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: 400.49 E-value: 3.55e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 9 VGGEERNKGSAGTLCLTDPADGRELTIAPRAGRAEALQA-AAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIM 87
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAvDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 88 SMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAG 167
Cdd:cd07088 82 VEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 168 CSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTM 247
Cdd:cd07088 162 NTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 248 ELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQ 327
Cdd:cd07088 242 ELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 328 NQLETVLSMVEDALTKGAKIETGGNRI-GDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVG 406
Cdd:cd07088 322 AALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597799983 407 LGAYLFTSSMTTAHRVQNHLQAGMLGVNHFAlalPETPFG---GVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07088 402 LTSYIYTENLNTAMRATNELEFGETYINREN---FEAMQGfhaGWKKSGLGGADGKHGLEEYL 461
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
26-466 |
4.14e-134 |
|
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: 395.00 E-value: 4.14e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 26 DPADGRELTIAPRAGRA-EALQAAAAEKGF--AEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEW 102
Cdd:cd07114 3 NPATGEPWARVPEASAAdVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 103 LGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTA 182
Cdd:cd07114 83 RYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPAST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 183 WLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADAD 262
Cdd:cd07114 163 LELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 263 LDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALT 342
Cdd:cd07114 243 LDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARARE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 343 KGAKIETGGNRIG----DTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTT 418
Cdd:cd07114 323 EGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLAR 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 597799983 419 AHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07114 403 AHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYT 450
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
24-457 |
3.23e-133 |
|
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: 392.34 E-value: 3.23e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 24 LTDPADGRELTIAPRAGRAEALQAAAAEK-GFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEW 102
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKeGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 103 LGSADLLDWFAEEGRRVYGRIVP-SRAPNIQIQV---LKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDT 178
Cdd:cd07149 83 DRAIETLRLSAEEAKRLAGETIPfDASPGGEGRIgftIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 179 PGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGeyLKKVTMELGGHGPVIVA 258
Cdd:cd07149 163 PLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 259 ADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVE 338
Cdd:cd07149 241 ADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 339 DALTKGAKIETGGNRIgdtGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTT 418
Cdd:cd07149 321 EAVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQK 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 597799983 419 AHRVQNHLQAGMLGVNhfalalpET--------PFGGVRDSGFGSEG 457
Cdd:cd07149 398 ALKAARELEVGGVMIN-------DSstfrvdhmPYGGVKESGTGREG 437
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
26-465 |
6.18e-131 |
|
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: 386.54 E-value: 6.18e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 26 DPADGRELTIAPRAGRAEALQAAAAEK-GFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEAR-GEWL 103
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKeAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRDIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 104 GSADLLDWFAEEGRRVYGRIVPSRAPNIQIqVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAW 183
Cdd:cd07093 83 RAAANFRFFADYILQLDGESYPQDGGALNY-VLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 184 LIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADL 263
Cdd:cd07093 162 LLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 264 DHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTK 343
Cdd:cd07093 242 DRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 344 GAKIETGGNRIG----DTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTA 419
Cdd:cd07093 322 GATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 597799983 420 HRVQNHLQAGMLGVN-HFALALPeTPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07093 402 HRVARRLEAGTVWVNcWLVRDLR-TPFGGVKASGIGREGGDYSLEFY 447
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
54-465 |
6.38e-130 |
|
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: 383.03 E-value: 6.38e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 54 FAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQI 133
Cdd:cd07104 13 QKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPSDVPGKES 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 134 QVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGT-AWLIGKCLLEAGLPPKAVSVIWGTTSELSDA 212
Cdd:cd07104 93 MVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPGGGSEIGDA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 213 LIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEA 292
Cdd:cd07104 173 LVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 293 SIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRigdTGNFYEPTILSGMTAE 372
Cdd:cd07104 253 SVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY---EGLFYQPTVLSDVTPD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 373 MLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN-HFALALPETPFGGVRDS 451
Cdd:cd07104 330 MPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINdQTVNDEPHVPFGGVKAS 409
|
410
....*....|....
gi 597799983 452 GFGSEGGLEGIEAY 465
Cdd:cd07104 410 GGGRFGGPASLEEF 423
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
9-466 |
9.91e-129 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 381.95 E-value: 9.91e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 9 VGGEERNKGSAGTLCLTDPADGRELTIAPRAGRAEALQA-AAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIM 87
Cdd:PRK11241 15 INGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAiDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 88 SMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAG 167
Cdd:PRK11241 95 TLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 168 CSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTM 247
Cdd:PRK11241 175 CTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 248 ELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQ 327
Cdd:PRK11241 255 ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 328 NQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGL 407
Cdd:PRK11241 335 KAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGL 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 597799983 408 GAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:PRK11241 415 AAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYL 473
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
25-465 |
4.51e-125 |
|
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: 371.66 E-value: 4.51e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 25 TDPADGRELTIAPRAGRAEALQAAAAEK-GFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWL 103
Cdd:cd07150 4 LNPADGSVYARVAVGSRQDAERAIAAAYdAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 104 GSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAW 183
Cdd:cd07150 84 FTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 184 LIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADL 263
Cdd:cd07150 164 KIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 264 DHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTK 343
Cdd:cd07150 244 DYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 344 GAKIETGGNRigdTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQ 423
Cdd:cd07150 324 GAKLLTGGKY---DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 597799983 424 NHLQAGMLGVNHFALaLPET--PFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07150 401 ERLESGMVHINDPTI-LDEAhvPFGGVKASGFGREGGEWSMEEF 443
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
25-465 |
1.72e-123 |
|
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: 367.24 E-value: 1.72e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 25 TDPADGRELTIAPRAGRAEALQAAAAEKG-FAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWL 103
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAaFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 104 GSADLLDWFAE-----------EGRRVYGRIVPsrapniqiqvlkhpIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVI 172
Cdd:cd07106 82 GAVAWLRYTASldlpdevieddDTRRVELRRKP--------------LGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 173 KPASDTPGTAWLIGKCLLEAgLPPKAVSVIWGTtSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGH 252
Cdd:cd07106 148 KPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGG-DELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 253 GPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLET 332
Cdd:cd07106 226 DAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 333 VLSMVEDALTKGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLF 412
Cdd:cd07106 306 VKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVW 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 597799983 413 TSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07106 386 SSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEY 438
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
52-466 |
1.38e-122 |
|
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: 362.32 E-value: 1.38e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 52 KGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNI 131
Cdd:cd06534 5 AAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 132 QIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSD 211
Cdd:cd06534 85 EAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 212 ALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVE 291
Cdd:cd06534 165 ALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 292 ASIHDEFIRRfsekarelkvgkgveegtqmgpltsqnqLETVLSMVEDaltkgakietggnrigdtgnfyeptilsgmta 371
Cdd:cd06534 245 ESIYDEFVEK----------------------------LVTVLVDVDP-------------------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 372 EMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN-HFALALPETPFGGVRD 450
Cdd:cd06534 265 DMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINdSSIGVGPEAPFGGVKN 344
|
410
....*....|....*.
gi 597799983 451 SGFGSEGGLEGIEAYL 466
Cdd:cd06534 345 SGIGREGGPYGLEEYT 360
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
27-465 |
5.19e-122 |
|
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: 363.97 E-value: 5.19e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 27 PADGRELTIAPRAGRA-EALQAAAAEKGF--AEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWL 103
Cdd:cd07118 4 PAHGVVVARYAEGTVEdVDAAVAAARKAFdkGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 104 GSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAW 183
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 184 LIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADL 263
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 264 DHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTK 343
Cdd:cd07118 244 DAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 344 GAKIETGGNRIGD-TGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRV 422
Cdd:cd07118 324 GATLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTV 403
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 597799983 423 QNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07118 404 ARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEY 446
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
26-464 |
5.12e-121 |
|
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: 361.28 E-value: 5.12e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 26 DPADGRELTIAPRAGRAEALQA-AAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLG 104
Cdd:cd07145 5 NPANGEVIDTVPSLSREEVREAiEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 105 SADLLDWFAEEGRRVYGRIVPSRA----PNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPG 180
Cdd:cd07145 85 TIRLFKLAAEEAKVLRGETIPVDAyeynERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 181 TAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAAD 260
Cdd:cd07145 165 TAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 261 ADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDA 340
Cdd:cd07145 245 ADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 341 LTKGAKIETGGNRIGdtGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAH 420
Cdd:cd07145 325 VEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRAL 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 597799983 421 RVQNHLQAGMLGVNHFALALPET-PFGGVRDSGFGSEGGLEGIEA 464
Cdd:cd07145 403 KVARELEAGGVVINDSTRFRWDNlPFGGFKKSGIGREGVRYTMLE 447
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
26-465 |
2.29e-120 |
|
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: 359.83 E-value: 2.29e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 26 DPADGRELTIAPRAGRAEALQAAAAEK-GFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARG-EWL 103
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARaAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 104 GSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKhPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAW 183
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRGPFLNYTVRE-PVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 184 LIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGR-IVAAQAGEyLKKVTMELGGHGPVIVAADAD 262
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRkIMQGAAGN-LKRVSLELGGKSANIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 263 LDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALT 342
Cdd:cd07115 241 LDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 343 KGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRV 422
Cdd:cd07115 321 EGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 597799983 423 QNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07115 401 AAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEY 443
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
26-466 |
3.36e-120 |
|
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: 360.09 E-value: 3.36e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 26 DPADGRELTIAPRAGRAEALQAAAAEKGF---AEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEW 102
Cdd:cd07119 19 NPANGEVIATVPEGTAEDAKRAIAAARRAfdsGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 103 LGSADLLDWFAEEGRRVYGRIVPSrAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTA 182
Cdd:cd07119 99 DDVANCFRYYAGLATKETGEVYDV-PPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 183 WLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADAD 262
Cdd:cd07119 178 IALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADAD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 263 LDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALT 342
Cdd:cd07119 258 FETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 343 KGAKIETGGNRIGD----TGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTT 418
Cdd:cd07119 338 EGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIAR 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 597799983 419 AHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07119 418 ANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
9-465 |
2.19e-118 |
|
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: 355.50 E-value: 2.19e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 9 VGGEERNKGSAGTLCLTDPADGREL-TIAPRAGRAEALQAAAAEK-GFAEWSALSALERSKIMRRAADIMRERADAAARI 86
Cdd:cd07131 3 IGGEWVDSASGETFDSRNPADLEEVvGTFPLSTASDVDAAVEAAReAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 87 MSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGA 166
Cdd:cd07131 83 VTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 167 GCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVT 246
Cdd:cd07131 163 GNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 247 MELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTS 326
Cdd:cd07131 243 LEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLIN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 327 QNQLETVLSMVEDALTKGAKIETGGNRI----GDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNR 402
Cdd:cd07131 323 EAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAND 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 597799983 403 LPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFAL-ALPETPFGGVRDSGFGS-EGGLEGIEAY 465
Cdd:cd07131 403 TEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGHrEAGTTALDAF 467
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
54-466 |
3.83e-117 |
|
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: 351.81 E-value: 3.83e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 54 FAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEAR--------GEWLGSADLLDWFAEEGRRVYGRIVp 125
Cdd:cd07138 49 FPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARaaqvglgiGHLRAAADALKDFEFEERRGNSLVV- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 126 srapniqiqvlKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGT 205
Cdd:cd07138 128 -----------REPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 206 TSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSP 285
Cdd:cd07138 197 GPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 286 TRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGnrIG-----DTGNF 360
Cdd:cd07138 277 TRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGG--PGrpeglERGYF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 361 YEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALAl 440
Cdd:cd07138 355 VKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFN- 433
|
410 420
....*....|....*....|....*.
gi 597799983 441 PETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07138 434 PGAPFGGYKQSGNGREWGRYGLEEFL 459
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
55-466 |
7.08e-117 |
|
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: 351.51 E-value: 7.08e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 55 AEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLG-SADLLDWFAEEGRRVYGRIVPSRAPNIQI 133
Cdd:cd07091 57 GWWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESAKGDVAlSIKCLRYYAGWADKIQGKTIPIDGNFLAY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 134 qVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDAL 213
Cdd:cd07091 137 -TRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 214 IKAPEFRKVSLTGSTRVGRIVAAQAGEY-LKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEA 292
Cdd:cd07091 216 SSHMDVDKIAFTGSTAVGRTIMEAAAKSnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 293 SIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEPTILSGMTAE 372
Cdd:cd07091 296 SIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDD 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 373 MLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSG 452
Cdd:cd07091 376 MKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSG 455
|
410
....*....|....
gi 597799983 453 FGSEGGLEGIEAYL 466
Cdd:cd07091 456 FGRELGEEGLEEYT 469
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
7-466 |
6.02e-116 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 348.80 E-value: 6.02e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 7 LIVGGEERNKGSAGTLCLTDPADGRELTIAPRAGRA-EALQAAAAEKGFAE--WSALSALERSKIMRRAADIMRERADAA 83
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPAdVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 84 ARIMSMEQGKPLAEAR-GEWLGSADLLDWFAEEGRRV-YGRIVPSRAPNiQIQVLKHPIGPVAAFTPWNFPAWNTMQKVA 161
Cdd:cd07139 81 ARLWTAENGMPISWSRrAQGPGPAALLRYYAALARDFpFEERRPGSGGG-HVLVRREPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 162 PALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTsELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEY 241
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADR-EVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 242 LKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQM 321
Cdd:cd07139 239 LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 322 GPLTSQNQLETVLSMVEDALTKGAKIETGGNRIG--DTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAE 399
Cdd:cd07139 319 GPLASARQRERVEGYIAKGRAEGARLVTGGGRPAglDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRI 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597799983 400 SNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALAlPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07139 399 ANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLD-FGAPFGGFKQSGIGREGGPEGLDAYL 464
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
57-466 |
9.62e-116 |
|
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: 348.05 E-value: 9.62e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 57 WSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWL-GSADLLDWFAEEGRRVYGRIVPSrAPNIQIQV 135
Cdd:cd07112 42 WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAVDVpSAANTFRWYAEAIDKVYGEVAPT-GPDALALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 136 LKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIK 215
Cdd:cd07112 121 TREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 216 APEFRKVSLTGSTRVGRIVAAQAGEY-LKKVTMELGGHGPVIVAADA-DLDHLIPLAVQWKFRNCGQVCVSPTRFIVEAS 293
Cdd:cd07112 201 HMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHES 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 294 IHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIG-DTGNFY-EPTILSGMTA 371
Cdd:cd07112 281 IKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKRVLtETGGFFvEPTVFDGVTP 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 372 EMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDS 451
Cdd:cd07112 361 DMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQS 440
|
410
....*....|....*
gi 597799983 452 GFGSEGGLEGIEAYL 466
Cdd:cd07112 441 GNGRDKSLHALDKYT 455
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
24-457 |
6.02e-114 |
|
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: 343.07 E-value: 6.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 24 LTDPADGRELTIAPRAGRAEALQA-AAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEW 102
Cdd:cd07147 3 VTNPYTGEVVARVALAGPDDIEEAiAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 103 LGSADLLDWFAEEGRRVYGRIVP----SRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDT 178
Cdd:cd07147 83 ARAIDTFRIAAEEATRIYGEVLPldisARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 179 PGTAWLIGKCLLEAGLPPKAVSVIwGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEylKKVTMELGGHGPVIVA 258
Cdd:cd07147 163 PLSALILGEVLAETGLPKGAFSVL-PCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 259 ADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVE 338
Cdd:cd07147 240 SDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 339 DALTKGAKIETGGNRigdTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTT 418
Cdd:cd07147 320 EAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEK 396
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 597799983 419 AHRVQNHLQAGMLGVNHF-ALALPETPFGGVRDSGFGSEG 457
Cdd:cd07147 397 ALRAWDELEVGGVVINDVpTFRVDHMPYGGVKDSGIGREG 436
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
11-465 |
2.44e-113 |
|
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: 341.98 E-value: 2.44e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 11 GEERNKGSAGTLCLTDPADGRELTIAPRAGRAEALQA-AAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSM 89
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAyRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 90 EQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCS 169
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 170 VVIKPASDTPGTA-WLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTME 248
Cdd:cd07151 161 VVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 249 LGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQN 328
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 329 QLETVLSMVEDALTKGAKIETGGNRigdTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLG 408
Cdd:cd07151 321 QVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLS 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 597799983 409 AYLFTSSMTTAHRVQNHLQAGMLGVNHFALA-LPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07151 398 GAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEF 455
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
25-465 |
3.23e-113 |
|
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: 341.12 E-value: 3.23e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 25 TDPADGRELTIAPRAG-RAEALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWL 103
Cdd:cd07099 1 RNPATGEVLGEVPVTDpAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 104 GSADLLDWFAEEGRRVYG-RIVPSRA--PNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPG 180
Cdd:cd07099 81 LALEAIDWAARNAPRVLApRKVPTGLlmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 181 TAWLIGKCLLEAGLPPKAVSVIWGTtSELSDALIKApEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAAD 260
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGD-GATGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 261 ADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDA 340
Cdd:cd07099 239 ADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 341 LTKGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAH 420
Cdd:cd07099 319 VAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAE 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 597799983 421 RVQNHLQAGMLGVNHFAL--ALPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07099 399 AIARRLEAGAVSINDVLLtaGIPALPFGGVKDSGGGRRHGAEGLREF 445
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
20-457 |
3.39e-112 |
|
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: 338.64 E-value: 3.39e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 20 GTLCLTDPADGRELTIAPRAGraealqaaaaekgFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEAR 99
Cdd:cd07094 13 GKVPADDRADAEEALATARAG-------------AENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 100 GEWLGSADLLDWFAEEGRRVYGRIVPS----RAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPA 175
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRGEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 176 SDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGeyLKKVTMELGGHGPV 255
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 256 IVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLS 335
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 336 MVEDALTKGAKIETGGNRigdTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSS 415
Cdd:cd07094 318 WVEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 597799983 416 MTTAHRVQNHLQAGMLGVN-HFALALPETPFGGVRDSGFGSEG 457
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVNdSSAFRTDWMPFGGVKESGVGREG 437
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
26-466 |
9.31e-112 |
|
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: 337.68 E-value: 9.31e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 26 DPADGRELTIAPRAGRAEALQAAAAEK-GFAEWS-ALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWL 103
Cdd:cd07089 3 NPATEEVIGTAPDAGAADVDAAIAAARrAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 104 -GSADLLDWFAEEGRRVYG-RIVPSRAPNIQIQ---VLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDT 178
Cdd:cd07089 83 dGPIGHLRYFADLADSFPWeFDLPVPALRGGPGrrvVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 179 PGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVA 258
Cdd:cd07089 163 PLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 259 ADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVE 338
Cdd:cd07089 243 DDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 339 DALTKGAKIETGGNRI--GDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSM 416
Cdd:cd07089 323 RGRDEGARLVTGGGRPagLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADV 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 597799983 417 TTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07089 403 DRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
26-465 |
1.97e-110 |
|
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: 334.27 E-value: 1.97e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 26 DPADGRELTIAPRAGRAEA-LQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLG 104
Cdd:cd07090 3 EPATGEVLATVHCAGAEDVdLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 105 SADLLDWFAEEGRRVYGRIVPSRAPNIqIQVLKHPIGPVAAFTPWNFP----AWntmqKVAPALGAGCSVVIKPASDTPG 180
Cdd:cd07090 83 SADCLEYYAGLAPTLSGEHVPLPGGSF-AYTRREPLGVCAGIGAWNYPiqiaSW----KSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 181 TAWLIGKCLLEAGLPPKAVSVIWGTtSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAAD 260
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGG-GETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 261 ADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDA 340
Cdd:cd07090 237 ADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 341 LTKGAKIETGGNRIG-----DTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSS 415
Cdd:cd07090 317 KQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 597799983 416 MTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHY 446
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
26-465 |
3.93e-110 |
|
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: 333.43 E-value: 3.93e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 26 DPADGRELTIAPRAGRAEALQAAAAEK-GFAE-WSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWL 103
Cdd:cd07109 3 DPSTGEVFARIARGGAADVDRAVQAARrAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 104 GSADLLDWFAEEGRRVYGRIVPSrAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAW 183
Cdd:cd07109 83 AAARYFEYYGGAADKLHGETIPL-GPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 184 LIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADL 263
Cdd:cd07109 162 RLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 264 DHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGvEEGTQMGPLTSQNQLETVLSMVEDALTK 343
Cdd:cd07109 242 EAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPG-LEDPDLGPLISAKQLDRVEGFVARARAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 344 GAKIETGGNRIGDT---GNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAH 420
Cdd:cd07109 321 GARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRAL 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 597799983 421 RVQNHLQAGMLGVN-HFALALPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07109 401 RVARRLRAGQVFVNnYGAGGGIELPFGGVKKSGHGREKGLEALYNY 446
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
52-466 |
4.21e-108 |
|
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: 327.61 E-value: 4.21e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 52 KGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNI 131
Cdd:cd07105 11 AAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIPSDKPGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 132 QIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIwgTTS---- 207
Cdd:cd07105 91 LAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVV--THSpeda 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 208 -ELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPT 286
Cdd:cd07105 169 pEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 287 RFIVEASIHDEFIRRFSEKARELKVGKGVEegtqmGPLTSQNQLETVLSMVEDALTKGAKIETGG-NRIGDTGNFYEPTI 365
Cdd:cd07105 249 RIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVDDALSKGAKLVVGGlADESPSGTSMPPTI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 366 LSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN----HFAlalP 441
Cdd:cd07105 324 LDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINgmtvHDE---P 400
|
410 420
....*....|....*....|....*
gi 597799983 442 ETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07105 401 TLPHGGVKSSGYGRFNGKWGIDEFT 425
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
9-465 |
3.18e-107 |
|
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: 326.83 E-value: 3.18e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 9 VGGEERNKGSaGTLCLTDPADGREL-TIAPRAGRAEALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIM 87
Cdd:cd07086 3 IGGEWVGSGG-ETFTSRNPANGEPIaRVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 88 SMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFP----AWNTMqkvaPA 163
Cdd:cd07086 82 SLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPvavpGWNAA----IA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 164 LGAGCSVVIKPASDTPGTAWLIGKCLLEA----GLPPKAVSVIWGTtSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAG 239
Cdd:cd07086 158 LVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGG-GDGGELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 240 EYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGT 319
Cdd:cd07086 237 RRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 320 QMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRI--GDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAI 397
Cdd:cd07086 317 LVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597799983 398 AESNRLPVGLGAYLFTSSMTTAHRVQ--NHLQAGMLGVNhfalaLPET------PFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07086 397 AINNDVPQGLSSSIFTEDLREAFRWLgpKGSDCGIVNVN-----IPTSgaeiggAFGGEKETGGGRESGSDAWKQY 467
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
7-466 |
8.78e-107 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 325.60 E-value: 8.78e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 7 LIVGGEERNKGSAGTLCLTDPADGRE-LTIAPRAGRAEALQAAAAEKGFAE--WSALSALERSKIMRRAADIMRERADAA 83
Cdd:cd07142 6 LFINGQFVDAASGKTFPTIDPRNGEViAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 84 ARIMSMEQGKPLAEAR-GEWLGSADLLDWFAEEGRRVYGRIVPSRAPNiQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAP 162
Cdd:cd07142 86 AALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGPH-HVYTLHEPIGVVGQIIPWNFPLLMFAWKVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 163 ALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEY- 241
Cdd:cd07142 165 ALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSn 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 242 LKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQM 321
Cdd:cd07142 245 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 322 GPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESN 401
Cdd:cd07142 325 GPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRAN 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 597799983 402 RLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07142 405 NSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYL 469
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
26-465 |
3.25e-105 |
|
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: 320.81 E-value: 3.25e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 26 DPADGRELTIAPRAGRAE-ALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEAR-GEWL 103
Cdd:cd07092 3 DPATGEEIATVPDASAADvDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 104 GSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFP----AWntmqKVAPALGAGCSVVIKPASDTP 179
Cdd:cd07092 83 GAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPlmmaAW----KIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 180 GTAWLIGKcLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAA 259
Cdd:cd07092 159 LTTLLLAE-LAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 260 DADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVED 339
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 340 AlTKGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTA 419
Cdd:cd07092 318 A-PAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRA 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 597799983 420 HRVQNHLQAGMLGVN-HFALAlPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07092 397 MRLSARLDFGTVWVNtHIPLA-AEMPHGGFKQSGYGKDLSIYALEDY 442
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
26-466 |
1.19e-104 |
|
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: 319.30 E-value: 1.19e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 26 DPADGRELTIAPRAG-RAEALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLG 104
Cdd:cd07110 3 NPATEATIGEIPAATaEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 105 SADLLDWFAE--EGRRVY-GRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGT 181
Cdd:cd07110 83 VAGCFEYYADlaEQLDAKaERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 182 AWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADA 261
Cdd:cd07110 163 ELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 262 DLDhlipLAVQWK----FRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMV 337
Cdd:cd07110 243 DLE----KAVEWAmfgcFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 338 EDALTKGAKIETGGNR--IGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSS 415
Cdd:cd07110 319 ARGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 597799983 416 MTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07110 399 AERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYL 449
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
55-466 |
4.82e-104 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 318.52 E-value: 4.82e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 55 AEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEAR-GEWLGSADLLDWFAEEGRRVYGRIVPSRApNIQI 133
Cdd:cd07141 61 SPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTIPMDG-DFFT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 134 QVLKHPIGPVAAFTPWNFP----AWntmqKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSEL 209
Cdd:cd07141 140 YTRHEPVGVCGQIIPWNFPllmaAW----KLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 210 SDALIKAPEFRKVSLTGSTRVGRIVAAQAGEY-LKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRF 288
Cdd:cd07141 216 GAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSnLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 289 IVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEPTILSG 368
Cdd:cd07141 296 FVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSD 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 369 MTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGV 448
Cdd:cd07141 376 VTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGY 455
|
410
....*....|....*...
gi 597799983 449 RDSGFGSEGGLEGIEAYL 466
Cdd:cd07141 456 KMSGNGRELGEYGLQEYT 473
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
55-465 |
3.34e-103 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 317.98 E-value: 3.34e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 55 AEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGrivPSRAPNI--- 131
Cdd:PRK09407 68 RAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPKLLA---PRRRAGAlpv 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 132 --QIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSEL 209
Cdd:PRK09407 145 ltKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 210 SDALIKAPEFrkVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFI 289
Cdd:PRK09407 225 GTALVDNADY--LMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIY 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 290 VEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGN-FYEPTILSG 368
Cdd:PRK09407 303 VHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGPlFYEPTVLTG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 369 MTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNH---FALALPETPF 445
Cdd:PRK09407 383 VTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEgyaAAWGSVDAPM 462
|
410 420
....*....|....*....|
gi 597799983 446 GGVRDSGFGSEGGLEGIEAY 465
Cdd:PRK09407 463 GGMKDSGLGRRHGAEGLLKY 482
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
2-465 |
7.32e-103 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 316.05 E-value: 7.32e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 2 YPNLTLIVGGEERNKGSAGTLCLTDPADGRELTIAPRAGRAEALQAAAAEK-GFAEWSALSALERSKIMRRAADIMRERA 80
Cdd:PRK13252 4 QPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKqGQKIWAAMTAMERSRILRRAVDILRERN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 81 DAAARIMSMEQGKPLAEAR-GEWLGSADLLDWFAeegrrvygrivpSRAPNI---QIQVL--------KHPIGPVAAFTP 148
Cdd:PRK13252 84 DELAALETLDTGKPIQETSvVDIVTGADVLEYYA------------GLAPALegeQIPLRggsfvytrREPLGVCAGIGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 149 WNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTtSELSDALIKAPEFRKVSLTGST 228
Cdd:PRK13252 152 WNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGD-GRVGAWLTEHPDIAKVSFTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 229 RVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARE 308
Cdd:PRK13252 231 PTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 309 LKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRI----GDTGNFYEPTILSGMTAEMLAMNEEPFGPl 384
Cdd:PRK13252 311 IRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLteggFANGAFVAPTVFTDCTDDMTIVREEIFGP- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 385 alVMRVHSL---DEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEG 461
Cdd:PRK13252 390 --VMSVLTFddeDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIAT 467
|
....
gi 597799983 462 IEAY 465
Cdd:PRK13252 468 LEHY 471
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
25-461 |
7.42e-103 |
|
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: 314.68 E-value: 7.42e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 25 TDPADGRELTIAPRAGRA-EALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPL-AEARGEW 102
Cdd:cd07108 2 INPATGQVIGEVPRSRAAdVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 103 LGSADLLDWFAEEGRRVYGRIVPSrAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTA 182
Cdd:cd07108 82 AVLADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 183 WLIGKcLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADAD 262
Cdd:cd07108 161 LLLAE-ILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 263 LDHLIPLAVQ-WKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDAL 341
Cdd:cd07108 240 LDDAVDGAIAgMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 342 -TKGAKIETGGNRIGDT----GNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSM 416
Cdd:cd07108 320 sTSGATVLRGGPLPGEGpladGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 597799983 417 TTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEG 461
Cdd:cd07108 400 GRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEG 444
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
58-465 |
1.02e-102 |
|
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: 314.30 E-value: 1.02e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 58 SALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRA-PNIQ---I 133
Cdd:cd07146 35 STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRDDGESFSCDLtANGKarkI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 134 QVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDAL 213
Cdd:cd07146 115 FTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 214 IKAPEFRKVSLTGSTRVGRIVAAQAGeyLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEAS 293
Cdd:cd07146 195 ITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHES 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 294 IHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRigdTGNFYEPTILSGMTAEM 373
Cdd:cd07146 273 VADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 374 LAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN---HFalALPETPFGGVRD 450
Cdd:cd07146 350 ELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNevpGF--RSELSPFGGVKD 427
|
410
....*....|....*.
gi 597799983 451 SGFGS-EGGLEGIEAY 465
Cdd:cd07146 428 SGLGGkEGVREAMKEM 443
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
56-465 |
2.25e-102 |
|
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: 313.48 E-value: 2.25e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 56 EWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAeegRRVYGRIVPSRAPNI---- 131
Cdd:cd07101 33 AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYA---RRAERLLKPRRRRGAipvl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 132 -QIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELS 210
Cdd:cd07101 110 tRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 211 DALIKAPEFrkVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIV 290
Cdd:cd07101 190 GAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 291 EASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGN-FYEPTILSGM 369
Cdd:cd07101 268 HESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPDLGPyFYEPTVLTGV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 370 TAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNH---FALALPETPFG 446
Cdd:cd07101 348 TEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEgyaAAWASIDAPMG 427
|
410
....*....|....*....
gi 597799983 447 GVRDSGFGSEGGLEGIEAY 465
Cdd:cd07101 428 GMKDSGLGRRHGAEGLLKY 446
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
25-465 |
1.10e-101 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 311.67 E-value: 1.10e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 25 TDPADGREL-TIAPRAGRAEALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWL 103
Cdd:PRK09406 6 INPATGETVkTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 104 GSADLLDWFAEEGRRVYGRiVPSRAPNI---QIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPG 180
Cdd:PRK09406 86 KCAKGFRYYAEHAEALLAD-EPADAAAVgasRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 181 TAWLIGKCLLEAGLPPKAVSVIWgTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAAD 260
Cdd:PRK09406 165 TALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 261 ADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDA 340
Cdd:PRK09406 244 ADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 341 LTKGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAH 420
Cdd:PRK09406 324 VAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQE 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 597799983 421 RVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:PRK09406 404 RFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREF 448
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
7-466 |
1.82e-101 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 311.84 E-value: 1.82e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 7 LIVGGEeRNKGSAGTLCLTDPADGRELTIAPRAG-RAEALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAAR 85
Cdd:PRK13473 5 LLINGE-LVAGEGEKQPVYNPATGEVLAEIAEASaAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 86 IMSMEQGKPLAEARGEWL-GSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFP----AWntmqKV 160
Cdd:PRK13473 84 LESLNCGKPLHLALNDEIpAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPlmmaAW----KL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 161 APALGAGCSVVIKPASDTPGTAWLIGKCLLEAgLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGE 240
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 241 YLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQ 320
Cdd:PRK13473 239 SVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 321 MGPLTSQNQLETVLSMVEDALTKG-AKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAE 399
Cdd:PRK13473 319 LGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRW 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597799983 400 SNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN-HFALAlPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:PRK13473 399 ANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNtHFMLV-SEMPHGGQKQSGYGKDMSLYGLEDYT 465
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
4-465 |
1.35e-98 |
|
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: 304.84 E-value: 1.35e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 4 NLTLIVGGEERNKGSAGTLCLTDPADGRELTIAPRAGRAEALQAAAAEKGFAEWSA---LSALERSKIMRRAADIMRERA 80
Cdd:cd07143 6 PTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWglkVSGSKRGRCLSKLADLMERNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 81 DAAARIMSMEQGKP-LAEARGEWLGSADLLDWFAEEGRRVYGRIVPSrAPNIQIQVLKHPIGPVAAFTPWNFP----AWn 155
Cdd:cd07143 86 DYLASIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIET-DIKKLTYTRHEPIGVCGQIIPWNFPllmcAW- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 156 tmqKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGR-IV 234
Cdd:cd07143 164 ---KIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRkVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 235 AAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKG 314
Cdd:cd07143 241 EAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 315 VEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLD 394
Cdd:cd07143 321 FAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597799983 395 EAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENY 471
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
24-466 |
5.23e-98 |
|
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: 302.37 E-value: 5.23e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 24 LTDPADGRELTIAPRAGRAEALQAAAAEK-GFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEW 102
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARaAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 103 LGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQvLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTA 182
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLHYT-LREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 183 WLIGKCLLEAgLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADAD 262
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 263 LDHLIPLAVQ-WKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDAL 341
Cdd:cd07107 239 PEAAADAAVAgMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 342 TKGAKIETGGNR----IGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMT 417
Cdd:cd07107 319 REGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 597799983 418 TAHRVQNHLQAGMLGVN----HFALAlpetPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07107 399 QAHRTARRVEAGYVWINgssrHFLGA----PFGGVKNSGIGREECLEELLSYT 447
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
56-466 |
9.56e-98 |
|
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: 302.79 E-value: 9.56e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 56 EWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPL-AEARGEWLGSADLLDWFAEEGRRVYGRIVPSrAPNIQIQ 134
Cdd:cd07144 61 WWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPT-SPNKLAY 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 135 VLKHPIGPVAAFTPWNFP----AWntmqKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELS 210
Cdd:cd07144 140 TLHEPYGVCGQIIPWNYPlamaAW----KLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 211 DALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHliplAVQWK----FRNCGQVCVSPT 286
Cdd:cd07144 216 SALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQ----AVKWAaagiMYNSGQNCTATS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 287 RFIVEASIHDEFIRRFSEKARE-LKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDT---GNFYE 362
Cdd:cd07144 292 RIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGlgkGYFIP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 363 PTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPE 442
Cdd:cd07144 372 PTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVG 451
|
410 420
....*....|....*....|....
gi 597799983 443 TPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07144 452 VPFGGFKMSGIGRELGEYGLETYT 475
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
26-456 |
8.85e-97 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 299.47 E-value: 8.85e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 26 DPADGRELTIAPRAG-RAEALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLG 104
Cdd:PRK13968 13 NPATGEQLSVLPWAGaDDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 105 SADLLDWFAEEGRRVYgRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWL 184
Cdd:PRK13968 93 SANLCDWYAEHGPAML-KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 185 IGKCLLEAGLPPKAVSVIWGTTSELSdALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLD 264
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWLNADNDGVS-QMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 265 HLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKG 344
Cdd:PRK13968 251 LAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 345 AKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQN 424
Cdd:PRK13968 331 ARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAA 410
|
410 420 430
....*....|....*....|....*....|..
gi 597799983 425 HLQAGMLGVNHFALALPETPFGGVRDSGFGSE 456
Cdd:PRK13968 411 RLECGGVFINGYCASDARVAFGGVKKSGFGRE 442
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
52-457 |
8.07e-96 |
|
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: 297.18 E-value: 8.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 52 KGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPS----R 127
Cdd:cd07082 50 AGRGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGdwfpG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 128 APNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTS 207
Cdd:cd07082 130 TKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 208 ELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGeyLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTR 287
Cdd:cd07082 210 EIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 288 FIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGdtGNFYEPTILS 367
Cdd:cd07082 288 VLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLD 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 368 GMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN--------HFala 439
Cdd:cd07082 366 PVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINskcqrgpdHF--- 442
|
410
....*....|....*...
gi 597799983 440 lpetPFGGVRDSGFGSEG 457
Cdd:cd07082 443 ----PFLGRKDSGIGTQG 456
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
26-466 |
1.02e-95 |
|
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: 296.56 E-value: 1.02e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 26 DPADGRELTIAPRAGRAEALQAAAAEK-GF--AEWSALSALeRSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEW 102
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARrAFdeTDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 103 LGSADLLDWFAEEGRRVYGRIVPSRAPNIQIqVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTA 182
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEPEPGSFSL-VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 183 WLIGKCLLEA-GLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADA 261
Cdd:cd07120 161 AAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 262 DLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDAL 341
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 342 TKGAKIETGGNRIGDT---GNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTT 418
Cdd:cd07120 321 AAGAEVVLRGGPVTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLAR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 597799983 419 AHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07120 401 AMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
26-462 |
2.14e-94 |
|
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: 293.44 E-value: 2.14e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 26 DPADGREL-TIAPRAGRAEALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEAR-GEWL 103
Cdd:cd07098 2 DPATGQHLgSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 104 GSADLLDWFAEEGRRVygrIVPSRAPNIQIQVLK------HPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASD 177
Cdd:cd07098 82 VTCEKIRWTLKHGEKA---LRPESRPGGLLMFYKrarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 178 TpgtAW-------LIGKCLLEAGLPPKAVSVIWGTtSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELG 250
Cdd:cd07098 159 V---AWssgfflsIIRECLAACGHDPDLVQLVTCL-PETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 251 GHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQL 330
Cdd:cd07098 235 GKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 331 ETVLSMVEDALTKGAKIETGGNRIGDT----GNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVG 406
Cdd:cd07098 315 DRLEELVADAVEKGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 597799983 407 LGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALA--LPETPFGGVRDSGFGSEGGLEGI 462
Cdd:cd07098 395 LGASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGL 452
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
7-465 |
6.85e-94 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 292.33 E-value: 6.85e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 7 LIVGGEERNKGSAGTLCLTDPADGRELTIAPRAG-RAEALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAAR 85
Cdd:cd07559 3 NFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTaEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 86 IMSMEQGKPLAEARGEWLG-SADLLDWFAEEGRRVYGRIVPSRAPNIQIqVLKHPIGPVAAFTPWNFP----AWntmqKV 160
Cdd:cd07559 83 AETLDNGKPIRETLAADIPlAIDHFRYFAGVIRAQEGSLSEIDEDTLSY-HFHEPLGVVGQIIPWNFPllmaAW----KL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 161 APALGAGCSVVIKPASDTPGTAWLIGKcLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGE 240
Cdd:cd07559 158 APALAAGNTVVLKPASQTPLSILVLME-LIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 241 YLKKVTMELGGHGPVIVAADAD------LDHLIPLAVQWKFrNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKG 314
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAMdadddfDDKAEEGQLGFAF-NQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 315 VEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRI----GDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRV 390
Cdd:cd07559 316 LDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITF 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 597799983 391 HSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07559 396 KDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHY 470
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
52-466 |
1.15e-93 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 293.64 E-value: 1.15e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 52 KGFAE--WSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGS-ADLLDWFAEEGRRVYGRIVPSRA 128
Cdd:PLN02466 106 KAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMfARLFRYYAGWADKIHGLTVPADG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 129 PNiQIQVLKHPIGPVAAFTPWNFP----AWntmqKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWG 204
Cdd:PLN02466 186 PH-HVQTLHEPIGVAGQIIPWNFPllmfAW----KVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 205 TTSELSDALIKAPEFRKVSLTGSTRVGRIV-AAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCV 283
Cdd:PLN02466 261 FGPTAGAALASHMDVDKLAFTGSTDTGKIVlELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCC 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 284 SPTRFIVEASIHDEFIRRfsEKARELK--VGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGNFY 361
Cdd:PLN02466 341 AGSRTFVHERVYDEFVEK--AKARALKrvVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYI 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 362 EPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALP 441
Cdd:PLN02466 419 QPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDA 498
|
410 420
....*....|....*....|....*
gi 597799983 442 ETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:PLN02466 499 AIPFGGYKMSGIGREKGIYSLNNYL 523
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
9-465 |
1.30e-93 |
|
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: 291.65 E-value: 1.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 9 VGGEERNKGSAGTLCLTDPADGREL-TIAPRAGRAEALQAAAAEKGF-AEWSALSALERSKIMRRAADIMRERADAAARI 86
Cdd:cd07113 4 IDGRPVAGQSEKRLDITNPATEQVIaSVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 87 MSMEQGKPLAEARGEWLG-SADLLDWFAEEGRRVYGRIVPSRAPNIQIQ-----VLKHPIGPVAAFTPWNFPAWNTMQKV 160
Cdd:cd07113 84 ETLCSGKSIHLSRAFEVGqSANFLRYFAGWATKINGETLAPSIPSMQGErytafTRREPVGVVAGIVPWNFSVMIAVWKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 161 APALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTtSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGE 240
Cdd:cd07113 164 GAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGK-GAVGAQLISHPDVAKVSFTGSVATGKKIGRQAAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 241 YLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQ 320
Cdd:cd07113 243 DLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 321 MGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAES 400
Cdd:cd07113 323 FGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLI 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 597799983 401 NRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07113 403 NDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDY 467
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
69-466 |
3.24e-93 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 288.56 E-value: 3.24e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 69 MRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTP 148
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 149 WNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGST 228
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 229 RVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARE 308
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 309 LKVGKGVEEGT-QMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALV 387
Cdd:PRK10090 241 VQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597799983 388 MRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYL 399
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
7-465 |
6.72e-92 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 287.11 E-value: 6.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 7 LIVGGEERNKGSAGTLCLTDPADGRELTIAPRAGRAEALQAAAAEK-GFAEWSALSALERSKIMRRAADIMRERADAAAR 85
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKaAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 86 IMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALG 165
Cdd:cd07085 83 LITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 166 AGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTtSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKV 245
Cdd:cd07085 163 CGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGG-KEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 246 TMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLT 325
Cdd:cd07085 242 QALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 326 SQNQLETVLSMVEDALTKGAKIETGGNRI----GDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESN 401
Cdd:cd07085 322 SPAAKERIEGLIESGVEEGAKLVLDGRGVkvpgYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIIN 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597799983 402 RLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN-HFALALPETPFGGVRDSGFGSEG--GLEGIEAY 465
Cdd:cd07085 402 ANPYGNGAAIFTRSGAAARKFQREVDAGMVGINvPIPVPLAFFSFGGWKGSFFGDLHfyGKDGVRFY 468
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
55-465 |
7.30e-92 |
|
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: 286.11 E-value: 7.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 55 AEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIq 134
Cdd:cd07152 27 RAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQPQGEILPSAPGRLSL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 135 VLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTA-WLIGKCLLEAGLPPKAVSVIWGTtSELSDAL 213
Cdd:cd07152 106 ARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLPGG-ADAGEAL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 214 IKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEAS 293
Cdd:cd07152 185 VEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHES 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 294 IHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRigdTGNFYEPTILSGMTAEM 373
Cdd:cd07152 265 VADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTY---DGLFYRPTVLSGVKPGM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 374 LAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN-HFALALPETPFGGVRDSG 452
Cdd:cd07152 342 PAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINdQTVNDEPHNPFGGMGASG 421
|
410
....*....|....
gi 597799983 453 FGSE-GGLEGIEAY 465
Cdd:cd07152 422 NGSRfGGPANWEEF 435
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
56-466 |
6.27e-91 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 285.56 E-value: 6.27e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 56 EWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARG-EWLGSADLLDWFAEEGRRVYGRIVPSRAPnIQIQ 134
Cdd:PLN02766 75 PWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQ-LQGY 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 135 VLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALI 214
Cdd:PLN02766 154 TLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 215 KAPEFRKVSLTGSTRVGR-IVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEAS 293
Cdd:PLN02766 234 SHMDVDKVSFTGSTEVGRkIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 294 IHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEPTILSGMTAEM 373
Cdd:PLN02766 314 IYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDM 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 374 LAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGF 453
Cdd:PLN02766 394 KIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGF 473
|
410
....*....|...
gi 597799983 454 GSEGGLEGIEAYL 466
Cdd:PLN02766 474 GRDQGMDALDKYL 486
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
3-466 |
1.78e-89 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 282.01 E-value: 1.78e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 3 PNLTLIVGGEERNKGSAGTLCLTDPADGRELTIAPRAGRA-EALQAAAAEKGF-----AEWSALSALERSKIMRRAADIM 76
Cdd:PLN02467 6 PRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEdVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 77 RERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRivpSRAP------NIQIQVLKHPIGPVAAFTPWN 150
Cdd:PLN02467 86 TERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAK---QKAPvslpmeTFKGYVLKEPLGVVGLITPWN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 151 FPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRV 230
Cdd:PLN02467 163 YPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 231 GRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHliplAVQWKFRNC----GQVCVSPTRFIVEASIHDEFIRRFSEKA 306
Cdd:PLN02467 243 GRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDK----AVEWAMFGCfwtnGQICSATSRLLVHERIASEFLEKLVKWA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 307 RELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGD--TGNFYEPTILSGMTAEMLAMNEEPFGPL 384
Cdd:PLN02467 319 KNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 385 ALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEA 464
Cdd:PLN02467 399 LCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLEN 478
|
..
gi 597799983 465 YL 466
Cdd:PLN02467 479 YL 480
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
2-458 |
2.05e-89 |
|
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: 281.80 E-value: 2.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 2 YPnltLIVGGEERnkGSAGTLCLTDPADGREL--TIAPRAGRAEALQAAAAEKGFAEWSALSALERSKIMRRAADIMRER 79
Cdd:cd07124 33 YP---LVIGGKEV--RTEEKIESRNPADPSEVlgTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 80 ADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKhPIGPVAAFTPWNFPAWNTMQK 159
Cdd:cd07124 108 RFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGM 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 160 VAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVG-RI--VAA 236
Cdd:cd07124 187 TTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGlRIyeRAA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 237 QAGE---YLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGK 313
Cdd:cd07124 267 KVQPgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 314 GVEEGTQMGPLTSQNQLETVLSMVEDALtKGAKIETGGNRIGDT--GNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVH 391
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597799983 392 SLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFAL-ALPET-PFGGVRDSGFGSEGG 458
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITgALVGRqPFGGFKMSGTGSKAG 494
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
52-464 |
1.74e-88 |
|
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: 277.59 E-value: 1.74e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 52 KGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNI 131
Cdd:cd07102 29 AAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEALADIRVPEKDGF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 132 QIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTtSELSD 211
Cdd:cd07102 109 ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLS-HETSA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 212 ALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVE 291
Cdd:cd07102 188 ALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 292 ASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNR---IGDTGNFYEPTILSG 368
Cdd:cd07102 268 ESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALfpeDKAGGAYLAPTVLTN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 369 MTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGV 448
Cdd:cd07102 348 VDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGV 427
|
410
....*....|....*.
gi 597799983 449 RDSGFGSEGGLEGIEA 464
Cdd:cd07102 428 KDSGRGVTLSRLGYDQ 443
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
7-465 |
5.71e-88 |
|
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: 277.03 E-value: 5.71e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 7 LIVGGEERNKGSAGTLCLTDPADGRELTIAPRAGRAEA-LQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAAR 85
Cdd:cd07117 3 LFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVdRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 86 IMSMEQGKPLAEARG-EWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIqVLKHPIGPVAAFTPWNFP----AWntmqKV 160
Cdd:cd07117 83 VETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSI-VLREPIGVVGQIIPWNFPflmaAW----KL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 161 APALGAGCSVVIKPASDTPGTAWLIGKcLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGE 240
Cdd:cd07117 158 APALAAGNTVVIKPSSTTSLSLLELAK-IIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 241 YLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQ 320
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 321 MGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIG----DTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEA 396
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTenglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597799983 397 IAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAY 465
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
52-466 |
2.07e-82 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 262.72 E-value: 2.07e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 52 KGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARG-----------EWLGSADLLDwFAEEGRRvy 120
Cdd:cd07111 70 TAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDcdiplvarhfyHHAGWAQLLD-TELAGWK-- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 121 grivpsrapniqiqvlkhPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVS 200
Cdd:cd07111 147 ------------------PVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 201 VIWGtTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQ 280
Cdd:cd07111 209 IVTG-NGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 281 VCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGNF 360
Cdd:cd07111 288 VCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPF 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 361 YEPTILSGM-TAEMLAMnEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALA 439
Cdd:cd07111 368 YPPTLFTNVpPASRIAQ-EEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLF 446
|
410 420
....*....|....*....|....*..
gi 597799983 440 LPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07111 447 DAAAGFGGYRESGFGREGGKEGLYEYL 473
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
7-466 |
1.03e-81 |
|
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: 261.28 E-value: 1.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 7 LIVGGEERNKGSAGTLCLTDPADGRELTIAPRAGRAEALQAAAAEK-GF--AEWSALSALERSKIMRRAADIMRERADAA 83
Cdd:cd07140 8 LFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKeAFenGEWGKMNARDRGRLMYRLADLMEEHQEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 84 ARIMSMEQGKPLAEARGEWLG-SADLLDWFAEEGRRVYGRIVP---SRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQK 159
Cdd:cd07140 88 ATIESLDSGAVYTLALKTHVGmSIQTFRYFAGWCDKIQGKTIPinqARPNRNLTLTKREPIGVCGIVIPWNYPLMMLAWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 160 VAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGR-IVAAQA 238
Cdd:cd07140 168 MAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKhIMKSCA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 239 GEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEG 318
Cdd:cd07140 248 VSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 319 TQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHS--LDEA 396
Cdd:cd07140 328 TDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGV 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 397 IAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:cd07140 408 LQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYL 477
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
55-457 |
5.17e-79 |
|
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: 253.11 E-value: 5.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 55 AEWsaLSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVP---SRAPNI 131
Cdd:cd07148 38 NNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIPmglTPASAG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 132 QIQ-VLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKavsviWGTT---- 206
Cdd:cd07148 116 RIAfTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEG-----WCQAvpce 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 207 SELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYlKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPT 286
Cdd:cd07148 191 NAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 287 RFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTgnFYEPTIL 366
Cdd:cd07148 270 RVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDT--TYAPTVL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 367 SGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN-HFALALPETPF 445
Cdd:cd07148 348 LDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNdHTAFRVDWMPF 427
|
410
....*....|..
gi 597799983 446 GGVRDSGFGSEG 457
Cdd:cd07148 428 AGRRQSGYGTGG 439
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
7-465 |
9.29e-76 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 245.96 E-value: 9.29e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 7 LIVGGEERNKGSAGTLCLTDPADGRELTIAPRAGRAEALQAAAAEKGFAE---WSALSALERSKIMRRAADIMRERADAA 83
Cdd:PRK09847 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgdWSLSSPAKRKAVLNKLADLMEAHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 84 ARIMSMEQGKPLAEA-RGEWLGSADLLDWFAEEGRRVYGRIVPSrAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAP 162
Cdd:PRK09847 102 ALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATT-SSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 163 ALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEY- 241
Cdd:PRK09847 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSn 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 242 LKKVTMELGGHGPVIVAADA-DLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQ 320
Cdd:PRK09847 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 321 MGPLTSQNQLETVLSMVEDALTKGAKIETGGNR-----IGdtgnfyePTILSGMTAEMLAMNEEPFGPLALVMRVHSLDE 395
Cdd:PRK09847 341 MGTLIDCAHADSVHSFIREGESKGQLLLDGRNAglaaaIG-------PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQ 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 396 AIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:PRK09847 414 ALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKF 483
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
2-458 |
6.22e-74 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 241.76 E-value: 6.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 2 YPnltLIVGGEERNKgsAGTLCLTDPADGRELT-IAPRAGRAEA-LQAAAAEKGFAEWSALSALERSKIMRRAADIMRER 79
Cdd:PRK03137 37 YP---LIIGGERITT--EDKIVSINPANKSEVVgRVSKATKELAeKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 80 ADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRV-YGRIVPSRaPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQ 158
Cdd:PRK03137 112 KHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLaDGKPVESR-PGEHNRYFYIPLGVGVVISPWNFPFAIMAG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 159 KVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVG-RI--VA 235
Cdd:PRK03137 191 MTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlRIyeRA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 236 A--QAGE-YLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVG 312
Cdd:PRK03137 271 AkvQPGQiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 313 KGvEEGTQMGPLTSQNQLETVLSMVEDALTKGaKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHS 392
Cdd:PRK03137 351 NP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597799983 393 LDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN----------HfalalpetPFGGVRDSGFGSEGG 458
Cdd:PRK03137 429 FDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgctgaivgyH--------PFGGFNMSGTDSKAG 496
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
17-458 |
1.18e-72 |
|
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: 237.10 E-value: 1.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 17 GSAGTLCLTDPADGRELTIAPRAGRA-EALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPL 95
Cdd:cd07130 9 GGGGVVTSISPANGEPIARVRQATPEdYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 96 AEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFP----AWNTMQkvapALGAGCSVV 171
Cdd:cd07130 89 PEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPvavwGWNAAI----ALVCGNVVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 172 IKPASDTPGTAW----LIGKCLLEAGLPPKAVSVIWGTtSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTM 247
Cdd:cd07130 165 WKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCGG-ADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 248 ELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQ 327
Cdd:cd07130 244 ELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 328 NQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEPTILSgMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGL 407
Cdd:cd07130 324 AAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGL 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597799983 408 GAYLFTSSMTTAHRVQNHLQA--GMLGVNhfalalpeTP---------FGGVRDSGFGSEGG 458
Cdd:cd07130 403 SSSIFTTDLRNAFRWLGPKGSdcGIVNVN--------IGtsgaeiggaFGGEKETGGGRESG 456
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
125-464 |
1.28e-70 |
|
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: 230.49 E-value: 1.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 125 PSRApniqiQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKcLLEAGLPPKAVSVIWG 204
Cdd:cd07087 91 PAKA-----YVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAK-LIPKYFDPEAVAVVEG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 205 TTSElSDALIKAPeFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDhlipLAVQ---W-KFRNCGQ 280
Cdd:cd07087 165 GVEV-ATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLE----VAARriaWgKFLNAGQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 281 VCVSPTRFIVEASIHDEFIRRFSEKARELkVGKGVEEGTQMGPLTSQNQLETVLSMVEDAltkgaKIETGGnRIGDTGNF 360
Cdd:cd07087 239 TCIAPDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGG-QVDKEERY 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 361 YEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNH--FAL 438
Cdd:cd07087 312 IAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDvlLHA 391
|
330 340
....*....|....*....|....*.
gi 597799983 439 ALPETPFGGVRDSGFGSEGGLEGIEA 464
Cdd:cd07087 392 AIPNLPFGGVGNSGMGAYHGKAGFDT 417
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
17-466 |
1.30e-70 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 231.96 E-value: 1.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 17 GSAGTLCLTDPADGRELTIAPRA-GRAEALQAAAAEKGFAE--WSALSALeRSKIMRRAADIMRERADAAARIMSMEQGK 93
Cdd:TIGR04284 12 GSAGTFPTVNPATEEVLGVAADAtAADMDAAIAAARRAFDEtdWSRDTAL-RVRCLRQLRDALRAHVEELRELTIAEVGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 94 PLAEARGEWL-GSADLLDWFAE-----EGRRVYGRIVPSRAPNIQiQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAG 167
Cdd:TIGR04284 91 PRMLTAGAQLeGPVDDLGFAADlaesyAWTTDLGVASPMGIPTRR-TLRREAVGVVGAITPWNFPHQINLAKLGPALAAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 168 CSVVIKPASDTPGTAWLIGKCLLE-AGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVT 246
Cdd:TIGR04284 170 NTVVLKPAPDTPWCAAVLGELIAEhTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRAVMADAAATLKKVF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 247 MELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTS 326
Cdd:TIGR04284 250 LELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADPGTVCGPVIS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 327 QNQLETVLSMVEDALTKGAKIETGGNRIGD--TGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLP 404
Cdd:TIGR04284 330 ARQRDRVQSYLDLAVAEGGRFACGGGRPADrdRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIANDSP 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597799983 405 VGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:TIGR04284 410 YGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYL 471
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
27-457 |
5.05e-70 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 230.42 E-value: 5.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 27 PADGRELTIAPRAG-RAEALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGS 105
Cdd:cd07116 23 PVTGKVFCEVPRSTaEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAADIPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 106 A-DLLDWFAEEGRRVYGRIVPSRAPNIQIQvLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWL 184
Cdd:cd07116 103 AiDHFRYFAGCIRAQEGSISEIDENTVAYH-FHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 185 IGKcLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGP------VIVA 258
Cdd:cd07116 182 LME-LIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPniffadVMDA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 259 ADADLDHLIPLAVQWKFrNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVE 338
Cdd:cd07116 261 DDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYID 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 339 DALTKGAKIETGGNR----IGDTGNFYEPTILSGmTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTS 414
Cdd:cd07116 340 IGKEEGAEVLTGGERnelgGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTR 418
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 597799983 415 SMTTAHRVQNHLQAGMLGVNHFALALPETPFGGVRDSGFGSEG 457
Cdd:cd07116 419 DGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGREN 461
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
2-458 |
7.66e-70 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 230.91 E-value: 7.66e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 2 YPnltLIVGGEERNkgSAGTLCLTDPADGREL--TIAPRAGRAEALQAAAAEKGFAEWSALSALERSKIMRRAADIMRER 79
Cdd:TIGR01237 33 YP---LVINGERVE--TENKIVSINPCDKSEVvgTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 80 ADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQK 159
Cdd:TIGR01237 108 RHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 160 VAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVG-RI--VAA 236
Cdd:TIGR01237 188 TVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGtRIfeRAA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 237 --QAGE-YLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGK 313
Cdd:TIGR01237 268 kvQPGQkHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 314 GVEEGTQMGPLTSQNQLETVLSMVEDALTKGaKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSL 393
Cdd:TIGR01237 348 PDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDF 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597799983 394 DEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALA--LPETPFGGVRDSGFGSEGG 458
Cdd:TIGR01237 427 DEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGaiVGYQPFGGFKMSGTDSKAG 493
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
52-452 |
1.05e-69 |
|
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: 228.31 E-value: 1.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 52 KGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGE---WLGSADL-LDWFAEegrrvygRIVPSR 127
Cdd:cd07095 11 AAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEvaaMAGKIDIsIKAYHE-------RTGERA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 128 APNIQIQ-VLKH-PIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGt 205
Cdd:cd07095 84 TPMAQGRaVLRHrPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 206 TSELSDALIKAPEFRKVSLTGSTRVGRIVAAQ-AGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVS 284
Cdd:cd07095 163 GRETGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 285 PTRFIV-EASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEP 363
Cdd:cd07095 243 ARRLIVpDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLSP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 364 TILSGMTAEMLAmNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNhfalaLPET 443
Cdd:cd07095 323 GIIDVTDAADVP-DEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWN-----RPTT 396
|
410
....*....|....*
gi 597799983 444 ------PFGGVRDSG 452
Cdd:cd07095 397 gasstaPFGGVGLSG 411
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
132-465 |
5.36e-69 |
|
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: 226.33 E-value: 5.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 132 QIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKcLLEAGLPPKAVSVIWGTTSELSd 211
Cdd:cd07135 101 KPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE-LVPKYLDPDAFQVVQGGVPETT- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 212 ALIKAPeFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDhlipLAVQ---W-KFRNCGQVCVSPTR 287
Cdd:cd07135 179 ALLEQK-FDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLE----LAAKrilWgKFGNAGQICVAPDY 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 288 FIVEASIHDEFIRRFsEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDalTKGaKIETGGNRIGDTgNFYEPTILS 367
Cdd:cd07135 254 VLVDPSVYDEFVEEL-KKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT--TKG-KVVIGGEMDEAT-RFIPPTIVS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 368 GMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFAL--ALPETPF 445
Cdd:cd07135 329 DVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVDNAPF 408
|
330 340
....*....|....*....|
gi 597799983 446 GGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07135 409 GGVGDSGYGAYHGKYGFDTF 428
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
52-465 |
2.92e-67 |
|
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: 221.72 E-value: 2.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 52 KGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEAR-GEWLG--------SADLLDWFAeeGRRVYgr 122
Cdd:cd07134 9 AHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlTEILPvlseinhaIKHLKKWMK--PKRVR-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 123 iVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAgLPPKAVSVI 202
Cdd:cd07134 85 -TPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 203 WGTtSELSDALIKAPeFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVC 282
Cdd:cd07134 163 EGD-AEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 283 VSPTRFIVEASIHDEFIRRFSEK-ARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNrIGDTGNFY 361
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHLKAEiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQ-FDAAQRYI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 362 EPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFAL--A 439
Cdd:cd07134 320 APTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLhfL 399
|
410 420
....*....|....*....|....*.
gi 597799983 440 LPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07134 400 NPNLPFGGVNNSGIGSYHGVYGFKAF 425
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
134-455 |
1.14e-59 |
|
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: 202.35 E-value: 1.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 134 QVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKcLLEAGLPPKAVSVIWGTTSElSDAL 213
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAK-IIEETFDEEYVAVVEGGVEE-NQEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 214 IKAPeFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDhlipLAVQ---W-KFRNCGQVCVSPTRFI 289
Cdd:cd07136 173 LDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLK----LAAKrivWgKFLNAGQTCVAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 290 VEASIHDEFIRRFSEKARELKvGKGVEEGTQMGPLTSQNQLETVLSMVEDaltkgAKIETGGNriGDTGNFY-EPTILSG 368
Cdd:cd07136 248 VHESVKEKFIKELKEEIKKFY-GEDPLESPDYGRIINEKHFDRLAGLLDN-----GKIVFGGN--TDRETLYiEPTILDN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 369 MTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN----HfaLALPETP 444
Cdd:cd07136 320 VTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtimH--LANPYLP 397
|
330
....*....|.
gi 597799983 445 FGGVRDSGFGS 455
Cdd:cd07136 398 FGGVGNSGMGS 408
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
57-457 |
3.45e-59 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 202.29 E-value: 3.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 57 WSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGR---IV----PSRAP 129
Cdd:PLN00412 69 WAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEgkfLVsdsfPGNER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 130 NIQIQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSEL 209
Cdd:PLN00412 149 NKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 210 SDALIKAPEFRKVSLTGSTrVGRIVAAQAGeyLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFI 289
Cdd:PLN00412 229 GDFLTMHPGVNCISFTGGD-TGIAISKKAG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 290 VEASIHDEFIRRFSEKARELKVGKGvEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRigdTGNFYEPTILSGM 369
Cdd:PLN00412 306 VMESVADALVEKVNAKVAKLTVGPP-EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR---EGNLIWPLLLDNV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 370 TAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN--------HFalalp 441
Cdd:PLN00412 382 RPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINsapargpdHF----- 456
|
410
....*....|....*.
gi 597799983 442 etPFGGVRDSGFGSEG 457
Cdd:PLN00412 457 --PFQGLKDSGIGSQG 470
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
61-461 |
2.36e-56 |
|
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: 193.09 E-value: 2.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 61 SALERSKIMRRAADIMRERADAAARIMSMEQG-KPLAEAR-GEWLGSADLLD--------WFAEEGRRVYGRIVPSRApn 130
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLlAEILPSIAGIKharkhlkkWMKPSRRHVGLLFLPAKA-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 131 iqiQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKcLLEAGLPPKAVSVIWGTtSELS 210
Cdd:cd07133 96 ---EVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAE-LLAEYFDEDEVAVVTGG-ADVA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 211 DALIKAPeFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHliplAVQ----WKFRNCGQVCVSPT 286
Cdd:cd07133 171 AAFSSLP-FDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAK----AAEriafGKLLNAGQTCVAPD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 287 RFIVEASIHDEFIRRFseKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIET--GGNRIGDTGNFYEPT 364
Cdd:cd07133 246 YVLVPEDKLEEFVAAA--KAAVAKMYPTLADNPDYTSIINERHYARLQGLLEDARAKGARVIElnPAGEDFAATRKLPPT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 365 ILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFAL--ALPE 442
Cdd:cd07133 324 LVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLhvAQDD 403
|
410
....*....|....*....
gi 597799983 443 TPFGGVRDSGFGSEGGLEG 461
Cdd:cd07133 404 LPFGGVGASGMGAYHGKEG 422
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
8-458 |
6.84e-55 |
|
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: 191.25 E-value: 6.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 8 IVGGEERNKGSAGTLclTDPADGRELT---------IAPRAGRAEAlqaaaaeKGFAEWSALSALERSKIMRRAADIMRE 78
Cdd:cd07125 36 IINGEETETGEGAPV--IDPADHERTIgevsladaeDVDAALAIAA-------AAFAGWSATPVEERAEILEKAADLLEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 79 RADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIV---PSRAPNiqiQVLKHPIGPVAAFTPWNFP-AW 154
Cdd:cd07125 107 NRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPElpgPTGELN---GLELHGRGVFVCISPWNFPlAI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 155 NTMQkVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIV 234
Cdd:cd07125 184 FTGQ-IAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 235 A---AQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCvSPTR-FIVEASIHDEFIRRFSEKARELK 310
Cdd:cd07125 263 NralAERDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRC-SALRlLYLQEEIAERFIEMLKGAMASLK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 311 VGKGVEEGTQMGPLTSQNQLETVlsmveDALTkgaKIETGGNRI-------GDTGNFYEPTILSGMTAEMLamNEEPFGP 383
Cdd:cd07125 342 VGDPWDLSTDVGPLIDKPAGKLL-----RAHT---ELMRGEAWLiapapldDGNGYFVAPGIIEIVGIFDL--TTEVFGP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 384 LALVMRVHS--LDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHfalalPET-------PFGGVRDSGFG 454
Cdd:cd07125 412 ILHVIRFKAedLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINR-----NITgaivgrqPFGGWGLSGTG 486
|
....
gi 597799983 455 SEGG 458
Cdd:cd07125 487 PKAG 490
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
135-465 |
4.15e-54 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 188.70 E-value: 4.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 135 VLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKcLLEAGLPPKAVSVIWGTtSELSDALI 214
Cdd:PTZ00381 105 IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAK-LLTKYLDPSYVRVIEGG-VEVTTELL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 215 KAPeFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASI 294
Cdd:PTZ00381 183 KEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 295 HDEFIRRFSEkARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDaltKGAKIETGGNriGDTGNFY-EPTILSGMTAEM 373
Cdd:PTZ00381 262 KDKFIEALKE-AIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE--VDIENKYvAPTIIVNPDLDS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 374 LAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNH--FALALPETPFGGVRDS 451
Cdd:PTZ00381 336 PLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDcvFHLLNPNLPFGGVGNS 415
|
330
....*....|....
gi 597799983 452 GFGSEGGLEGIEAY 465
Cdd:PTZ00381 416 GMGAYHGKYGFDTF 429
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
1-454 |
1.51e-53 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 189.57 E-value: 1.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 1 MYPNLTLIVGGEERNKGSAGTLCLTDPADGRELTIAPRAGRAEALQAAAAEK-GFAEWSALSALERSKIMRRAADIMRER 79
Cdd:PLN02419 110 MPPRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKqAFPLWRNTPITTRQRVMLKFQELIRKN 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 80 ADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVLKHPIGPVAAFTPWNFPAWNTMQK 159
Cdd:PLN02419 190 MDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWM 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 160 VAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELsDALIKAPEFRKVSLTGSTRVGRIVAAQAG 239
Cdd:PLN02419 270 FPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 240 EYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVC--VSPTRFIVEASIHDEfirRFSEKARELKVGKGVEE 317
Cdd:PLN02419 349 AKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCmaLSTVVFVGDAKSWED---KLVERAKALKVTCGSEP 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 318 GTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRI----GDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSL 393
Cdd:PLN02419 426 DADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSF 505
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597799983 394 DEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN-HFALALPETPFGGVRDSGFG 454
Cdd:PLN02419 506 DEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINvPIPVPLPFFSFTGNKASFAG 567
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
57-466 |
4.94e-52 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 183.50 E-value: 4.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 57 WSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNIQIQVL 136
Cdd:PLN02315 72 WMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 137 KHPIGPVAAFTPWNFP----AWNTmqkvAPALGAGCSVVIKPASDTP----GTAWLIGKCLLEAGLPPKAVSVIWGTTsE 208
Cdd:PLN02315 152 WNPLGIVGVITAFNFPcavlGWNA----CIALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIFTSFCGGA-E 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 209 LSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADldhlIPLAVQ----WKFRNCGQVCVS 284
Cdd:PLN02315 227 IGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDAD----IQLAVRsvlfAAVGTAGQRCTT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 285 PTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEPT 364
Cdd:PLN02315 303 CRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPT 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 365 ILSgMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQA--GMLGVNhfalaLPE 442
Cdd:PLN02315 383 IVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVN-----IPT 456
|
410 420 430
....*....|....*....|....*....|
gi 597799983 443 T------PFGGVRDSGFGSEGGLEGIEAYL 466
Cdd:PLN02315 457 NgaeiggAFGGEKATGGGREAGSDSWKQYM 486
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
55-465 |
8.08e-50 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 175.68 E-value: 8.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 55 AEWsalsaleRSKIMRRAADIMRERADAAARIMSMEQGKPLAEA-RGEW--------LGSADLLDWFAEEGRRVYGRIVP 125
Cdd:cd07137 20 AEW-------RKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVsvlvssckLAIKELKKWMAPEKVKTPLTTFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 126 SRApniqiQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKcLLEAGLPPKAVSVIWGT 205
Cdd:cd07137 93 AKA-----EIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAK-LIPEYLDTKAIKVIEGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 206 TSELSdALIKApEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNC-GQVCVS 284
Cdd:cd07137 167 VPETT-ALLEQ-KWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQACIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 285 PTRFIVEASIHDEFIRRFSEKARELkVGKGVEEGTQMGPLTSQNQLETvLSMVEDALTKGAKIETGGNRigDTGNFY-EP 363
Cdd:cd07137 245 PDYVLVEESFAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQR-LSRLLDDPSVADKIVHGGER--DEKNLYiEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 364 TILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFAL--ALP 441
Cdd:cd07137 321 TILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVqyAID 400
|
410 420
....*....|....*....|....
gi 597799983 442 ETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:cd07137 401 TLPFGGVGESGFGAYHGKFSFDAF 424
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
54-452 |
1.16e-48 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 173.99 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 54 FAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGE---WLGSADL-LDWFAEegrRVYGRIVPsrAP 129
Cdd:PRK09457 50 FPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEvtaMINKIAIsIQAYHE---RTGEKRSE--MA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 130 NIQIqVLKH-PIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGtTSE 208
Cdd:PRK09457 125 DGAA-VLRHrPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 209 LSDALIKAPEFRKVSLTGSTRVGRIVAAQ-AGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTR 287
Cdd:PRK09457 203 TGKALAAHPDIDGLLFTGSANTGYLLHRQfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 288 FIVEASIH-DEFIRRFSEKARELKVGKGVEEGTQ-MGPLTSQNQLETVLSMVEDALTKGAKIETGGNRIGDTGNFYEPTI 365
Cdd:PRK09457 283 LLVPQGAQgDAFLARLVAVAKRLTVGRWDAEPQPfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGI 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 366 LSgMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHfalalPET-- 443
Cdd:PRK09457 363 ID-VTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNK-----PLTga 436
|
410
....*....|...
gi 597799983 444 ----PFGGVRDSG 452
Cdd:PRK09457 437 ssaaPFGGVGASG 449
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
52-458 |
1.24e-46 |
|
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: 168.91 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 52 KGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGR--IVPSRAP 129
Cdd:cd07083 66 AAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPavEVVPYPG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 130 NIQIQVLKhPIGPVAAFTPWNFP-AWNTMQKVAPALgAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSE 208
Cdd:cd07083 146 EDNESFYV-GLGAGVVISPWNFPvAIFTGMIVAPVA-VGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 209 LSDALIKAPEFRKVSLTGSTRVGRIVAAQAGE------YLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVC 282
Cdd:cd07083 224 VGAYLTEHERIRGINFTGSLETGKKIYEAAARlapgqtWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKC 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 283 VSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGaKIETGGNRIGDTGNFYE 362
Cdd:cd07083 304 SAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 363 PTILSGMTAEMLAMNEEPFGPLALVMRVHSLD--EAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNHFALA- 439
Cdd:cd07083 383 PTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGa 462
|
410 420
....*....|....*....|
gi 597799983 440 -LPETPFGGVRDSGFGSEGG 458
Cdd:cd07083 463 lVGVQPFGGFKLSGTNAKTG 482
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
124-455 |
6.27e-45 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 162.78 E-value: 6.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 124 VPSRAPNIQ--IQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKcLLEAGLPPKAVSV 201
Cdd:cd07132 83 VKKNLATLLddVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAE-LIPKYLDKECYPV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 202 IWGTTSELSDALikAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDhlipLAVQ---W-KFRN 277
Cdd:cd07132 162 VLGGVEETTELL--KQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDID----VAARriaWgKFIN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 278 CGQVCVSPTRFIVEASIHDEFIrrfsEKARE-LK--VGKGVEEGTQMGPLTSQNQLETVLsmvedALTKGAKIETGGnRI 354
Cdd:cd07132 236 AGQTCIAPDYVLCTPEVQEKFV----EALKKtLKefYGEDPKESPDYGRIINDRHFQRLK-----KLLSGGKVAIGG-QT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 355 GDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN 434
Cdd:cd07132 306 DEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVN 385
|
330 340
....*....|....*....|....*
gi 597799983 435 ----HFalALPETPFGGVRDSGFGS 455
Cdd:cd07132 386 dtimHY--TLDSLPFGGVGNSGMGA 408
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
103-465 |
1.40e-40 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 151.74 E-value: 1.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 103 LGSADLLDWFAEEGRRVYGRIVPSRApniqiQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTA 182
Cdd:PLN02174 81 LALKQLKNWMAPEKAKTSLTTFPASA-----EIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 183 WLIGKcLLEAGLPPKAVSVIWGTTSELSdALIKApEFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIVAADAD 262
Cdd:PLN02174 156 ALLAK-LLEQYLDSSAVRVVEGAVTETT-ALLEQ-KWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 263 LDHLIP--LAVQWKFRNcGQVCVSPTRFIVEASIHDEFIRRFsEKARELKVGKGVEEGTQMGPLTSQNQLETvLSMVEDA 340
Cdd:PLN02174 233 LKVTVRriIAGKWGCNN-GQACISPDYILTTKEYAPKVIDAM-KKELETFYGKNPMESKDMSRIVNSTHFDR-LSKLLDE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 341 LTKGAKIETGGNRigDTGNF-YEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTA 419
Cdd:PLN02174 310 KEVSDKIVYGGEK--DRENLkIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLK 387
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 597799983 420 HRVQNHLQAGMLGVNHFA--LALPETPFGGVRDSGFGSEGGLEGIEAY 465
Cdd:PLN02174 388 ERFAATVSAGGIVVNDIAvhLALHTLPFGGVGESGMGAYHGKFSFDAF 435
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
8-458 |
1.07e-39 |
|
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: 149.68 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 8 IVGGEERNKGSAGTLclTDPADGREL--TIAPRAGRAEALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAAR 85
Cdd:TIGR01238 41 IIGHSYKADGEAQPV--TNPADRRDIvgQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 86 IMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGrivpsrapniqiQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALG 165
Cdd:TIGR01238 119 LCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLG------------EFSVESRGVFVCISPWNFPLAIFTGQISAALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 166 AGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIVA---AQAGEYL 242
Cdd:TIGR01238 187 AGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINqtlAQREDAP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 243 KKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMG 322
Cdd:TIGR01238 267 VPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 323 PLTSQNQLETVLSMVEDALTKGAKI---ETGGNRIGDTGNFYEPTILSgmTAEMLAMNEEPFGPLALVMRVHS--LDEAI 397
Cdd:TIGR01238 347 PVIDAEAKQNLLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIV 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597799983 398 AESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNH--FALALPETPFGGVRDSGFGSEGG 458
Cdd:TIGR01238 425 DQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRnqVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
55-452 |
1.27e-35 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 138.49 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 55 AEWSALSALERSKIMRRAADIM--RERADAAARIMsMEQGKPLAEARGEwlGSADLLDWF---AEEGRRVYGRIVPSRAP 129
Cdd:cd07123 83 KEWARMPFEDRAAIFLKAADLLsgKYRYELNAATM-LGQGKNVWQAEID--AACELIDFLrfnVKYAEELYAQQPLSSPA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 130 NIQIQVLKHPI-GPVAAFTPWNFPAWNTMQKVAPALgAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSE 208
Cdd:cd07123 160 GVWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 209 LSDALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLK------KVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVC 282
Cdd:cd07123 239 VGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKC 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 283 VSPTRFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALT-KGAKIETGGNRIGDTGNFY 361
Cdd:cd07123 319 SAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSdPEAEIIAGGKCDDSVGYFV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 362 EPTILSGMTAEMLAMNEEPFGPLaLVMRVHSlDEAIAESNRL-----PVGLGAYLFT---SSMTTAHRVQNHlQAGMLGV 433
Cdd:cd07123 399 EPTVIETTDPKHKLMTEEIFGPV-LTVYVYP-DSDFEETLELvdttsPYALTGAIFAqdrKAIREATDALRN-AAGNFYI 475
|
410 420
....*....|....*....|....*
gi 597799983 434 NhfalALP------ETPFGGVRDSG 452
Cdd:cd07123 476 N----DKPtgavvgQQPFGGARASG 496
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
55-454 |
6.05e-35 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 136.01 E-value: 6.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 55 AEW--SALSALERskimrraadIMRERADAAARIMSMEQGKPLAEARGEWLG----SA-----DLLDWFAEEGRRVYGRI 123
Cdd:PLN02203 27 LEWrkSQLKGLLR---------LLKDNEEAIFKALHQDLGKHRVEAYRDEVGvltkSAnlalsNLKKWMAPKKAKLPLVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 124 VPSRApniqiQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLlEAGLPPKAVSVIW 203
Cdd:PLN02203 98 FPATA-----EVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANI-PKYLDSKAVKVIE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 204 GTtSELSDALIKAPeFRKVSLTGSTRVGRIVAAQAGEYLKKVTMELGGHGPVIV---AADADLDHLIPLAVQWKFRNC-G 279
Cdd:PLN02203 172 GG-PAVGEQLLQHK-WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGSCaG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 280 QVCVSPTRFIVE---ASIHDEFIRR-----FSEKARELKvgkgveegtQMGPLTSQNQLETVLSMVEDALTKgAKIETGG 351
Cdd:PLN02203 250 QACIAIDYVLVEerfAPILIELLKStikkfFGENPRESK---------SMARILNKKHFQRLSNLLKDPRVA-ASIVHGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 352 NrIGDTGNFYEPTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGML 431
Cdd:PLN02203 320 S-IDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV 398
|
410 420
....*....|....*....|....*
gi 597799983 432 GVNHFAL--ALPETPFGGVRDSGFG 454
Cdd:PLN02203 399 TFNDAIIqyACDSLPFGGVGESGFG 423
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
57-466 |
1.75e-32 |
|
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: 128.51 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 57 WSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEArGEWLGSADLLDWFAEEGR--RVYGRIV--PSRAPNIQ 132
Cdd:cd07084 15 ARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAFVIYsyRIPHEPGnhLGQGLKQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 133 IQVLKHPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAG-LPPKAVSVIWGtTSELSD 211
Cdd:cd07084 94 SHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLING-DGKTMQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 212 ALIKAPEFRKVSLTGSTRVGRIVAAQAGEylKKVTMELGGHGPVIVAADAD-LDHLIPLAVQWKFRNCGQVCVSPTR-FI 289
Cdd:cd07084 173 ALLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMlFV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 290 VEASIHDEFIRRFSEKARELKVgkgveEGTQMGPLtsqnQLETVLSMVEDALTKGAKIETGGNRI---GDTGNFYEPTIL 366
Cdd:cd07084 251 PENWSKTPLVEKLKALLARRKL-----EDLLLGPV----QTFTTLAMIAHMENLLGSVLLFSGKElknHSIPSIYGACVA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 367 SGM-------TAEMLAMNEEPFGPLALVMR------VHSLDEAIAESNRLPVGLGA--YLFTSSMTTAHRVQNHLQAGML 431
Cdd:cd07084 322 SALfvpideiLKTYELVTEEIFGPFAIVVEykkdqlALVLELLERMHGSLTAAIYSndPIFLQELIGNLWVAGRTYAILR 401
|
410 420 430
....*....|....*....|....*....|....*.
gi 597799983 432 GvnHFALALPETPFGGVRDSGFGSE-GGLEGIEAYL 466
Cdd:cd07084 402 G--RTGVAPNQNHGGGPAADPRGAGiGGPEAIKLVW 435
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
52-434 |
6.94e-30 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 123.77 E-value: 6.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 52 KGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRIVPSRAPNI 131
Cdd:PRK11904 596 AAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPTG 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 132 QIQVLK-HPIGPVAAFTPWNFP-AWNTMQkVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSEL 209
Cdd:PRK11904 676 ESNELRlHGRGVFVCISPWNFPlAIFLGQ-VAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATV 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 210 SDALIKAPEFRKVSLTGSTRVGRIV----AAQAGEYLKKVTmELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCvSP 285
Cdd:PRK11904 755 GAALTADPRIAGVAFTGSTETARIInrtlAARDGPIVPLIA-ETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRC-SA 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 286 TRFI-VEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEdALTKGAKI--ETGGNRIGDTGNFYE 362
Cdd:PRK11904 833 LRVLfVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIE-RMKREARLlaQLPLPAGTENGHFVA 911
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597799983 363 PTI--LSGMTaemlAMNEEPFGPLALVMRVHS--LDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN 434
Cdd:PRK11904 912 PTAfeIDSIS----QLEREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
54-404 |
6.40e-29 |
|
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: 118.41 E-value: 6.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 54 FAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFA---EEGRRVYGRI------- 123
Cdd:cd07129 12 FESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFAdlvREGSWLDARIdpadpdr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 124 VPSRAPNI-QIQVlkhPIGPVAAFTPWNFP-AWNTM-QKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEA----GLPP 196
Cdd:cd07129 92 QPLPRPDLrRMLV---PLGPVAVFGASNFPlAFSVAgGDTASALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 197 KAVSVIWGTTSELSDALIKAPEFRKVSLTGSTRVGRIV--AAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWK 274
Cdd:cd07129 169 GVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALfdAAAARPEPIPFYAELGSVNPVFILPGALAERGEAIAQGFV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 275 FR---NCGQVCVSP-TRFIVEASIHDEFIRRFSEKARELKVgkgveegtqmGPLTSQNQLETVLSMVEDALTKGAKIETG 350
Cdd:cd07129 249 GSltlGAGQFCTNPgLVLVPAGPAGDAFIAALAEALAAAPA----------QTMLTPGIAEAYRQGVEALAAAPGVRVLA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 597799983 351 GNRIGDTGNFYEPTILSgMTAEML----AMNEEPFGPLALVMRVHSLDEAIAESNRLP 404
Cdd:cd07129 319 GGAAAEGGNQAAPTLFK-VDAAAFladpALQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
53-434 |
8.08e-29 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 120.74 E-value: 8.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 53 GFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGrivPSRAPniq 132
Cdd:PRK11905 602 AFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLN---GPGHK--- 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 133 iqvlkhPIGPVAAFTPWNFP-AWNTMQkVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSD 211
Cdd:PRK11905 676 ------PLGPVVCISPWNFPlAIFTGQ-IAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGA 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 212 ALIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKKVTM---ELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCvSPTRF 288
Cdd:PRK11905 749 ALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRC-SALRV 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 289 I-VEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKIETGG-NRIGDTGNFYEPTIL 366
Cdd:PRK11905 828 LcLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPlPAETEKGTFVAPTLI 907
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 367 SgmTAEMLAMNEEPFGPLALVMRVHS--LDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVN 434
Cdd:PRK11905 908 E--IDSISDLEREVFGPVLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN 975
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
139-466 |
2.03e-24 |
|
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: 105.81 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 139 PIGPVA----AFtpwNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAG-LPPKAVSVIWGTTSELSDAL 213
Cdd:cd07128 143 PRRGVAvhinAF---NFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 214 ikaPEFRKVSLTGSTRVGRIVAAQAG--EYLKKVTMELGGHGPVIVAADA-----DLDHLIPLAVQWKFRNCGQVCVSPT 286
Cdd:cd07128 220 ---GEQDVVAFTGSAATAAKLRAHPNivARSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 287 RFIVEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEdALTKGAKIETGGN-------RIGDTGN 359
Cdd:cd07128 297 RAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVA-TLLAEAEVVFGGPdrfevvgADAEKGA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 360 FYEPTIL--SGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQA--GMLGVNH 435
Cdd:cd07128 376 FFPPTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVLN 455
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 597799983 436 FALA---------LPETPFGGVRDSGFGSE-GGLEGIEAYL 466
Cdd:cd07128 456 RDSAkestghgspLPQLVHGGPGRAGGGEElGGLRGVKHYM 496
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
52-434 |
1.08e-23 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 105.02 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 52 KGFAEWSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGRivpsrapni 131
Cdd:COG4230 604 AAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAA--------- 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 132 qiQVLKHPIGPVAAFTPWNFP-AWNTMQkVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELS 210
Cdd:COG4230 675 --PTVLRGRGVFVCISPWNFPlAIFTGQ-VAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVG 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 211 DALIKAPEFRKVSLTGSTRVGRIV----AAQAGEYLKKVTmELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCvSPT 286
Cdd:COG4230 752 AALVADPRIAGVAFTGSTETARLInrtlAARDGPIVPLIA-ETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRC-SAL 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 287 RFI-VEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKI-ETGGNRIGDTGNFYEPT 364
Cdd:COG4230 830 RVLcVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPT 909
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597799983 365 I--LSGMTaemlAMNEEPFGPLALVMRVHS--LDEAIAESNRLPVGLgaylfTSSM-----TTAHRVQNHLQAGMLGVN 434
Cdd:COG4230 910 LieIDSIS----DLEREVFGPVLHVVRYKAdeLDKVIDAINATGYGL-----TLGVhsridETIDRVAARARVGNVYVN 979
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
57-458 |
2.53e-23 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 103.90 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 57 WSALSALERSKIMRRAADIMRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYG----Rivpsrapniq 132
Cdd:PRK11809 698 WFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDndthR---------- 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 133 iqvlkhPIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDA 212
Cdd:PRK11809 768 ------PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAA 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 213 LIKAPEFRKVSLTGSTRVGRIVAAQAGEYLKK------VTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCvSPT 286
Cdd:PRK11809 842 LVADARVRGVMFTGSTEVARLLQRNLAGRLDPqgrpipLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRC-SAL 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 287 RFI-VEASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVLSMVEDALTKGAKI---ETGGNRIGDTGNFYE 362
Cdd:PRK11809 921 RVLcLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVfqaARENSEDWQSGTFVP 1000
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 363 PTILS-GMTAEmlaMNEEPFGPLALVMRV--HSLDEAIAESNRLPVGLGAYLFTSSMTTAHRVQNHLQAGMLGVNH--FA 437
Cdd:PRK11809 1001 PTLIElDSFDE---LKREVFGPVLHVVRYnrNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRnmVG 1077
|
410 420
....*....|....*....|.
gi 597799983 438 LALPETPFGGVRDSGFGSEGG 458
Cdd:PRK11809 1078 AVVGVQPFGGEGLSGTGPKAG 1098
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
9-465 |
1.47e-22 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 100.55 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 9 VGGEERNKGSAGTLcLTDPADGRELTIAPRAG-RAEALQAAAAEKGFAEWSALSALERSKIMRRAADIMRERADAAARIM 87
Cdd:PRK11903 9 VAGRWQAGSGAGTP-LFDPVTGEELVRVSATGlDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 88 SMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGR--------IVPSRAPNIQIQVLKHPIGPVAAF-TPWNFPAWNTMQ 158
Cdd:PRK11903 88 TANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDArllrdgeaVQLGKDPAFQGQHVLVPTRGVALFiNAFNFPAWGLWE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 159 KVAPALGAGCSVVIKPASdtpGTAWL---IGKCLLEAG-LPPKAVSVIWGTTSELSDALikaPEFRKVSLTGSTRVGRIV 234
Cdd:PRK11903 168 KAAPALLAGVPVIVKPAT---ATAWLtqrMVKDVVAAGiLPAGALSVVCGSSAGLLDHL---QPFDVVSFTGSAETAAVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 235 AAQAGEYLKKVTMELGGH-------GPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRRFSEKAR 307
Cdd:PRK11903 242 RSHPAVVQRSVRVNVEADslnsallGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 308 ELKVGKGVEEGTQMGPLTSQNQLETVLSMVEdALTKGAKIETGGNRIG------DTGNFYEPTIL--SGMTAEMLAMNEE 379
Cdd:PRK11903 322 KTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLgaSDPDAATAVHDVE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 380 PFGPLALVMRVHSLDEAIAESNRLPVGLGAYLFTS----------SMTTAH-RVqnHLQAGMLGVNH--FALALPETPFG 446
Cdd:PRK11903 401 VFGPVATLLPYRDAAHALALARRGQGSLVASVYSDdaaflaaaalELADSHgRV--HVISPDVAALHtgHGNVMPQSLHG 478
|
490 500
....*....|....*....|
gi 597799983 447 GVRDSGFGSE-GGLEGIEAY 465
Cdd:PRK11903 479 GPGRAGGGEElGGLRALAFY 498
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
76-418 |
8.64e-10 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 60.74 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 76 MRERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAE---EGRRVYGRI-------VPSRAPNIQIQVLKHPIGPVAA 145
Cdd:cd07081 22 MVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKnhfAAEYIYNVYkdektcgVLTGDENGGTLIIAEPIGVVAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 146 FTPWNFPAWNTMQKVAPALGAGCSVVIKP---ASD-TPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALIKAPEFRK 221
Cdd:cd07081 102 ITPSTNPTSTVIFKSLISLKTRNSIIFSPhprAKKvTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLMKFPGIGL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 222 VSLTGstrvGRIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVEASIHDEFIRR 301
Cdd:cd07081 182 LLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 302 FSEkarelkvgkgveegtQMGPLTSQNQLETVLSMV-EDALTKGAKIETGGNRIGDTGNFYEPTILSGMTAEMLAMNEEP 380
Cdd:cd07081 258 FEG---------------QGAYKLTAEELQQVQPVIlKNGDVNRDIVGQDAYKIAAAAGLKVPQETRILIGEVTSLAEHE 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 597799983 381 F------GPLALVMRVHSLDEAIAESNRLpVGLGAYLFTSSMTT 418
Cdd:cd07081 323 PfaheklSPVLAMYRAANFADADAKALAL-KLEGGCGHTSAMYS 365
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
68-431 |
8.79e-09 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 57.51 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 68 IMRRAADIMR--ERADAAARIMSMEQGKPLAEARGEWLGSADLLDWFAEEGRRVYGR--IVPSRAPNIQIQVLKHPIGPV 143
Cdd:cd07126 67 VSHRVAHELRkpEVEDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLARsfNVPGDHQGQQSSGYRWPYGPV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 144 AAFTPWNFPAWNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELsDALIKAPEFRKVS 223
Cdd:cd07126 147 AIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTM-NKILLEANPRMTL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 224 LTGSTRVGRIVAAqagEYLKKVTMELGGHGPVIVAAD-ADLDHLIPLAVQWKFRNCGQVCVSPTRFIVeasiHDEFIRR- 301
Cdd:cd07126 226 FTGSSKVAERLAL---ELHGKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFA----HENWVQAg 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 302 FSEKARELKVGKGVEEGTqMGP-LTSQNQleTVLSMVEDALT-KGAKIETGG-----NRIGDTGNFYEPT--------IL 366
Cdd:cd07126 299 ILDKLKALAEQRKLEDLT-IGPvLTWTTE--RILDHVDKLLAiPGAKVLFGGkpltnHSIPSIYGAYEPTavfvpleeIA 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 597799983 367 SGMTAEMLAmnEEPFGPLALVMRVhsldeaiaESNRLPVGLGAylftssmttAHRVQNHLQAGML 431
Cdd:cd07126 376 IEENFELVT--TEVFGPFQVVTEY--------KDEQLPLVLEA---------LERMHAHLTAAVV 421
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
151-423 |
6.20e-08 |
|
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: 55.18 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 151 FPAWNTMQKVAPALGAGCSVVIKPAsdtPGT----AWLIGKC---LLEAGLPPKAVSVIWGTTSE-LSDALIKAPEFRKV 222
Cdd:cd07127 205 FPTWNGYPGLFASLATGNPVIVKPH---PAAilplAITVQVArevLAEAGFDPNLVTLAADTPEEpIAQTLATRPEVRII 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 223 SLTGSTRVGRIVAAQAGEylKKVTMELGGHGPVIVAAdadLDHLIPLAVQWKFRNC---GQVCVSPTRFIVE-------- 291
Cdd:cd07127 282 DFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVVDS---TDDLKAMLRNLAFSLSlysGQMCTTPQNIYVPrdgiqtdd 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 292 ---------ASIHDEFIRRFSEKARELKVGKGVEEGTQMGPLTSQNQLETVL---SMVEDALTKGAKIETggnrigdtgn 359
Cdd:cd07127 357 grksfdevaADLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLGEVLlasEAVAHPEFPDARVRT---------- 426
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597799983 360 fyePTILSGMTAEMLAMNEEPFGPLALVMRVHSLDEAIAESNRLPVGLGA---YLFTSSMTTAHRVQ 423
Cdd:cd07127 427 ---PLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVREHGAmtvGVYSTDPEVVERVQ 490
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
74-351 |
2.58e-07 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 52.61 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 74 DIMRERADAAARIMSMEQGKPLAEA----RGEWLGS--ADLLDW------------FAEEG-----RRVYGRIVPSRAPN 130
Cdd:cd07077 15 DEQRDLIINAIANALYDTRQRLASEavseRGAYIRSliANWIAMmgcsesklykniDTERGitasvGHIQDVLLPDNGET 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 131 IQIQVlkhPIGPVAAFTPWNFPAwNTMQKVAPALGAGCSVVIKPASDTPGTAWLIGKCLLEA--GLPPKAVSVIWGTTS- 207
Cdd:cd07077 95 YVRAF---PIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaAHGPKILVLYVPHPSd 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 208 ELSDALIKAPEFRKVSLTGSTRVgrIVAAQAGEYLKKVTMELGGHGPVIVAADADLDHLIPLAVQWKFRNcGQVCVSPTR 287
Cdd:cd07077 171 ELAEELLSHPKIDLIVATGGRDA--VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQN 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597799983 288 FIVEASIHDEFIRRFSEKARE--LKVGKGV-------------EEGTQMGPLTSQNQLETVLSMVEDALtkgAKIETGG 351
Cdd:cd07077 248 LYVVDDVLDPLYEEFKLKLVVegLKVPQETkplskettpsfddEALESMTPLECQFRVLDVISAVENAW---MIIESGG 323
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
139-304 |
3.90e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 52.11 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 139 PIGPVAAFTPWNFPAWNTMQKVAPALGAGCSVVIKP----ASDTPGTAWLIGKCLLEAGLPPKAVSVIWGTTSELSDALI 214
Cdd:cd07122 95 PVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhpraKKCSIEAAKIMREAAVAAGAPEGLIQWIEEPSIELTQELM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597799983 215 KAPEFRKVSLTGSTRVGRiVAAQAGeylkkvTMELG---GHGPVIVAADADLDHLIPLAVQWKFRNCGQVCVSPTRFIVE 291
Cdd:cd07122 175 KHPDVDLILATGGPGMVK-AAYSSG------KPAIGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSVIVD 247
|
170
....*....|...
gi 597799983 292 ASIHDEFIRRFSE 304
Cdd:cd07122 248 DEIYDEVRAELKR 260
|
|
| |
