|
Name |
Accession |
Description |
Interval |
E-value |
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
66-516 |
0e+00 |
|
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: 839.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEV 145
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 146 AYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSA 225
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 226 LALAELADQAAIPPGVYNVIPCSRakAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFD 305
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGSR--AKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 306 SANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEKVEKHVN 385
Cdd:TIGR01780 239 DADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKK-LKVGNGLDEGVTQGPLINEKAVEKVEKHIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 386 DAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQ 465
Cdd:TIGR01780 318 DAVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2080330760 466 IWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 516
Cdd:TIGR01780 398 IWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
66-520 |
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: 817.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEV 145
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 146 AYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSA 225
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 226 LALAELADQAAIPPGVYNVIPCSRAkakEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFD 305
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPA---EIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 306 SANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEKVEKHVN 385
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKK-LKVGNGLDEGTDMGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 386 DAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQ 465
Cdd:cd07103 317 DAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2080330760 466 IWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCF 520
Cdd:cd07103 397 AWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
43-523 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 764.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 43 SAALLRTESFVGGRWLPA--AAAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMM 120
Cdd:PLN02278 19 NAGLLRTQGLIGGKWTDAydGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLII 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 121 QNKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMIT 200
Cdd:PLN02278 99 ANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMIT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 201 RKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIpcsRAKAKEVGEALCTDPLVSKISFTGSTATGKIL 280
Cdd:PLN02278 179 RKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVV---MGDAPEIGDALLASPKVRKITFTGSTAVGKKL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 281 LHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGN 360
Cdd:PLN02278 256 MAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQK-LVVGD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 361 GFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTE 440
Cdd:PLN02278 335 GFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 441 EEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCF 520
Cdd:PLN02278 415 EEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
...
gi 2080330760 521 GGL 523
Cdd:PLN02278 495 GNM 497
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
48-520 |
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: 652.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 48 RTESFVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDD 125
Cdd:COG1012 5 EYPLFIGGEWVAAASGetFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 126 LAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGA 205
Cdd:COG1012 85 LAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 206 ALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSrakAKEVGEALCTDPLVSKISFTGSTATGKILLHHAA 285
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGD---GSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 286 GSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEER 365
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKA-LKVGDPLDPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 366 TTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGK-NFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAV 444
Cdd:COG1012 321 TDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGgYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2080330760 445 AIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSV-ECPFGGVKQSGLGREGSKYGIDEYLELKYVCF 520
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVpQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
44-521 |
0e+00 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 633.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 44 AALLRTESFVGGRWLPA--AAAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQ 121
Cdd:PRK11241 6 STLFRQQALINGEWLDAnnGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMME 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 122 NKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITR 201
Cdd:PRK11241 86 HQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 202 KVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSrakAKEVGEALCTDPLVSKISFTGSTATGKILL 281
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGS---AGAVGGELTSNPLVRKLSFTGSTEIGRQLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 282 HHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIkTNLHVGNG 361
Cdd:PRK11241 243 EQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAV-SKLHIGDG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 362 FEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEE 441
Cdd:PRK11241 322 LEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 442 EAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCFG 521
Cdd:PRK11241 402 DVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIG 481
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
57-518 |
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: 586.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 57 WLPAAA-AFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESG 135
Cdd:pfam00171 1 WVDSESeTIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 136 KPLKEAQGEVAYSALFLEWFSEEARRVYGDVIyTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVV 215
Cdd:pfam00171 81 KPLAEARGEVDRAIDVLRYYAGLARRLDGETL-PSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 216 KPAEHTPFSALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMEL 295
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAGLPAGVLNVVT---GSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 296 GGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEK 375
Cdd:pfam00171 237 GGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKK-LKVGDPLDPDTDMGPLISKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 376 AVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLA 455
Cdd:pfam00171 316 QLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2080330760 456 GYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVE-CPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:pfam00171 396 AGVFTSDLERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
88-520 |
0e+00 |
|
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: 542.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 88 AAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVI 167
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 168 YTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPC 247
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 248 SrakAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQT 327
Cdd:cd07078 162 D---GDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 328 CVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGK-N 406
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVK-ALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKgY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 407 FFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLIS 486
Cdd:cd07078 318 FVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVG 397
|
410 420 430
....*....|....*....|....*....|....*
gi 2080330760 487 -SVECPFGGVKQSGLGREGSKYGIDEYLELKYVCF 520
Cdd:cd07078 398 aEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
52-518 |
7.05e-166 |
|
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: 477.91 E-value: 7.05e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAA--AAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKI 129
Cdd:cd07088 1 YINGEFVPSSsgETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 130 ITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAA 209
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 210 GCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVK 289
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVT---GRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENIT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 290 RVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQG 369
Cdd:cd07088 238 KVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMK-AVKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 370 PLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGK-NFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIAN 448
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKgYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAN 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 449 AADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
66-518 |
1.47e-161 |
|
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: 466.64 E-value: 1.47e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPETRAAVRAAYEAF--CSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQG 143
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 144 EVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPF 223
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 224 SALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIV 303
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVT---GFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 304 FDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEKVEKH 383
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARA-IRVGDPLDPETQMGPLATERQLEKVERY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 384 VNDAVSKGATVVTGGKRHQLGKN----FFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFY 459
Cdd:cd07114 317 VARAREEGARVLTGGERPSGADLgagyFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIW 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2080330760 460 SQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07114 397 TRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
66-519 |
4.46e-159 |
|
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: 460.11 E-value: 4.46e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQ-GE 144
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 145 VAYSALFLEWFSEEARRVYGDViYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFS 224
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGES-YPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 225 ALALAELADQAAIPPGVYNVIpcsRAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVF 304
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVV---HGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 305 DSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEKVEKHV 384
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAK-ALKVGDPLDPDTEVGPLISKEHLEKVLGYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 385 NDAVSKGATVVTGGKRHQL----GKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYS 460
Cdd:cd07093 316 ELARAEGATILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2080330760 461 QDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 519
Cdd:cd07093 396 RDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
52-518 |
2.02e-154 |
|
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: 449.35 E-value: 2.02e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAF--CSWRGVSAKERSSLLRKWYDLMMQNKDDLA 127
Cdd:cd07091 7 FINNEFVDSVSGktFPTINPATEEVICQVAEADEEDVDAAVKAARAAFetGWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 128 KIITAESGKPLKE-AQGEVAYSALFLEWFSEEARRVYGDVIYTPaKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAA 206
Cdd:cd07091 87 ALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIPID-GNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 207 LAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSRAKAkevGEALCTDPLVSKISFTGSTATGKILLHHAAG 286
Cdd:cd07091 166 LAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTA---GAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 287 S-VKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTNLhVGNGFEER 365
Cdd:cd07091 243 SnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRV-VGDPFDPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 366 TTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVA 445
Cdd:cd07091 322 TFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2080330760 446 IANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07091 402 RANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
64-518 |
1.35e-153 |
|
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: 446.01 E-value: 1.35e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 64 FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQG 143
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 144 EVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPF 223
Cdd:cd07150 81 ETTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 224 SALALAELADQAAIPPGVYNVIPCSRAkakEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIV 303
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGA---EVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 304 FDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEKVEKH 383
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASK-LKVGDPRDPDTVIGPLISPRQVERIKRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 384 VNDAVSKGATVVTGGKRHqlgKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDP 463
Cdd:cd07150 317 VEDAVAKGAKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2080330760 464 AQIWRVAERLEVGMVGVNEGLISS-VECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07150 394 QRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
87-518 |
1.36e-152 |
|
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: 442.74 E-value: 1.36e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 87 RAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDV 166
Cdd:cd07104 3 DRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 167 IYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFS-ALALAELADQAAIPPGVYNVI 245
Cdd:cd07104 83 LPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 246 PCSrakAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSG 325
Cdd:cd07104 163 PGG---GSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 326 QTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQlgk 405
Cdd:cd07104 240 QICMAAGRILVHESVYDEFVEKLVAKAK-ALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEG--- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 406 NFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLI 485
Cdd:cd07104 316 LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTV 395
|
410 420 430
....*....|....*....|....*....|....*
gi 2080330760 486 SSvEC--PFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07104 396 ND-EPhvPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
52-516 |
7.08e-151 |
|
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: 439.63 E-value: 7.08e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKI 129
Cdd:cd07138 2 YIDGAWVAPAGTetIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 130 ITAESGKPLKEAQGEVAYSALfleWFSEEARRVYGDVIYTpAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAA 209
Cdd:cd07138 82 ITLEMGAPITLARAAQVGLGI---GHLRAAADALKDFEFE-ERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 210 GCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSrakAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVK 289
Cdd:cd07138 158 GCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGD---GPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 290 RVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFV---KKFAEAIKtnlhVGNGFEERT 366
Cdd:cd07138 235 RVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEeiaAAAAEAYV----VGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 367 TQGPLIDEKAVEKVEKHVNDAVSKGATVVTGG--KRHQLGKNFF-EPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEA 443
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgRPEGLERGYFvKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2080330760 444 VAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSvECPFGGVKQSGLGREGSKYGIDEYLELK 516
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP-GAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
64-520 |
4.13e-148 |
|
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: 432.40 E-value: 4.13e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 64 FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQG 143
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 144 EVAYSALFLEWFSEEARRVYGDVI----YTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAE 219
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIpfdaSPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 220 HTPFSALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKIlLHHAAGsVKRVSMELGGHA 299
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVT---GSGETVGDALVTDPRVRMISFTGSPAVGEA-IARKAG-LKKVTLELGSNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 300 PFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEK 379
Cdd:cd07149 236 AVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKK-LVVGDPLDEDTDVGPMISEAEAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 380 VEKHVNDAVSKGATVVTGGKRHQlgkNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFY 459
Cdd:cd07149 315 IEEWVEEAVEGGARLLTGGKRDG---AILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2080330760 460 SQDPAQIWRVAERLEVGMVGVNEglISSVEC---PFGGVKQSGLGREGSKYGIDEYLELKYVCF 520
Cdd:cd07149 392 TNDLQKALKAARELEVGGVMIND--SSTFRVdhmPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
64-518 |
5.40e-146 |
|
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: 427.15 E-value: 5.40e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 64 FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQG 143
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 144 EVAYSALFLEWFSEEARRVYGDVI----YTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAE 219
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIpvdaYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 220 HTPFSALALAELADQAAIPPGVYNVIPCSrakAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHA 299
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGY---GSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 300 PFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEK 379
Cdd:cd07145 238 PMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKK-LKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 380 VEKHVNDAVSKGATVVTGGKRHQlgKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFY 459
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 460 SQDPAQIWRVAERLEVGMVGVNE-GLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07145 395 TNDINRALKVARELEAGGVVINDsTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
64-516 |
7.55e-146 |
|
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: 426.63 E-value: 7.55e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 64 FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCS--WRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEA 141
Cdd:cd07112 4 FATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 142 Q-GEVAYSALFLEWFSEEARRVYGDVIYTPAKEkRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEH 220
Cdd:cd07112 84 LaVDVPSAANTFRWYAEAIDKVYGEVAPTGPDA-LALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 221 TPFSALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGS-VKRVSMELGGHA 299
Cdd:cd07112 163 SPLTALRLAELALEAGLPAGVLNVVP---GFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 300 PFIVF-DSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVE 378
Cdd:cd07112 240 PNIVFaDAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAARE-WKPGDPLDPATRMGALVSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 379 KVEKHVNDAVSKGATVVTGGKRHQL--GKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAG 456
Cdd:cd07112 319 KVLGYIESGKAEGARLVAGGKRVLTetGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2080330760 457 YFYSQDPAQIWRVAERLEVGMVGVN---EGLISSvecPFGGVKQSGLGREGSKYGIDEYLELK 516
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNcfdEGDITT---PFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
66-516 |
1.24e-145 |
|
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: 425.79 E-value: 1.24e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEV 145
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 146 AYSAlflEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSA 225
Cdd:cd07106 81 GGAV---AWLRYTASLDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 226 LALAELAdQAAIPPGVYNVIpcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFD 305
Cdd:cd07106 158 LKLGELA-QEVLPPGVLNVV----SGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 306 SANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEKVEKHVN 385
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAK-AAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 386 DAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQ 465
Cdd:cd07106 312 DAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2080330760 466 IWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 516
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
88-518 |
2.61e-145 |
|
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: 424.18 E-value: 2.61e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 88 AAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVi 167
Cdd:cd07100 3 AALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLADE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 168 YTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPC 247
Cdd:cd07100 82 PIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 248 SRAKAkevgEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQT 327
Cdd:cd07100 162 DSDQV----EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 328 CVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNF 407
Cdd:cd07100 238 CIAAKRFIVHEDVYDEFLEKFVEAMA-ALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 408 FEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISS 487
Cdd:cd07100 317 YPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSD 396
|
410 420 430
....*....|....*....|....*....|.
gi 2080330760 488 VECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07100 397 PRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
66-516 |
1.69e-143 |
|
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: 420.50 E-value: 1.69e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPETRAAVRAAYEAF--CSWRgVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQG 143
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFdtGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 144 -EVAYSALFLEWFSEEARRVYGDVIYT----PAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPA 218
Cdd:cd07089 80 mQVDGPIGHLRYFADLADSFPWEFDLPvpalRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 219 EHTPFSALALAELADQAAIPPGVYNVIPCSrakAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGH 298
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGS---DNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 299 APFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKfAEAIKTNLHVGNGFEERTTQGPLIDEKAVE 378
Cdd:cd07089 237 SANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEA-LAAAFEALPVGDPADPGTVMGPLISAAQRD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 379 KVEKHVNDAVSKGATVVTGGKR-HQLGKNFF-EPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAG 456
Cdd:cd07089 316 RVEGYIARGRDEGARLVTGGGRpAGLDKGFYvEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSG 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 457 YFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 516
Cdd:cd07089 396 GVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
52-518 |
6.67e-143 |
|
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: 420.18 E-value: 6.67e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCS--WRGVSAKERSSLLRKWYDLMMQNKDDLA 127
Cdd:cd07119 1 YIDGEWVEAASGktRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 128 KIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKEKrALVLKQPLGVAAVITPWNFPSAMITRKVGAAL 207
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVI-SRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 208 AAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIpcsRAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGS 287
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLV---TGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 288 VKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTT 367
Cdd:cd07119 237 VKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAK-KIKLGNGLDADTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 368 QGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKR---HQLGKNFF-EPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEA 443
Cdd:cd07119 316 MGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRptgDELAKGYFvEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2080330760 444 VAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07119 396 IRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
67-518 |
3.56e-142 |
|
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: 417.12 E-value: 3.56e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 67 HDPASGAQLGLVADCGVPETRAAVRAAYEAF--CSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGE 144
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFdkGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 145 VAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFS 224
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 225 ALALAELADQAAIPPGVYNVIPCSRAkakEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVF 304
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGA---TVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 305 DSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEKVEKHV 384
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSR-KVRVGDPLDPETKVGAIINEAQLAKITDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 385 NDAVSKGATVVTGGKRHQLGKN-FFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDP 463
Cdd:cd07118 318 DAGRAEGATLLLGGERLASAAGlFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2080330760 464 AQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07118 398 DTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
91-520 |
2.77e-141 |
|
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: 411.62 E-value: 2.77e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 91 RAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTP 170
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 171 AKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSra 250
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGG-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 251 kAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVC 330
Cdd:cd06534 159 -GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 331 SNRFLVQRGIHDSFVKKFAeaiktnlhvgngfeerttqgplidekavekvekhvndavskgatvvtggkrhqlgknffep 410
Cdd:cd06534 238 ASRLLVHESIYDEFVEKLV------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 411 TLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLI-SSVE 489
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPE 336
|
410 420 430
....*....|....*....|....*....|.
gi 2080330760 490 CPFGGVKQSGLGREGSKYGIDEYLELKYVCF 520
Cdd:cd06534 337 APFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
52-518 |
6.15e-138 |
|
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: 406.96 E-value: 6.15e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCS--WRGVSAKERSSLLRKWYDLMMQNKDDLA 127
Cdd:cd07139 2 FIGGRWVAPSGSetIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 128 KIITAESGKPLKEAQ-GEVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAA 206
Cdd:cd07139 82 RLWTAENGMPISWSRrAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 207 LAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSRakakEVGEALCTDPLVSKISFTGSTATGKILLHHAAG 286
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADR----EVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 287 SVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERT 366
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAA-LKVGDPLDPAT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 367 TQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKR--HQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAV 444
Cdd:cd07139 317 QIGPLASARQRERVEGYIAKGRAEGARLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2080330760 445 AIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNeGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07139 397 RIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
52-518 |
2.90e-137 |
|
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: 405.64 E-value: 2.90e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCS-WRGVSAKERSSLLRKWYDLMMQNKDDLAK 128
Cdd:cd07144 11 FINNEFVKSSDGetIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 129 IITAESGKPLKE-AQGEVAYSALFLEWFSEEARRVYGDVIYTpAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAAL 207
Cdd:cd07144 91 IEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKTIPT-SPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 208 AAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSRAKAkevGEALCTDPLVSKISFTGSTATGKILLHHAAGS 287
Cdd:cd07144 170 AAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVA---GSALAEHPDVDKIAFTGSTATGRLVMKAAAQN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 288 VKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTNLHVGNGFEERTT 367
Cdd:cd07144 247 LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYKVGSPFDDDTV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 368 QGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRH--QLGKNFF-EPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAV 444
Cdd:cd07144 327 VGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKApeGLGKGYFiPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAI 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2080330760 445 AIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07144 407 KKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
51-518 |
2.61e-135 |
|
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: 400.57 E-value: 2.61e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 51 SFVGGRWLPAA--AAFPVHDPASGAQL-GLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLA 127
Cdd:cd07131 1 NYIGGEWVDSAsgETFDSRNPADLEEVvGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 128 KIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAAL 207
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 208 AAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIpcsRAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGS 287
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVV---HGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 288 VKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTT 367
Cdd:cd07131 238 NKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKR-LRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 368 QGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKR---HQLGK-NFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEA 443
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERltgGGYEKgYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2080330760 444 VAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLI-SSVECPFGGVKQSGLG-REGSKYGIDEYLELKYV 518
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
68-519 |
1.28e-133 |
|
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: 395.27 E-value: 1.28e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 68 DPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQG-EVA 146
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 147 YSALFLEWFSEEARRVYGDVIytPAkEKRAL--VLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFS 224
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVI--PV-RGPFLnyTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 225 ALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVF 304
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVT---GFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 305 DSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEKVEKHV 384
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLAR-SLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 385 NDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPA 464
Cdd:cd07115 316 DVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2080330760 465 QIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 519
Cdd:cd07115 396 RAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVW 450
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
66-518 |
3.94e-133 |
|
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: 394.03 E-value: 3.94e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEV 145
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 146 AYSALFLEWFSEEARRV---YGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTP 222
Cdd:cd07110 81 DDVAGCFEYYADLAEQLdakAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 223 FSALALAELADQAAIPPGVYNVIpcsRAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFI 302
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVV---TGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 303 VFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEKVEK 382
Cdd:cd07110 238 VFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAE-AIRVGDPLEEGVRLGPLVSQAQYEKVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 383 HVNDAVSKGATVVTGGKRHQ-LGKNFF-EPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYS 460
Cdd:cd07110 317 FIARGKEEGARLLCGGRRPAhLEKGYFiAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2080330760 461 QDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
50-518 |
8.46e-133 |
|
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: 393.92 E-value: 8.46e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 50 ESFVGGRWLPAAAAFPVHDPASGAQ-LGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAK 128
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSDTSDvVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 129 IITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALA 208
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 209 AGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIpcsRAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSV 288
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLV---MGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 289 KRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQ 368
Cdd:cd07097 239 ARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKA-LKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 369 GPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKN--FFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAI 446
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEgyYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2080330760 447 ANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNE---GLISSVecPFGGVKQSGLG-REGSKYGIDEYLELKYV 518
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLptaGVDYHV--PFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
66-518 |
8.80e-132 |
|
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: 390.44 E-value: 8.80e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRG-VSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGE 144
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLrLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 145 VAYSALFLEWFSEEARRVYGDVIyTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFS 224
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETI-PLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 225 ALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVF 304
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVT---GLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 305 DSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGfEERTTQGPLIDEKAVEKVEKHV 384
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFR-ALRVGPG-LEDPDLGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 385 NDAVSKGATVVTGGKRHQL---GKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQ 461
Cdd:cd07109 315 ARARARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2080330760 462 DPAQIWRVAERLEVGMVGVNE-GLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07109 395 DGDRALRVARRLRAGQVFVNNyGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
66-520 |
2.31e-130 |
|
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: 386.79 E-value: 2.31e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEV 145
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 146 AYSALFLEWFSEEARRVYGDVI----YTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHT 221
Cdd:cd07094 83 DRAIDTLRLAAEEAERIRGEEIpldaTQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 222 PFSALALAELADQAAIPPGVYNVIPCSRAkakEVGEALCTDPLVSKISFTGSTATGKILLHHAAGsvKRVSMELGGHAPF 301
Cdd:cd07094 163 PLSALELAKILVEAGVPEGVLQVVTGERE---VLGDAFAADERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 302 IVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEKVE 381
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKK-LKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 382 KHVNDAVSKGATVVTGGKRHqlgKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQ 461
Cdd:cd07094 317 RWVEEAVEAGARLLCGGERD---GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 462 DPAQIWRVAERLEVGMVGVNEGLISSVE-CPFGGVKQSGLGREGSKYGIDEYLELKYVCF 520
Cdd:cd07094 394 DLNVAFKAAEKLEVGGVMVNDSSAFRTDwMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
67-518 |
4.64e-130 |
|
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: 386.19 E-value: 4.64e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 67 HDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVA 146
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 147 YSALFLEWFSEEARRVYGD-VIYTPA--KEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPF 223
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPrKVPTGLlmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 224 SALALAELADQAAIPPGVYNVIpcsrAKAKEVGEALCtDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIV 303
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVV----TGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 304 FDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEKVEKH 383
Cdd:cd07099 236 LADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARA-LRPGADDIGDADIGPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 384 VNDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDP 463
Cdd:cd07099 315 VDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2080330760 464 AQIWRVAERLEVGMVGVNEGLISSV--ECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07099 395 ARAEAIARRLEAGAVSINDVLLTAGipALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
66-519 |
3.40e-129 |
|
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: 383.96 E-value: 3.40e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEV 145
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 146 AYSALFLEWFSEEARRVYGDVIYTPAkEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSA 225
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPG-GSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 226 LALAELADQAAIPPGVYNVIPcsraKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFD 305
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQ----GGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 306 SANVDQAVAGAMASKFRNSGQtcVCSN--RFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEKVEKH 383
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQ--VCSNgtRVFVQRSIKDEFTERLVERTK-KIRIGDPLDEDTQMGALISEEHLEKVLGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 384 VNDAVSKGATVVTGGKRHQL-----GKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYF 458
Cdd:cd07090 313 IESAKQEGAKVLCGGERVVPedgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2080330760 459 YSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 519
Cdd:cd07090 393 FTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
47-518 |
3.72e-128 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 381.95 E-value: 3.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 47 LRTESFVGGRWLP-AAAAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDD 125
Cdd:PRK13473 1 MQTKLLINGELVAgEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 126 LAKIITAESGKPLKEA-QGEVAYSALFLEWFSEEARRVYGDViytpAKEKRA----LVLKQPLGVAAVITPWNFPSAMIT 200
Cdd:PRK13473 81 FARLESLNCGKPLHLAlNDEIPAIVDVFRFFAGAARCLEGKA----AGEYLEghtsMIRRDPVGVVASIAPWNYPLMMAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 201 RKVGAALAAGCTVVVKPAEHTPFSALALAELAdQAAIPPGVYNVIpCSRAKakEVGEALCTDPLVSKISFTGSTATGKIL 280
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELA-ADILPPGVLNVV-TGRGA--TVGDALVGHPKVRMVSLTGSIATGKHV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 281 LHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGN 360
Cdd:PRK13473 233 LSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVAT-LKVGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 361 GFEERTTQGPLIDEKAVEKVEKHVNDAVSKG-ATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDT 439
Cdd:PRK13473 312 PDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDD 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2080330760 440 EEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:PRK13473 392 EDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
64-516 |
3.14e-127 |
|
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: 378.90 E-value: 3.14e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 64 FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQG 143
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 144 EVAYSALFLEWFSEEARRVYGDV----IYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAE 219
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVlpldISARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 220 HTPFSALALAELADQAAIPPGVYNVIPCSRAKAkevgEALCTDPLVSKISFTGSTATGkILLHHAAGSvKRVSMELGGHA 299
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDDA----DLLVTDERIKLLSFTGSPAVG-WDLKARAGK-KKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 300 PFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEK 379
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKA-LKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 380 VEKHVNDAVSKGATVVTGGKRHQlgkNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGL-AGYF 458
Cdd:cd07147 314 VEGWVNEAVDAGAKLLTGGKRDG---ALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLqAGVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2080330760 459 ySQDPAQIWRVAERLEVGMVGVNEglISSVEC---PFGGVKQSGLGREGSKYGIDEYLELK 516
Cdd:cd07147 391 -TRDLEKALRAWDELEVGGVVIND--VPTFRVdhmPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
68-519 |
8.59e-126 |
|
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: 375.14 E-value: 8.59e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 68 DPASGAQLGLVADCGVPETRAAVRAAYEAF--CSWRgVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEV 145
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 146 AYSALFLEWFSEEARRVYGDVIyTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSA 225
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMI-EPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 226 LALAE-LADQAAIPPGVYNVIPCSRAkakEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVF 304
Cdd:cd07120 161 AAIIRiLAEIPSLPAGVVNLFTESGS---EGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 305 DSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEKVEKHV 384
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLA-AVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 385 NDAVSKGATVVTGGKRHQLGKN---FFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQ 461
Cdd:cd07120 317 ERAIAAGAEVVLRGGPVTEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2080330760 462 DPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 519
Cdd:cd07120 397 DLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
66-518 |
1.01e-124 |
|
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: 372.43 E-value: 1.01e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKE-AQGE 144
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 145 VAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFS 224
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 225 ALALAELAdQAAIPPGVYNVIPCSRAkakEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVF 304
Cdd:cd07092 161 TLLLAELA-AEVLPPGVVNVVCGGGA---SAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 305 DSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEKVEKHV 384
Cdd:cd07092 237 DDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSA-IRVGDPDDEDTEMGPLNSAAQRERVAGFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 385 nDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPA 464
Cdd:cd07092 316 -ERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2080330760 465 QIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07092 395 RAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
52-518 |
8.15e-123 |
|
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: 368.78 E-value: 8.15e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAA--AAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAF-CSW-RGVSAKERSSLLRKWYDLMMQNKDDLA 127
Cdd:cd07143 10 FINGEFVDSVhgGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFeTDWgLKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 128 KIITAESGKP-LKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKeKRALVLKQPLGVAAVITPWNFPSAMITRKVGAA 206
Cdd:cd07143 90 SIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIK-KLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 207 LAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAG 286
Cdd:cd07143 169 LAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVS---GYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 287 S-VKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEER 365
Cdd:cd07143 246 SnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKK-LKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 366 TTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVA 445
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2080330760 446 IANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
49-518 |
2.61e-122 |
|
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: 367.20 E-value: 2.61e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 49 TESFVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAF--CSWRGVSAKERSSLLRKWYDLMMQNKD 124
Cdd:cd07142 4 TKLFINGQFVDAASGktFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFdeGPWPRMTGYERSRILLRFADLLEKHAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 125 DLAKIITAESGKPLKEA-QGEVAYSALFLEWFSEEARRVYGDVIytPAKEK-RALVLKQPLGVAAVITPWNFPSAMITRK 202
Cdd:cd07142 84 ELAALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTL--PADGPhHVYTLHEPIGVVGQIIPWNFPLLMFAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 203 VGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSRAKAkevGEALCTDPLVSKISFTGSTATGKILLH 282
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTA---GAAIASHMDVDKVAFTGSTEVGKIIMQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 283 HAAGS-VKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKfAEAIKTNLHVGNG 361
Cdd:cd07142 239 LAAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEK-AKARALKRVVGDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 362 FEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEE 441
Cdd:cd07142 318 FRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVD 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2080330760 442 EAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07142 398 EVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
51-503 |
2.85e-122 |
|
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: 366.89 E-value: 2.85e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 51 SFVGGRWLPAAA-AFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKI 129
Cdd:cd07086 1 GVIGGEWVGSGGeTFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 130 ITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAA 209
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 210 GCTVVVKPAEHTPFSALALAELADQAA----IPPGVYNVIpCSRAkakEVGEALCTDPLVSKISFTGSTATGKILLHHAA 285
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVLekngLPPGVVNLV-TGGG---DGGELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 286 GSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEER 365
Cdd:cd07086 237 RRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQ-VRIGDPLDEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 366 TTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKR--HQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEA 443
Cdd:cd07086 316 TLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2080330760 444 VAIANAADVGLAGYFYSQDPAQI--WRVAERLEVGMVGVNEGLI-SSVECPFGGVKQSGLGRE 503
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAfrWLGPKGSDCGIVNVNIPTSgAEIGGAFGGEKETGGGRE 458
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
42-518 |
6.09e-122 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 367.14 E-value: 6.09e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 42 LSAALLRTESFVGGRWLPA--AAAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFC-----SWRGVSAKERSSLLRK 114
Cdd:PLN02467 1 MAIPVPRRQLFIGGEWREPvlGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKrnkgkDWARTTGAVRAKYLRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 115 WYDLMMQNKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYG---DVIYTPAKEKRALVLKQPLGVAAVITP 191
Cdd:PLN02467 81 IAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkqkAPVSLPMETFKGYVLKEPLGVVGLITP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 192 WNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFT 271
Cdd:PLN02467 161 WNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVT---GLGTEAGAPLASHPGVDKIAFT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 272 GSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEA 351
Cdd:PLN02467 238 GSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 352 IKtNLHVGNGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKR-HQLGKNFF-EPTLLSNVTRDMLCSHEETFG 429
Cdd:PLN02467 318 AK-NIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRpEHLKKGFFiEPTIITDVTTSMQIWREEVFG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 430 PLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGI 509
Cdd:PLN02467 397 PVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGL 476
|
....*....
gi 2080330760 510 DEYLELKYV 518
Cdd:PLN02467 477 ENYLSVKQV 485
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
88-518 |
5.87e-121 |
|
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: 361.89 E-value: 5.87e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 88 AAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVI 167
Cdd:cd07105 4 QAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 168 YTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPC 247
Cdd:cd07105 84 PSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 248 SRAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQT 327
Cdd:cd07105 164 SPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 328 CVCSNRFLVQRGIHDSFVKKFAEAIKtnlhvgNGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGK-RHQLGKN 406
Cdd:cd07105 244 CMSTERIIVHESIADEFVEKLKAAAE------KLFAGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLaDESPSGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 407 FFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEgliS 486
Cdd:cd07105 318 SMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHING---M 394
|
410 420 430
....*....|....*....|....*....|....*.
gi 2080330760 487 SVE----CPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07105 395 TVHdeptLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
50-509 |
7.13e-121 |
|
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: 363.43 E-value: 7.13e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 50 ESFVGGRWLPAAAAF-PVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSW-RGVSAKERSSLLRKWYDLMMQNKDDLA 127
Cdd:cd07082 3 KYLINGEWKESSGKTiEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWwPTMPLEERIDCLHKFADLLKENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 128 KIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGD----VIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKV 203
Cdd:cd07082 83 NLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDslpgDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 204 GAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIpcsRAKAKEVGEALCTDPLVSKISFTGSTATGKILLhh 283
Cdd:cd07082 163 IPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVV---TGRGREIGDPLVTHGRIDVISFTGSTEVGNRLK-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 284 AAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIkTNLHVGNGFE 363
Cdd:cd07082 238 KQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEV-AKLKVGMPWD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 364 ERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRhqLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEA 443
Cdd:cd07082 317 NGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2080330760 444 VAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGlissveC-------PFGGVKQSGLGREGSKYGI 509
Cdd:cd07082 395 IELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSK------CqrgpdhfPFLGRKDSGIGTQGIGDAL 461
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
29-514 |
8.58e-121 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 364.97 E-value: 8.58e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 29 PAQPRRSAGGPAGLSAALLRteSFVGGRWLPAAAAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKER 108
Cdd:PRK09407 1 ATTTALPMPAPSALTFERLR--RLTARVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 109 SSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRvygdvIYTPAKEK-------RALVLKQ 181
Cdd:PRK09407 79 AAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPK-----LLAPRRRAgalpvltKTTELRQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 182 PLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSRAkakEVGEALCt 261
Cdd:PRK09407 154 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGP---VVGTALV- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 262 dPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIH 341
Cdd:PRK09407 230 -DNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 342 DSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGK-RHQLGKNFFEPTLLSNVTRDM 420
Cdd:PRK09407 309 DEFVRAFVAAVR-AMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKaRPDLGPLFYEPTVLTGVTPDM 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 421 LCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLIS---SVECPFGGVKQ 497
Cdd:PRK09407 388 ELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAawgSVDAPMGGMKD 467
|
490
....*....|....*..
gi 2080330760 498 SGLGREGSKYGIDEYLE 514
Cdd:PRK09407 468 SGLGRRHGAEGLLKYTE 484
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
52-519 |
1.10e-119 |
|
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: 360.60 E-value: 1.10e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCS-WRGVSAKERSSLLRKWYDLMMQNKDDLAK 128
Cdd:cd07113 3 FIDGRPVAGQSEkrLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 129 IITAESGKPLKEAQG-EVAYSALFLEWFSEEARRVYGDV----IYTPAKEK-RALVLKQPLGVAAVITPWNFPSAMITRK 202
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETlapsIPSMQGERyTAFTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 203 VGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIpcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLH 282
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVV----NGKGAVGAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 283 HAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGF 362
Cdd:cd07113 239 QAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSS-FQVGSPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 363 EERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQlGKNFF-EPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEE 441
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA-GEGYFvQPTLVLARSADSRLMREETFGPVVSFVPYEDEE 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2080330760 442 EAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 519
Cdd:cd07113 397 ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
52-516 |
6.06e-119 |
|
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: 358.58 E-value: 6.06e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAA--AAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKI 129
Cdd:cd07559 4 FINGEWVAPSkgEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 130 ITAESGKPLKEAQG-EVAYSALFLEWFSEEARRVYGDvIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALA 208
Cdd:cd07559 84 ETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGS-LSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 209 AGCTVVVKPAEHTPFSALALAELADQAaIPPGVYNVIpcsRAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSV 288
Cdd:cd07559 163 AGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVV---TGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 289 KRVSMELGGHAPFIVFDSA-----NVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFE 363
Cdd:cd07559 239 IPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFE-AIKVGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 364 ERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKN----FFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDT 439
Cdd:cd07559 318 PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLdkgyFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2080330760 440 EEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 516
Cdd:cd07559 398 EEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
49-518 |
1.36e-118 |
|
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: 357.81 E-value: 1.36e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 49 TESFVGGRWLPAAA--AFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAF---CSWRGVSAKERSSLLRKWYDLMMQNK 123
Cdd:cd07141 7 TKIFINNEWHDSVSgkTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 124 DDLAKIITAESGKP-LKEAQGEVAYSALFLEWFSEEARRVYGDVIytPAKEKR-ALVLKQPLGVAAVITPWNFPSAMITR 201
Cdd:cd07141 87 AYLASLETLDNGKPfSKSYLVDLPGAIKVLRYYAGWADKIHGKTI--PMDGDFfTYTRHEPVGVCGQIIPWNFPLLMAAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 202 KVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSRAKAkevGEALCTDPLVSKISFTGSTATGKILL 281
Cdd:cd07141 165 KLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTA---GAAISSHPDIDKVAFTGSTEVGKLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 282 HHAAGS-VKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTNLhVGN 360
Cdd:cd07141 242 QAAGKSnLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRV-VGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 361 GFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTE 440
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2080330760 441 EEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
55-518 |
2.73e-118 |
|
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: 356.61 E-value: 2.73e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 55 GRWLPAAA--AFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITA 132
Cdd:cd07151 1 GEWRDGTSerTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 133 ESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVI--YTPAKEKRalVLKQPLGVAAVITPWNFPSAMITRKVGAALAAG 210
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILpsDVPGKENR--VYREPLGVVGVISPWNFPLHLSMRSVAPALALG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 211 CTVVVKPAEHTPFSA-LALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVK 289
Cdd:cd07151 159 NAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVV---GAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 290 RVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQG 369
Cdd:cd07151 236 KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVK-ALPYGDPSDPDTVVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 370 PLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHqlgKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANA 449
Cdd:cd07151 315 PLINESQVDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 450 ADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLIS-SVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
44-518 |
5.65e-117 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 353.80 E-value: 5.65e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 44 AALLRTESFVGGRWLPAA--AAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQ 121
Cdd:PRK13252 2 SRQPLQSLYIDGAYVEATsgETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 122 NKDDLAKIITAESGKPLKEAQ-GEVAYSALFLEWFSEEARRVYGDVI--------YTpakeKRalvlkQPLGVAAVITPW 192
Cdd:PRK13252 82 RNDELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIplrggsfvYT----RR-----EPLGVCAGIGAW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 193 NFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSRakakEVGEALCTDPLVSKISFTG 272
Cdd:PRK13252 153 NYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG----RVGAWLTEHPDIAKVSFTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 273 STATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQtcVCSN--RFLVQRGIHDSFVKKFAE 350
Cdd:PRK13252 229 GVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQ--VCTNgtRVFVQKSIKAAFEARLLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 351 AIKtNLHVGNGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQ---LGKNFF-EPTLLSNVTRDMLCSHEE 426
Cdd:PRK13252 307 RVE-RIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTeggFANGAFvAPTVFTDCTDDMTIVREE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 427 TFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSK 506
Cdd:PRK13252 386 IFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGI 465
|
490
....*....|..
gi 2080330760 507 YGIDEYLELKYV 518
Cdd:PRK13252 466 ATLEHYTQIKSV 477
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
66-516 |
1.47e-116 |
|
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: 351.66 E-value: 1.47e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADcgvpETRAAVRAAYEAFCSWRG-VSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGE 144
Cdd:cd07146 3 VRNPYTGEVVGTVPA----GTEEALREALALAASYRStLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 145 VAYSALFLEWFSEEARRVYGDVI----YTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEH 220
Cdd:cd07146 79 VGRAADVLRFAAAEALRDDGESFscdlTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 221 TPFSALALAELADQAAIPPGVYNVIpcsRAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGsvKRVSMELGGHAP 300
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVV---TGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGY--KRQLLELGGNDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 301 FIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEKV 380
Cdd:cd07146 234 LIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAA-LVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 381 EKHVNDAVSKGATVVTGGKRHqlgKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYS 460
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2080330760 461 QDPAQIWRVAERLEVGMVGVNEGLISSVE-CPFGGVKQSGLG-REGSKYGIDEYLELK 516
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGgKEGVREAMKEMTNVK 447
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
49-518 |
2.48e-116 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 352.59 E-value: 2.48e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 49 TESFVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAF--CSWRGVSAKERSSLLRKWYDLMMQNKD 124
Cdd:PLN02766 21 TKLFINGEFVDAASGktFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFdhGPWPRMSGFERGRIMMKFADLIEEHIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 125 DLAKIITAESGKPLKEAQG-EVAYSALFLEWFSEEARRVYGDVIYTpAKEKRALVLKQPLGVAAVITPWNFPSAMITRKV 203
Cdd:PLN02766 101 ELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKM-SRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 204 GAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSRAKAkevGEALCTDPLVSKISFTGSTATGKILLHH 283
Cdd:PLN02766 180 APALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTA---GAAIASHMDVDKVSFTGSTEVGRKIMQA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 284 AAGS-VKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGF 362
Cdd:PLN02766 257 AATSnLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAK-DWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 363 EERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKrhQLGKN--FFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTE 440
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGK--PCGDKgyYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2080330760 441 EEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:PLN02766 414 EEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
112-518 |
7.96e-116 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 348.26 E-value: 7.96e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 112 LRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITP 191
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 192 WNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIpcsRAKAKEVGEALCTDPLVSKISFT 271
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLV---LGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 272 GSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEA 351
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 352 IKtNLHVGNGFEERTTQ-GPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGP 430
Cdd:PRK10090 238 MQ-AVQFGNPAERNDIAmGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 431 LAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGID 510
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLH 396
|
....*...
gi 2080330760 511 EYLELKYV 518
Cdd:PRK10090 397 EYLQTQVV 404
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
67-514 |
1.07e-114 |
|
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: 346.99 E-value: 1.07e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 67 HDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVA 146
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 147 YSALFLEWFSEEARRVYgdviyTPAKEKRAL-------VLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAE 219
Cdd:cd07101 81 DVAIVARYYARRAERLL-----KPRRRRGAIpvltrttVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 220 HTPFSALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDplVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHA 299
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVT---GPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 300 PFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEK 379
Cdd:cd07101 231 PMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTR-ALRLGAALDYGPDMGSLISQAQLDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 380 VEKHVNDAVSKGATVVTGGK-RHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYF 458
Cdd:cd07101 310 VTAHVDDAVAKGATVLAGGRaRPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASV 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2080330760 459 YSQDPAQIWRVAERLEVGMVGVNEGLIS---SVECPFGGVKQSGLGREGSKYGIDEYLE 514
Cdd:cd07101 390 WTRDGARGRRIAARLRAGTVNVNEGYAAawaSIDAPMGGMKDSGLGRRHGAEGLLKYTE 448
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
52-516 |
1.30e-114 |
|
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: 347.52 E-value: 1.30e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAA--AAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKI 129
Cdd:cd07117 4 FINGEWVKGSsgETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 130 ITAESGKPLKEAQG-EVAYSALFLEWFSEEARRVYGDVIYTPaKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALA 208
Cdd:cd07117 84 ETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMID-EDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 209 AGCTVVVKPAEHTPFSALALAELADQAaIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSV 288
Cdd:cd07117 163 AGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVT---GKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 289 KRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQ 368
Cdd:cd07117 239 IPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFE-NVKVGNPLDPDTQM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 369 GPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGK----NFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAV 444
Cdd:cd07117 318 GAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGldkgFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2080330760 445 AIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 516
Cdd:cd07117 398 DMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMK 469
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
66-518 |
2.28e-114 |
|
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: 346.27 E-value: 2.28e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLK-EAQGE 144
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 145 VAYSALFLEWFSEEARRVYGDVIytPAKEKR-ALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPF 223
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETL--PFGPDVlTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 224 SALALAELAdQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIV 303
Cdd:cd07108 159 AVLLLAEIL-AQVLPAGVLNVIT---GYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 304 FDSANVDQAVAGAMAS-KFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEKVEK 382
Cdd:cd07108 235 FPDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSK-LKIGDPLDEATDIGAIISEKQFAKVCG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 383 HVNDAVS-KGATVVTGG---KRHQLGKNFF-EPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGY 457
Cdd:cd07108 314 YIDLGLStSGATVLRGGplpGEGPLADGFFvQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAY 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2080330760 458 FYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYG-IDEYLELKYV 518
Cdd:cd07108 394 VWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
52-515 |
1.58e-111 |
|
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: 340.74 E-value: 1.58e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAAAAFPVHDPA-SGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKII 130
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 131 TAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKqPLGVAAVITPWNFPSAMITRKVGAALAAG 210
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTTAALVTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 211 CTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGkILLHHAAGS--- 287
Cdd:cd07124 195 NTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLP---GPGEEVGDYLVEHPDVRFIAFTGSREVG-LRIYERAAKvqp 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 288 ----VKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFE 363
Cdd:cd07124 271 gqkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKA-LKVGDPED 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 364 ERTTQGPLIDEKAVEKVEKHVNDAVSKGaTVVTGGKR--HQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEE 441
Cdd:cd07124 350 PEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVleLAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFD 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2080330760 442 EAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNE---GLISSVEcPFGGVKQSGLgreGSKYGIDEYLEL 515
Cdd:cd07124 429 EALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRkitGALVGRQ-PFGGFKMSGT---GSKAGGPDYLLQ 501
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
72-518 |
1.80e-111 |
|
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: 338.11 E-value: 1.80e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 72 GAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVAYSALF 151
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 152 LEWFSEEARRVYGDVIyTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSA-LALAE 230
Cdd:cd07152 81 LHEAAGLPTQPQGEIL-PSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 231 LADQAAIPPGVYNVIPcsraKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVD 310
Cdd:cd07152 160 LFEEAGLPAGVLHVLP----GGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 311 QAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEKVEKHVNDAVSK 390
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAK-HLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 391 GATVVTGGKRHQLgknFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVA 470
Cdd:cd07152 315 GARLEAGGTYDGL---FYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2080330760 471 ERLEVGMVGVNEGLISSvEC--PFGGVKQSGLG-REGSKYGIDEYLELKYV 518
Cdd:cd07152 392 DRLRTGMLHINDQTVND-EPhnPFGGMGASGNGsRFGGPANWEEFTQWQWV 441
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
49-518 |
2.54e-109 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 336.01 E-value: 2.54e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 49 TESFVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAF--CSWRGVSAKERSSLLRKWYDLMMQNKD 124
Cdd:PLN02466 58 TQLLINGQFVDAASGktFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFdeGPWPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 125 DLAKIITAESGKPLKE-AQGEVAYSALFLEWFSEEARRVYGDVIytPAKEKRAL-VLKQPLGVAAVITPWNFPSAMITRK 202
Cdd:PLN02466 138 ELAALETWDNGKPYEQsAKAELPMFARLFRYYAGWADKIHGLTV--PADGPHHVqTLHEPIGVAGQIIPWNFPLLMFAWK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 203 VGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSRAKAkevGEALCTDPLVSKISFTGSTATGKILLH 282
Cdd:PLN02466 216 VGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTA---GAALASHMDVDKLAFTGSTDTGKIVLE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 283 HAAGS-VKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKF-AEAIKTNlhVGN 360
Cdd:PLN02466 293 LAAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAkARALKRV--VGD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 361 GFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTE 440
Cdd:PLN02466 371 PFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDL 450
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2080330760 441 EEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:PLN02466 451 DEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
52-520 |
3.76e-109 |
|
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: 333.69 E-value: 3.76e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCS--WRGVSAKERSSLLRKWYDLMMQNKDDLA 127
Cdd:cd07140 9 FINGEFVDAEGGktYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 128 KIITAESGKPLKEA-QGEVAYSALFLEWFSEEARRVYGDVI-YTPAKEKRALVL--KQPLGVAAVITPWNFPSAMITRKV 203
Cdd:cd07140 89 TIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIpINQARPNRNLTLtkREPIGVCGIVIPWNYPLMMLAWKM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 204 GAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSrakAKEVGEALCTDPLVSKISFTGSTATGKILLHH 283
Cdd:cd07140 169 AACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGS---GSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 284 AAGS-VKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGF 362
Cdd:cd07140 246 CAVSnLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKK-MKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 363 EERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTE-- 440
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdv 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 441 EEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCF 520
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
66-518 |
1.72e-108 |
|
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: 330.88 E-value: 1.72e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEV 145
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 146 AYSALFLEWFSEEARRVYGDVIYTPAkekRAL--VLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPF 223
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGG---RNLhyTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 224 SALALAELADQAaIPPGVYNVIPCSRAkakEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIV 303
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGA---TAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 304 FDSANVDQAVAGAMAS-KFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEKVEK 382
Cdd:cd07107 234 FPDADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAA-IKVGDPTDPATTMGPLVSRQQYDRVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 383 HVNDAVSKGATVVTGGKR---HQLGKNFF-EPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYF 458
Cdd:cd07107 313 YIDSAKREGARLVTGGGRpegPALEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 459 YSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07107 393 WTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
67-520 |
1.97e-105 |
|
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: 323.48 E-value: 1.97e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 67 HDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQ-GEV 145
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 146 AYSALFLEW--------FSEEARRVYGDVIYtpakeKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKP 217
Cdd:cd07098 81 LVTCEKIRWtlkhgekaLRPESRPGGLLMFY-----KRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 218 AEHTPFSALALAELADQA----AIPPGVYNVIPCsrakAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSM 293
Cdd:cd07098 156 SEQVAWSSGFFLSIIREClaacGHDPDLVQLVTC----LPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 294 ELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLID 373
Cdd:cd07098 232 ELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQA-LRQGPPLDGDVDVGAMIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 374 EKAVEKVEKHVNDAVSKGATVVTGGKRHQLGK----NFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANA 449
Cdd:cd07098 311 PARFDRLEELVADAVEKGARLLAGGKRYPHPEypqgHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANS 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2080330760 450 ADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVEC--PFGGVKQSGLGREGSKYGIDEYLELKYVCF 520
Cdd:cd07098 391 TEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQqlPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
49-510 |
4.28e-103 |
|
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: 317.92 E-value: 4.28e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 49 TESFVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDL 126
Cdd:cd07085 1 LKLFINGEWVESKTTewLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 127 AKIITAESGKPLKEAQGEV---------AYSA--LFLEWFSEEARRvygDVIytpakekrALVLKQPLGVAAVITPWNFP 195
Cdd:cd07085 81 ARLITLEHGKTLADARGDVlrglevvefACSIphLLKGEYLENVAR---GID--------TYSYRQPLGVVAGITPFNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 196 sAMITR-KVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCsrakAKEVGEALCTDPLVSKISFTGST 274
Cdd:cd07085 150 -AMIPLwMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG----GKEAVNALLDHPDIKAVSFVGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 275 ATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCV-CSNRFLVQrGIHDSFVKKFAEAIK 353
Cdd:cd07085 225 PVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMaLSVAVAVG-DEADEWIPKLVERAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 354 tNLHVGNGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGK----NFFEPTLLSNVTRDMLCSHEETFG 429
Cdd:cd07085 304 -KLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGyengNFVGPTILDNVTPDMKIYKEEIFG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 430 PLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVEC-PFGGVKQSGLGrEGSKYG 508
Cdd:cd07085 383 PVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFfSFGGWKGSFFG-DLHFYG 461
|
..
gi 2080330760 509 ID 510
Cdd:cd07085 462 KD 463
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
68-521 |
7.81e-100 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 308.59 E-value: 7.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 68 DPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVAY 147
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 148 SALFLEWFSEEARRVYGDVIYTPAK--EKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSA 225
Cdd:PRK09406 87 CAKGFRYYAEHAEALLADEPADAAAvgASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 226 LALAELADQAAIPPGVYNVIPCSRAKAkevgEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFD 305
Cdd:PRK09406 167 LYLADLFRRAGFPDGCFQTLLVGSGAV----EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 306 SANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEKVEKHVN 385
Cdd:PRK09406 243 SADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAA-LRVGDPTDPDTDVGPLATEQGRDEVEKQVD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 386 DAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQ 465
Cdd:PRK09406 322 DAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAE 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2080330760 466 IWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCFG 521
Cdd:PRK09406 402 QERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWIG 457
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
52-514 |
1.34e-99 |
|
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: 308.94 E-value: 1.34e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAA--AAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKI 129
Cdd:cd07111 25 FINGKWVKPEnrKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 130 ITAESGKPLKEAQ-GEVAYSALFLEWFSEEARrvygdviytpaKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALA 208
Cdd:cd07111 105 ESLDNGKPIRESRdCDIPLVARHFYHHAGWAQ-----------LLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 209 AGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIpcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSV 288
Cdd:cd07111 174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIV----TGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 289 KRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQ 368
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSH-LRVGDPLDKAIDM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 369 GPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIAN 448
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALAN 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2080330760 449 AADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLE 514
Cdd:cd07111 409 NTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLR 474
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
82-516 |
3.47e-98 |
|
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: 304.17 E-value: 3.47e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 82 GVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARR 161
Cdd:cd07102 16 SLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 162 VYGDVI-YTPAKEKRALVlKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPG 240
Cdd:cd07102 96 ALADIRvPEKDGFERYIR-REPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 241 VYNVIPCSrakaKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASK 320
Cdd:cd07102 175 VFQVLHLS----HETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 321 FRNSGQTCvCS-NRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGK 399
Cdd:cd07102 251 FFNSGQSC-CSiERIYVHESIYDAFVEAFVAVVK-GYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 400 R---HQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVG 476
Cdd:cd07102 329 LfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETG 408
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2080330760 477 MVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 516
Cdd:cd07102 409 TVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPK 448
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
52-518 |
1.01e-97 |
|
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: 304.00 E-value: 1.01e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAAAA-FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAF--CSW-RGVSAKERSslLRKWYDLMMQNKDDLA 127
Cdd:TIGR04284 4 LIDGKLVAGSAGtFPTVNPATEEVLGVAADATAADMDAAIAAARRAFdeTDWsRDTALRVRC--LRQLRDALRAHVEELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 128 KIITAESGKP--------LKEAQGEVAYSALFLEwfSEEARRVYGdvIYTPAKEK-RALVLKQPLGVAAVITPWNFPSAM 198
Cdd:TIGR04284 82 ELTIAEVGAPrmltagaqLEGPVDDLGFAADLAE--SYAWTTDLG--VASPMGIPtRRTLRREAVGVVGAITPWNFPHQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 199 ITRKVGAALAAGCTVVVKPAEHTPFSALALAEL-ADQAAIPPGVYNVIPCSRakaKEVGEALCTDPLVSKISFTGSTATG 277
Cdd:TIGR04284 158 NLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELiAEHTDFPPGVVNIVTSSD---HRLGALLAKDPRVDMVSFTGSTATG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 278 KILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLH 357
Cdd:TIGR04284 235 RAVMADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGS-IK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 358 VGNGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKR--HQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVI 435
Cdd:TIGR04284 314 PGDPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGRpaDRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 436 KFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLEL 515
Cdd:TIGR04284 394 AHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLET 473
|
...
gi 2080330760 516 KYV 518
Cdd:TIGR04284 474 KLI 476
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
47-516 |
4.24e-97 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 302.97 E-value: 4.24e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 47 LRTESFVGGRWLPAA--AAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCS--WRGVSAKERSSLLRKWYDLMMQN 122
Cdd:PRK09847 18 IENRLFINGEYTAAAenETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 123 KDDLAKIITAESGKPLKEA-QGEVAYSALFLEWFSEEARRVYGDVIYTPAKEkRALVLKQPLGVAAVITPWNFPSAMITR 201
Cdd:PRK09847 98 AEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHE-LAMIVREPVGVIAAIVPWNFPLLLTCW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 202 KVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILL 281
Cdd:PRK09847 177 KLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVT---GFGHEAGQALSRHNDIDAIAFTGSTRTGKQLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 282 HHAAGS-VKRVSMELGGHAPFIVF-DSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVG 359
Cdd:PRK09847 254 KDAGDSnMKRVWLEAGGKSANIVFaDCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQ-NWQPG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 360 NGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGgkRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDT 439
Cdd:PRK09847 333 HPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTS 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2080330760 440 EEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 516
Cdd:PRK09847 411 EEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
53-515 |
1.25e-87 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 278.74 E-value: 1.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 53 VGGRWLPAAAAFPVHDPASGAQL-GLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIIT 131
Cdd:PRK03137 41 IGGERITTEDKIVSINPANKSEVvGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 132 AESGKPLKEAQGEVAYSALFLEWFSEEARRvYGD---VIYTPAKEKRALVlkQPLGVAAVITPWNFPSAMITRKVGAALA 208
Cdd:PRK03137 121 KEAGKPWAEADADTAEAIDFLEYYARQMLK-LADgkpVESRPGEHNRYFY--IPLGVGVVISPWNFPFAIMAGMTLAAIV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 209 AGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSrakAKEVGEALCTDPLVSKISFTGSTATGKILLHHAA--- 285
Cdd:PRK03137 198 AGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGS---GSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAkvq 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 286 -GSV--KRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGf 362
Cdd:PRK03137 275 pGQIwlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKE-LTVGNP- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 363 EERTTQGPLIDEKAVEKVEKHVNDAVSKGaTVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEE 442
Cdd:PRK03137 353 EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDH 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2080330760 443 AVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNE---GLISSVEcPFGGVKQSGlgrEGSKYGIDEYLEL 515
Cdd:PRK03137 432 ALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRgctGAIVGYH-PFGGFNMSG---TDSKAGGPDYLLL 503
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
68-515 |
1.20e-84 |
|
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: 270.97 E-value: 1.20e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 68 DPASGAQ-LGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVA 146
Cdd:TIGR01237 52 NPCDKSEvVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 147 YSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSAL 226
Cdd:TIGR01237 132 EAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 227 ALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAA------GSVKRVSMELGGHAP 300
Cdd:TIGR01237 212 KFVEILEEAGLPKGVVQFVP---GSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkvqpgqKHLKRVIAEMGGKDT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 301 FIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEKV 380
Cdd:TIGR01237 289 VIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITES-LKVGPPDSADVYVGPVIDQKSFNKI 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 381 EKHVNDAVSKGaTVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYS 460
Cdd:TIGR01237 368 MEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVIS 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2080330760 461 QDPAQIWRVAERLEVGMVGVNE---GLISSVEcPFGGVKQSGLgreGSKYGIDEYLEL 515
Cdd:TIGR01237 447 NNRDHINRAKAEFEVGNLYFNRnitGAIVGYQ-PFGGFKMSGT---DSKAGGPDYLAL 500
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
58-518 |
1.92e-84 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 269.04 E-value: 1.92e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 58 LPAAAAFPVhDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKP 137
Cdd:PRK13968 4 TPATHAISV-NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 138 LKEAQGEVAYSALFLEWFSEearrvYGDVIYTP----AKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTV 213
Cdd:PRK13968 83 INQARAEVAKSANLCDWYAE-----HGPAMLKAeptlVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 214 VVKPAEHTPFSALALAELADQAAIPPGVYNVIpcsRAKAKEVGEALcTDPLVSKISFTGSTATGKILLHHAAGSVKRVSM 293
Cdd:PRK13968 158 LLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWL---NADNDGVSQMI-NDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 294 ELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLID 373
Cdd:PRK13968 234 ELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAA-LKMGDPRDEENALGPMAR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 374 EKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVG 453
Cdd:PRK13968 313 FDLRDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFG 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2080330760 454 LAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:PRK13968 393 LSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
50-516 |
2.09e-84 |
|
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: 269.32 E-value: 2.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 50 ESFVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLA 127
Cdd:cd07116 2 DNFIGGEWVAPVKGeyFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 128 KIITAESGKPLKEAQG-EVAYSALFLEWFSEEARRVYGDvIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAA 206
Cdd:cd07116 82 VAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGS-ISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 207 LAAGCTVVVKPAEHTPFSALALAELAdQAAIPPGVYNVIpcsRAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAG 286
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELI-GDLLPPGVVNVV---NGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 287 SVKRVSMELGGHAPFIVFDS------ANVDQAVAGAMASKFrNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGN 360
Cdd:cd07116 237 NIIPVTLELGGKSPNIFFADvmdaddAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKA-IKQGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 361 GFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKN----FFEPTLLSNvTRDMLCSHEETFGPLAPVIK 436
Cdd:cd07116 315 PLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 437 FDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELK 516
Cdd:cd07116 394 FKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
47-513 |
2.51e-83 |
|
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: 267.91 E-value: 2.51e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 47 LRTESFVGGRWLPAAAAFPVHDPASG-AQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDD 125
Cdd:cd07125 31 WEAIPIINGEETETGEGAPVIDPADHeRTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 126 LAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGA 205
Cdd:cd07125 111 LIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 206 ALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSRAkakEVGEALCTDPLVSKISFTGSTATGKIL---LH 282
Cdd:cd07125 191 ALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGE---EIGEALVAHPRIDGVIFTGSTETAKLInraLA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 283 HAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGF 362
Cdd:cd07125 268 ERDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMAS-LKVGDPW 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 363 EERTTQGPLIDEKAVEKVEKHVNdAVSKGATVVTGGKRHQLGKNFFEPTLLSNVTRDMLcsHEETFGPLAPVIKFDTE-- 440
Cdd:cd07125 347 DLSTDVGPLIDKPAGKLLRAHTE-LMRGEAWLIAPAPLDDGNGYFVAPGIIEIVGIFDL--TTEVFGPILHVIRFKAEdl 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2080330760 441 EEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSV--ECPFGGVKQSGLgreGSKYGIDEYL 513
Cdd:cd07125 424 DEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIvgRQPFGGWGLSGT---GPKAGGPNYL 495
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
88-510 |
9.81e-83 |
|
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: 263.75 E-value: 9.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 88 AAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVAYSALFLEwFSEEARRVYGDVI 167
Cdd:cd07095 4 AAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKID-ISIKAYHERTGER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 168 YTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIpc 247
Cdd:cd07095 83 ATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLV-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 248 srAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSV-KRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQ 326
Cdd:cd07095 161 --QGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPgKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 327 TCVCSNRFLVQRG-IHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGK 405
Cdd:cd07095 239 RCTCARRLIVPDGaVGDAFLERLVEAAK-RLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 406 NFFEPTLLsNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLI 485
Cdd:cd07095 318 AFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTT 396
|
410 420
....*....|....*....|....*.
gi 2080330760 486 -SSVECPFGGVKQSGLGREGSKYGID 510
Cdd:cd07095 397 gASSTAPFGGVGLSGNHRPSAYYAAD 422
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
52-505 |
1.21e-82 |
|
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: 264.84 E-value: 1.21e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAAAAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIIT 131
Cdd:cd07130 2 VYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 132 AESGKPLKEAQGEV------AYSALFLewfseeARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGA 205
Cdd:cd07130 82 LEMGKILPEGLGEVqemidiCDFAVGL------SRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 206 ALAAGCTVVVKPAEHTPFSALA----LAELADQAAIPPGVYNVIPCSRakakEVGEALCTDPLVSKISFTGSTATGKILL 281
Cdd:cd07130 156 ALVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGGA----DVGEALVKDPRVPLVSFTGSTAVGRQVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 282 HHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNG 361
Cdd:cd07130 232 QAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQ-VRIGDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 362 FEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLSnVTRDMLCSHEETFGPLAPVIKFDTEE 441
Cdd:cd07130 311 LDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLE 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2080330760 442 EAVAIANAADVGLAGYFYSQDPAQI--WRVAERLEVGMVGVNEGlISSVEC--PFGGVKQSGLGRE-GS 505
Cdd:cd07130 390 EAIAWNNEVPQGLSSSIFTTDLRNAfrWLGPKGSDCGIVNVNIG-TSGAEIggAFGGEKETGGGREsGS 457
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
66-511 |
3.82e-81 |
|
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: 260.43 E-value: 3.82e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPETRAAVRAAYEAF---CSWrgVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQ 142
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFldrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 143 GEVAYSALFLEWFSEEARRVYGDVI---YTPAKEKR-ALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPA 218
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGGREIpmgLTPASAGRiAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 219 EHTPFSALALAELADQAAIPPGVYNVIPCSRAkakeVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVkRVSMELGGH 298
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVPCENA----VAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT-RCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 299 APFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERTTQGPLIDEKAVE 378
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAE-KLVVGDPTDPDTEVGPLIRPREVD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 379 KVEKHVNDAVSKGATVVTGGKRhqLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYF 458
Cdd:cd07148 315 RVEEWVNEAVAAGARLLCGGKR--LSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAV 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2080330760 459 YSQDPAQIWRVAERLEVGMVGVNEGLISSVE-CPFGGVKQSGLGREGSKYGIDE 511
Cdd:cd07148 393 FTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYGTGGIPYTMHD 446
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
89-519 |
4.27e-78 |
|
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: 251.29 E-value: 4.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 89 AVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQ--------GEVAYSALFLEWFSEEaR 160
Cdd:cd07087 3 LVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlteiavvlGEIDHALKHLKKWMKP-R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 161 RVYGDVIYTPAKekrALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAaIPPG 240
Cdd:cd07087 82 RVSVPLLLQPAK---AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 241 VYNVIPcsraKAKEVGEALCTDPLvSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASK 320
Cdd:cd07087 158 AVAVVE----GGVEVATALLAEPF-DHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 321 FRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTNLhvGNGFEERTTQGPLIDEKAVEKVEKHVNDAvskgaTVVTGGKR 400
Cdd:cd07087 233 FLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFY--GEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGGQV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 401 HQlGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGV 480
Cdd:cd07087 306 DK-EERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2080330760 481 NEGLI--SSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 519
Cdd:cd07087 385 NDVLLhaAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVL 425
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
112-512 |
3.60e-74 |
|
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: 241.35 E-value: 3.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 112 LRKWYDLMMQNKDDLAKIITAESGKPLKEA--------QGEVAYSALFLEWFSEEARRVYGDVIYTPAKekrALVLKQPL 183
Cdd:cd07135 33 LKQLYWAVKDNEEAIVEALKKDLGRPPFETlltevsgvKNDILHMLKNLKKWAKDEKVKDGPLAFMFGK---PRIRKEPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 184 GVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAaIPPGVYNVIpcsRAKAKEVGEALctDP 263
Cdd:cd07135 110 GVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVV---QGGVPETTALL--EQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 264 LVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDS 343
Cdd:cd07135 184 KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 344 FVKKFAEAIktNLHVGNGFEERTTQGPLIDEKAVEKVEKHVNDavSKGaTVVTGGKRHQlGKNFFEPTLLSNVT-RDMLC 422
Cdd:cd07135 264 FVEELKKVL--DEFYPGGANASPDYTRIVNPRHFNRLKSLLDT--TKG-KVVIGGEMDE-ATRFIPPTIVSDVSwDDSLM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 423 ShEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLI--SSVECPFGGVKQSGL 500
Cdd:cd07135 338 S-EELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVDNAPFGGVGDSGY 416
|
410
....*....|..
gi 2080330760 501 GREGSKYGIDEY 512
Cdd:cd07135 417 GAYHGKYGFDTF 428
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
100-512 |
5.05e-73 |
|
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: 238.28 E-value: 5.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 100 WRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQ--------GEVAYSALFLE-WFseEARRVYGDVIYTP 170
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilpvlSEINHAIKHLKkWM--KPKRVRTPLLLFG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 171 AKEKralVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVynvipCSRA 250
Cdd:cd07134 92 TKSK---IRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-----AVFE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 251 KAKEVGEALCTDPlVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVC 330
Cdd:cd07134 164 GDAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 331 SNRFLVQRGIHDSFVKKFAEAIKTNLHVGNGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKrHQLGKNFFEP 410
Cdd:cd07134 243 PDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQ-FDAAQRYIAP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 411 TLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVE- 489
Cdd:cd07134 322 TVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNp 401
|
410 420
....*....|....*....|....
gi 2080330760 490 -CPFGGVKQSGLGREGSKYGIDEY 512
Cdd:cd07134 402 nLPFGGVNNSGIGSYHGVYGFKAF 425
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
52-518 |
2.35e-70 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 232.85 E-value: 2.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKI 129
Cdd:TIGR01722 4 WIGGKFAEGASGtyIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 130 ITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAA 209
Cdd:TIGR01722 84 ITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIAC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 210 GCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIpcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVK 289
Cdd:TIGR01722 164 GNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVV----HGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 290 RVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVC-SNRFLVqrGIHDSFVKKFAEAIKtNLHVGNGFEERTTQ 368
Cdd:TIGR01722 240 RVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAiSAAVLV--GAADEWVPEIRERAE-KIRIGPGDDPGAEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 369 GPLIDEKAVEKVEKHVNDAVSKGATVVTGG-----KRHQLGkNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEA 443
Cdd:TIGR01722 317 GPLITPQAKDRVASLIAGGAAEGAEVLLDGrgykvDGYEEG-NWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 444 VAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLisSVECP---FGGVKQSGLGREG--SKYGIDEYLELKYV 518
Cdd:TIGR01722 396 IALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPI--PVPLPyfsFTGWKDSFFGDHHiyGKQGTHFYTRGKTV 473
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
49-510 |
2.08e-69 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 230.62 E-value: 2.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 49 TESFVGGRWLP-AAAAFPVHDPASGAQL--GLVADCGvpETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDD 125
Cdd:PRK09457 1 MTLWINGDWIAgQGEAFESRNPVSGEVLwqGNDATAA--QVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 126 LAKIITAESGKPLKEAQGEVAYS----ALFLEWFSE---EARrvygdviyTPAKEKRALVLKQPLGVAAVITPWNFPSAM 198
Cdd:PRK09457 79 LAEVIARETGKPLWEAATEVTAMinkiAISIQAYHErtgEKR--------SEMADGAAVLRHRPHGVVAVFGPYNFPGHL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 199 ITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPcsraKAKEVGEALCTDPLVSKISFTGSTATGK 278
Cdd:PRK09457 151 PNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQ----GGRETGKALAAHPDIDGLLFTGSANTGY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 279 ILLHHAAGSVKRV-SMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIH-DSFVKKFAEAIKTnL 356
Cdd:PRK09457 227 LLHRQFAGQPEKIlALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKR-L 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 357 HVGNGFEERTT-QGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLsNVTRDMLCSHEETFGPLAPVI 435
Cdd:PRK09457 306 TVGRWDAEPQPfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVV 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2080330760 436 KFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLI-SSVECPFGGVKQSGLGREGSKYGID 510
Cdd:PRK09457 385 RYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTgASSAAPFGGVGASGNHRPSAYYAAD 460
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
52-515 |
9.88e-69 |
|
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: 229.00 E-value: 9.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAAAAFPVHDP-ASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKII 130
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 131 TAESGKPLKEAQGEVAYSALFLEWFSEEARRVYG--DVIYTPAKEKRALVLkQPLGVAAVITPWNFPSAMITRKVGAALA 208
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFY-VGLGAGVVISPWNFPVAIFTGMIVAPVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 209 AGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAA--- 285
Cdd:cd07083 181 VGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLP---GVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAArla 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 286 ---GSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIkTNLHVGNGF 362
Cdd:cd07083 258 pgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRA-ERLSVGPPE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 363 EERTTQGPLIDEKAVEKVEKHVNDAVSKGaTVVTGGKRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEE- 441
Cdd:cd07083 337 ENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDf 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2080330760 442 -EAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSV--ECPFGGVKQSGlgrEGSKYGIDEYLEL 515
Cdd:cd07083 416 aEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALvgVQPFGGFKLSG---TNAKTGGPHYLRR 489
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
95-519 |
1.76e-67 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 225.68 E-value: 1.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 95 EAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQ--------GEVAYSALFLEWFSEEaRRVYGDV 166
Cdd:PTZ00381 18 ESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmtevlltvAEIEHLLKHLDEYLKP-EKVDTVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 167 IYTPAKEKralVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAaIPPGVYNVIP 246
Cdd:PTZ00381 97 VFGPGKSY---IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 247 CSRakakEVGEALCTDPLvSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQ 326
Cdd:PTZ00381 173 GGV----EVTTELLKEPF-DHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 327 TCVCSNRFLVQRGIHDSFVKKFAEAIKTNLhvGNGFEERTTQGPLIDEKAVEKVEKHVNDavsKGATVVTGGKrHQLGKN 406
Cdd:PTZ00381 248 TCVAPDYVLVHRSIKDKFIEALKEAIKEFF--GEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE-VDIENK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 407 FFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGL-- 484
Cdd:PTZ00381 322 YVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVfh 401
|
410 420 430
....*....|....*....|....*....|....*
gi 2080330760 485 ISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVC 519
Cdd:PTZ00381 402 LLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVL 436
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
91-502 |
2.48e-63 |
|
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: 212.73 E-value: 2.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 91 RAAYEAFcswRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKE---------AQGEVAYSALFL-EWFSEEAR 160
Cdd:cd07133 8 KAAFLAN---PPPSLEERRDRLDRLKALLLDNQDALAEAISADFGHRSRHetllaeilpSIAGIKHARKHLkKWMKPSRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 161 RVygDVIYTPAKekrALVLKQPLGVAAVITPWNFP-----SAMItrkvgAALAAGCTVVVKPAEHTPFSALALAELADQA 235
Cdd:cd07133 85 HV--GLLFLPAK---AEVEYQPLGVVGIIVPWNYPlylalGPLI-----AALAAGNRVMIKPSEFTPRTSALLAELLAEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 236 aIPPGVYNVI---PcsrakakEVGEALCT---DPLVskisFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANV 309
Cdd:cd07133 155 -FDEDEVAVVtggA-------DVAAAFSSlpfDHLL----FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 310 DQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTNLHVGNGFEERTtqgPLIDEKAVEKVEKHVNDAVS 389
Cdd:cd07133 223 AKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNPDYT---SIINERHYARLQGLLEDARA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 390 KGATVVTGGKRHQL--GKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIW 467
Cdd:cd07133 300 KGARVIELNPAGEDfaATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQD 379
|
410 420 430
....*....|....*....|....*....|....*..
gi 2080330760 468 RVAERLEVGMVGVNEGL--ISSVECPFGGVKQSGLGR 502
Cdd:cd07133 380 RVLRRTHSGGVTINDTLlhVAQDDLPFGGVGASGMGA 416
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
52-504 |
1.55e-61 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 210.00 E-value: 1.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 52 FVGGRWLPAAAAFPVH--DPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKI 129
Cdd:PLN00412 19 YADGEWRTSSSGKSVAitNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 130 ITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYG-------DVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRK 202
Cdd:PLN00412 99 LVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGegkflvsDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 203 VGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVynvIPCSRAKAKEVGEALCTDPLVSKISFTGSTaTGkILLH 282
Cdd:PLN00412 179 IAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGL---ISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TG-IAIS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 283 HAAGSVKrVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGf 362
Cdd:PLN00412 254 KKAGMVP-LQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVA-KLTVGPP- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 363 EERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQlgkNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEE 442
Cdd:PLN00412 331 EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREG---NLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEE 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2080330760 443 AVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVE-CPFGGVKQSGLGREG 504
Cdd:PLN00412 408 GIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQG 470
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
108-510 |
5.50e-60 |
|
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: 204.28 E-value: 5.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 108 RSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQ--------GEVAYSALFLEWFSEEaRRVYGDVIYTPAKekrALVL 179
Cdd:cd07136 22 RIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYmteigfvlSEINYAIKHLKKWMKP-KRVKTPLLNFPSK---SYIY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 180 KQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELAdQAAIPPGVYNVIPcsraKAKEVGEAL 259
Cdd:cd07136 98 YEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKII-EETFDEEYVAVVE----GGVEENQEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 260 CTDPlVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRG 339
Cdd:cd07136 173 LDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHES 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 340 IHDSFVKKFAEAIKTnlHVGNGFEERTTQGPLIDEKAVEKVEKHVndavsKGATVVTGGKrHQLGKNFFEPTLLSNVTRD 419
Cdd:cd07136 252 VKEKFIKELKEEIKK--FYGEDPLESPDYGRIINEKHFDRLAGLL-----DNGKIVFGGN-TDRETLYIEPTILDNVTWD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 420 MLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLI--SSVECPFGGVKQ 497
Cdd:cd07136 324 DPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMhlANPYLPFGGVGN 403
|
410
....*....|...
gi 2080330760 498 SGLGREGSKYGID 510
Cdd:cd07136 404 SGMGSYHGKYSFD 416
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
51-513 |
3.43e-58 |
|
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: 200.91 E-value: 3.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 51 SFVGGRWLPAAAAFPVHDPAS-GAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKI 129
Cdd:TIGR01238 40 PIIGHSYKADGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 130 ITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYtpakekralvlkQPLGVAAVITPWNFPSAMITRKVGAALAA 209
Cdd:TIGR01238 120 CVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSV------------ESRGVFVCISPWNFPLAIFTGQISAALAA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 210 GCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAgsvK 289
Cdd:TIGR01238 188 GNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLP---GRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLA---Q 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 290 RVS------MELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFE 363
Cdd:TIGR01238 262 REDapvpliAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQ-ELKVGVPHL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 364 ERTTQGPLIDEKAVEKVEKHVNDAVSKGATV---VTGGKRHQLGKNFFEPTLLSNVTRDMLcsHEETFGPLAPVIKFDTE 440
Cdd:TIGR01238 341 LTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTLFELDDIAEL--SEEVFGPVLHVVRYKAR 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2080330760 441 EEAVAI--ANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVEC--PFGGvkqSGLGREGSKYGIDEYL 513
Cdd:TIGR01238 419 ELDQIVdqINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGvqPFGG---QGLSGTGPKAGGPHYL 492
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
62-501 |
5.46e-56 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 202.79 E-value: 5.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 62 AAFPVHDPA-SGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKE 140
Cdd:PRK11905 567 GTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLAN 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 141 AQGEVAYSALFLEWFSEEARRVYGDVIYtpakekralvlkQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEH 220
Cdd:PRK11905 647 AIAEVREAVDFLRYYAAQARRLLNGPGH------------KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQ 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 221 TPFSALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGSTATGKI----LLHHAAGSVKRVSmELG 296
Cdd:PRK11905 715 TPLIAARAVRLLHEAGVPKDALQLLP---GDGRTVGAALVADPRIAGVMFTGSTEVARLiqrtLAKRSGPPVPLIA-ETG 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 297 GHAPFIVFDSANVDQAVAGAMASKFRNSGQTcvCSN-RFL-VQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDE 374
Cdd:PRK11905 791 GQNAMIVDSSALPEQVVADVIASAFDSAGQR--CSAlRVLcLQEDVADRVLTMLKGAMDE-LRIGDPWRLSTDVGPVIDA 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 375 KAVEKVEKHVNDAVSKGATVvtggKRHQLGKN-----FFEPTL--LSNVtRDMlcsHEETFGPLAPVIKFDTEE-EAV-- 444
Cdd:PRK11905 868 EAQANIEAHIEAMRAAGRLV----HQLPLPAEtekgtFVAPTLieIDSI-SDL---EREVFGPVLHVVRFKADElDRVid 939
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2080330760 445 AIaNAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSV--ECPFGGVKQSGLG 501
Cdd:PRK11905 940 DI-NATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVvgVQPFGGEGLSGTG 997
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
48-518 |
8.59e-56 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 196.89 E-value: 8.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 48 RTESFVGGRWLPAAAA--FPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDD 125
Cdd:PLN02419 113 RVPNLIGGSFVESQSSsfIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 126 LAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGA 205
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 206 ALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIpcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAA 285
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIV----HGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 286 GSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRfLVQRGIHDSFVKKFAEAIKTnLHVGNGFEER 365
Cdd:PLN02419 349 AKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALST-VVFVGDAKSWEDKLVERAKA-LKVTCGSEPD 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 366 TTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKR-----HQLGkNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTE 440
Cdd:PLN02419 427 ADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpgYEKG-NFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSF 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 441 EEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLisSVECP---FGGVKQSGLGREG--SKYGIDEYLEL 515
Cdd:PLN02419 506 DEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPI--PVPLPffsFTGNKASFAGDLNfyGKAGVDFFTQI 583
|
...
gi 2080330760 516 KYV 518
Cdd:PLN02419 584 KLV 586
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
51-513 |
1.78e-54 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 197.73 E-value: 1.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 51 SFVGGrwlpAAAAFPVHDPASGAQ-LGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKI 129
Cdd:PRK11904 555 PIING----EGEARPVVSPADRRRvVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIAL 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 130 ITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGD--VIYTPAKEKRALVLkQPLGVAAVITPWNFPSAMITRKVGAAL 207
Cdd:PRK11904 631 CVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGApeKLPGPTGESNELRL-HGRGVFVCISPWNFPLAIFLGQVAAAL 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 208 AAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSrakAKEVGEALCTDPLVSKISFTGSTATGKIL---LHHA 284
Cdd:PRK11904 710 AAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGD---GATVGAALTADPRIAGVAFTGSTETARIInrtLAAR 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 285 AGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTcvCSN-RFL-VQRGIHDSFVKKFAEAIKtNLHVGNGF 362
Cdd:PRK11904 787 DGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQR--CSAlRVLfVQEDIADRVIEMLKGAMA-ELKVGDPR 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 363 EERTTQGPLIDEKAVEKVEKHVnDAVSKGATVVTGGKRHQLGKN--FFEPTL--LSNVtrDMLcsHEETFGPLAPVIKFD 438
Cdd:PRK11904 864 LLSTDVGPVIDAEAKANLDAHI-ERMKREARLLAQLPLPAGTENghFVAPTAfeIDSI--SQL--EREVFGPILHVIRYK 938
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2080330760 439 TEEEAVAIA--NAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSV--ECPFGGvkqSGLGREGSKYGIDEYL 513
Cdd:PRK11904 939 ASDLDKVIDaiNATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVvgVQPFGG---QGLSGTGPKAGGPHYL 1014
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
51-513 |
3.87e-53 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 187.73 E-value: 3.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 51 SFVGGRWLPAAAAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKII 130
Cdd:PLN02315 23 CYVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 131 TAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYTPAKEKRALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAG 210
Cdd:PLN02315 103 SLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 211 CTVVVKPAEHTPFSALAL----AELADQAAIPPGVYNVIpCSRAkakEVGEALCTDPLVSKISFTGSTATGKILLHHAAG 286
Cdd:PLN02315 183 NCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSF-CGGA---EIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 287 SVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKtNLHVGNGFEERT 366
Cdd:PLN02315 259 RFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYK-QVKIGDPLEKGT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 367 TQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKNFFEPTLLSnVTRDMLCSHEETFGPLAPVIKFDTEEEAVAI 446
Cdd:PLN02315 338 LLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEI 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2080330760 447 ANAADVGLAGYFYSQDPAQI--WRVAERLEVGMVGVN---EGliSSVECPFGGVKQSGLGREGSKYGIDEYL 513
Cdd:PLN02315 417 NNSVPQGLSSSIFTRNPETIfkWIGPLGSDCGIVNVNiptNG--AEIGGAFGGEKATGGGREAGSDSWKQYM 486
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
42-501 |
1.26e-51 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 189.76 E-value: 1.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 42 LSAALLRTE-------SFVGGRwLPAAAAFPVHDPASGAQ-LGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLR 113
Cdd:COG4230 544 LSAALAAAAekqwqaaPLIAGE-AASGEARPVRNPADHSDvVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILE 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 114 KWYDLMMQNKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGdviytpakekrALVLKQPLGVAAVITPWN 193
Cdd:COG4230 623 RAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFA-----------APTVLRGRGVFVCISPWN 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 194 FPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKISFTGS 273
Cdd:COG4230 692 FPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLP---GDGETVGAALVADPRIAGVAFTGS 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 274 TATGKILLHHAAgsvKRvsmeLGGHAPFI----------VFDSANVDQAVAGAMASKFRNSGQTC-----VCsnrflVQR 338
Cdd:COG4230 769 TETARLINRTLA---AR----DGPIVPLIaetggqnamiVDSSALPEQVVDDVLASAFDSAGQRCsalrvLC-----VQE 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 339 GIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVvtggKRHQLGKN-----FFEPTL- 412
Cdd:COG4230 837 DIADRVLEMLKGAMAE-LRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLV----HQLPLPEEcangtFVAPTLi 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 413 -LSNVtRDMlcsHEETFGPLAPVIKFDTEE-EAV--AIaNAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSV 488
Cdd:COG4230 912 eIDSI-SDL---EREVFGPVLHVVRYKADElDKVidAI-NATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAV 986
|
490
....*....|....*
gi 2080330760 489 --ECPFGGVKQSGLG 501
Cdd:COG4230 987 vgVQPFGGEGLSGTG 1001
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
88-510 |
1.69e-48 |
|
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: 173.56 E-value: 1.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 88 AAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQ-GEVAYsalflewfseearrVYGDV 166
Cdd:cd07132 2 EAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVlSEILL--------------VKNEI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 167 IYT---------PAKEKRALV--------LKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALA 229
Cdd:cd07132 68 KYAisnlpewmkPEPVKKNLAtllddvyiYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 230 ELadqaaIP----PGVYNVIpcsRAKAKEVGEALctDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFD 305
Cdd:cd07132 148 EL-----IPkyldKECYPVV---LGGVEETTELL--KQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 306 SANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnlHVGNGFEERTTQGPLIDEKAVEKVEKhvn 385
Cdd:cd07132 218 SCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKE--FYGEDPKESPDYGRIINDRHFQRLKK--- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 386 daVSKGATVVTGGkRHQLGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQ 465
Cdd:cd07132 293 --LLSGGKVAIGG-QTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKV 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2080330760 466 IWRVAERLEVGMVGVNEGLISSV--ECPFGGVKQSGLGREGSKYGID 510
Cdd:cd07132 370 INKILSNTSSGGVCVNDTIMHYTldSLPFGGVGNSGMGAYHGKYSFD 416
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
40-501 |
2.15e-48 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 180.17 E-value: 2.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 40 AGLSAALLRTESfvgGRW---------LPAAAAFPVHDPASGA-QLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERS 109
Cdd:PRK11809 631 ASLSSALLASAH---QKWqaapmledpVAAGEMSPVINPADPRdIVGYVREATPAEVEQALESAVNAAPIWFATPPAERA 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 110 SLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVYGDVIYtpakekralvlkQPLGVAAVI 189
Cdd:PRK11809 708 AILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTH------------RPLGPVVCI 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 190 TPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPcsrAKAKEVGEALCTDPLVSKIS 269
Cdd:PRK11809 776 SPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLP---GRGETVGAALVADARVRGVM 852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 270 FTGSTATGKILLHHAAGsvkRVS---------MELGGHAPFIVFDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQRGI 340
Cdd:PRK11809 853 FTGSTEVARLLQRNLAG---RLDpqgrpipliAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDV 929
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 341 HDSFVKKFAEAIKtNLHVGNgfEER--TTQGPLIDEKAVEKVEKHVNDAVSKGATV----VTGGKRHQLGkNFFEPTLLS 414
Cdd:PRK11809 930 ADRTLKMLRGAMA-ECRMGN--PDRlsTDIGPVIDAEAKANIERHIQAMRAKGRPVfqaaRENSEDWQSG-TFVPPTLIE 1005
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 415 NVTRDMLcsHEETFGPLAPVIKFDTEE--EAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSVEC-- 490
Cdd:PRK11809 1006 LDSFDEL--KREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvq 1083
|
490
....*....|.
gi 2080330760 491 PFGGVKQSGLG 501
Cdd:PRK11809 1084 PFGGEGLSGTG 1094
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
83-518 |
1.56e-46 |
|
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: 167.97 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 83 VPETRAAVRAAYEafcSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEA-QGEV------AYSAL--FLE 153
Cdd:cd07137 1 APRLVRELRETFR---SGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVsvlvssCKLAIkeLKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 154 WFSEEarRVYGDVIYTPAKekrALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELA- 232
Cdd:cd07137 78 WMAPE--KVKTPLTTFPAK---AEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 233 ---DQAAIppgvyNVIpcsrAKAKEVGEALcTDPLVSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANV 309
Cdd:cd07137 153 eylDTKAI-----KVI----EGGVPETTAL-LEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 310 DQAVAGAMASKF-RNSGQTCVCSNRFLVQrgihDSFVKKFAEAIKTNLHVGNGFEERTTQ--GPLIDEKAVEKVEKHVND 386
Cdd:cd07137 223 KVAVRRIAGGKWgCNNGQACIAPDYVLVE----ESFAPTLIDALKNTLEKFFGENPKESKdlSRIVNSHHFQRLSRLLDD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 387 AvSKGATVVTGGKRHQlGKNFFEPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQI 466
Cdd:cd07137 299 P-SVADKIVHGGERDE-KNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELK 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2080330760 467 WRVAERLEVGMVGVNEGLISSV--ECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:cd07137 377 RRIVAETSSGGVTFNDTVVQYAidTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
82-518 |
1.52e-40 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 152.57 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 82 GVPETRAAVRAAYEafcSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQ----GEVAYSALFL----- 152
Cdd:PLN02203 7 TLEGSVAELRETYE---SGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYrdevGVLTKSANLAlsnlk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 153 EWFSEEarRVYGDVIYTPAKekrALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAela 232
Cdd:PLN02203 84 KWMAPK--KAKLPLVAFPAT---AEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 233 dqAAIP----PGVYNVIpcsrAKAKEVGEALCTDPLvSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIV--FDS 306
Cdd:PLN02203 156 --ANIPkyldSKAVKVI----EGGPAVGEQLLQHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 307 A-NVDQAVAGAMASKFRN-SGQTCVCSNRFLVQrgihDSFVKKFAEAIKTNLH--VGNGFEERTTQGPLIDEKAVEKVEK 382
Cdd:PLN02203 229 SrDTKVAVNRIVGGKWGScAGQACIAIDYVLVE----ERFAPILIELLKSTIKkfFGENPRESKSMARILNKKHFQRLSN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 383 HVNDAVSKgATVVTGGKRHQlgKNFF-EPTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQ 461
Cdd:PLN02203 305 LLKDPRVA-ASIVHGGSIDE--KKLFiEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTN 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2080330760 462 DPAQIWRVAERLEVGMVGVNEGLISSV--ECPFGGVKQSGLGREGSKYGIDEYLELKYV 518
Cdd:PLN02203 382 NEKLKRRILSETSSGSVTFNDAIIQYAcdSLPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
88-449 |
1.33e-31 |
|
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: 126.89 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 88 AAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARR-VYGDV 166
Cdd:cd07129 3 AAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgSWLDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 167 IYTPAKEKRALV-------LKQPLGVAAVITPWNFPSAMITrkVG----AALAAGCTVVVK--PAeHTPFSALaLAELAD 233
Cdd:cd07129 83 RIDPADPDRQPLprpdlrrMLVPLGPVAVFGASNFPLAFSV--AGgdtaSALAAGCPVVVKahPA-HPGTSEL-VARAIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 234 QAA----IPPGVYNVIPCSRakaKEVGEALCTDPLVSKISFTGSTATGKILLHHAAgsvKR-----VSMELGGHAPFIVF 304
Cdd:cd07129 159 AALratgLPAGVFSLLQGGG---REVGVALVKHPAIKAVGFTGSRRGGRALFDAAA---ARpepipFYAELGSVNPVFIL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 305 DSANvdQAVAGAMASKFRNS-----GQTCVCSNRFLVQRGIH-DSFVKKFAEAIK-----TNLHVG--NGFeerttqgpl 371
Cdd:cd07129 233 PGAL--AERGEAIAQGFVGSltlgaGQFCTNPGLVLVPAGPAgDAFIAALAEALAaapaqTMLTPGiaEAY--------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 372 idEKAVEKVEKHvndavsKGATVVTGGKRHQlGKNFFEPTLLSNVTRDMLCS---HEETFGPLAPVIKFDTEEEAVAIAN 448
Cdd:cd07129 302 --RQGVEALAAA------PGVRVLAGGAAAE-GGNQAAPTLFKVDAAAFLADpalQEEVFGPASLVVRYDDAAELLAVAE 372
|
.
gi 2080330760 449 A 449
Cdd:cd07129 373 A 373
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
176-523 |
1.01e-29 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 122.08 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 176 ALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQaAIPPGVYNVIPCSRAKAKEV 255
Cdd:PLN02174 106 AEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQ-YLDSSAVRVVEGAVTETTAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 256 GEALCtdplvSKISFTGSTATGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMASKFR-NSGQTCVCSNRF 334
Cdd:PLN02174 185 LEQKW-----DKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 335 LVQRgihdSFVKKFAEAIKTNLHV--GNGFEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGGKRHQLGKnfFEPTL 412
Cdd:PLN02174 260 LTTK----EYAPKVIDAMKKELETfyGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLK--IAPTI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 413 LSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVAERLEVGMVGVNEGLISSV--EC 490
Cdd:PLN02174 334 LLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTL 413
|
330 340 350
....*....|....*....|....*....|...
gi 2080330760 491 PFGGVKQSGLGREGSKYGIDEYLELKYVCFGGL 523
Cdd:PLN02174 414 PFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSL 446
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
85-499 |
3.31e-29 |
|
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: 120.77 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 85 ETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDdlAKIITAE---SGKPLKEAQGEVAYSAL-FLEWFSEEAR 160
Cdd:cd07123 70 LVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYR--YELNAATmlgQGKNVWQAEIDAACELIdFLRFNVKYAE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 161 RVYGDVIYTPAKEKRALVLKQPL-GVAAVITPWNFPSamitrkVGAALAA-----GCTVVVKPAEHTPFSALALAELADQ 234
Cdd:cd07123 148 ELYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTA------IGGNLAGapalmGNVVLWKPSDTAVLSNYLVYKILEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 235 AAIPPGVYNVIPCSrakAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSVK------RVSMELGGHAPFIVFDSAN 308
Cdd:cd07123 222 AGLPPGVINFVPGD---GPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtypRIVGETGGKNFHLVHPSAD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 309 VDQAVAGAMASKFRNSGQTCVCSNRFLVQRGIHDSFVKKFAEAIKTnLHVGNGFEERTTQGPLIDEKAVEKVEKHVNDA- 387
Cdd:cd07123 299 VDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKE-IKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAk 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 388 VSKGATVVTGGKRHQLGKNFFEPTLL--SNVTRDMLCshEETFGPLAPVIKFDTEE-EAV--AIANAADVGLAGYFYSQD 462
Cdd:cd07123 378 SDPEAEIIAGGKCDDSVGYFVEPTVIetTDPKHKLMT--EEIFGPVLTVYVYPDSDfEETleLVDTTSPYALTGAIFAQD 455
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2080330760 463 PAQIWRVAERLE--VGMVGVNEGLISSV--ECPFGGVKQSG 499
Cdd:cd07123 456 RKAIREATDALRnaAGNFYINDKPTGAVvgQQPFGGARASG 496
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
88-475 |
3.59e-27 |
|
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: 113.87 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 88 AAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAqGEVAYSALFLEWFSE--EARRVYGD 165
Cdd:cd07084 3 RALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAFviYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 166 VIYTPAKEKRALVLKQ--PLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQA-AIPPGVY 242
Cdd:cd07084 82 PGNHLGQGLKQQSHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAgLLPPEDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 243 NVIpcsrAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGSvkRVSMELGGHAPFIVFDSANVDQAVAGAMA-SKF 321
Cdd:cd07084 162 TLI----NGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYVAWQCVqDMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 322 RNSGQTCVCSNRFLVQrgiHDSFVKKFAEAIKTNLhvgngfEERTTQGPLIDEKAVEKVEKHVNDAVSKGATVVTGG--- 398
Cdd:cd07084 236 ACSGQKCTAQSMLFVP---ENWSKTPLVEKLKALL------ARRKLEDLLLGPVQTFTTLAMIAHMENLLGSVLLFSgke 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 399 -KRHQLGKNF--FEPTLLSNVTRDMLCSH----EETFGPLAPVIKFdtEEEAVAIANAADVGLAGYF----YSQDPAQIW 467
Cdd:cd07084 307 lKNHSIPSIYgaCVASALFVPIDEILKTYelvtEEIFGPFAIVVEY--KKDQLALVLELLERMHGSLtaaiYSNDPIFLQ 384
|
....*...
gi 2080330760 468 RVAERLEV 475
Cdd:cd07084 385 ELIGNLWV 392
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
48-470 |
5.53e-26 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 111.33 E-value: 5.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 48 RTESFVGGRWLP-AAAAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDL 126
Cdd:PRK11903 4 LLANYVAGRWQAgSGAGTPLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 127 AKIITAESGKPLKEAQGEVAYSALFLEWFSEEARRVyGDVIYTPAKEKRAL----------VLKQPLGVAAVITPWNFPS 196
Cdd:PRK11903 84 YDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAAL-GDARLLRDGEAVQLgkdpafqgqhVLVPTRGVALFINAFNFPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 197 AMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAI-PPGVYNVIPCSRA------KAKEVgealctdplvskIS 269
Cdd:PRK11903 163 WGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAglldhlQPFDV------------VS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 270 FTGSTATGKILLHHAA---GSVkRVSME---------LGGHAPfivfDSANVDQAVAGAMASKFRNSGQTCVCSNRFLVQ 337
Cdd:PRK11903 231 FTGSAETAAVLRSHPAvvqRSV-RVNVEadslnsallGPDAAP----GSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 338 RGIHDSfvkkFAEAIKTNLH---VGNGFEERTTQGPLIDEKAVEKVEKHVnDAVSKGATVVTGGKRHQL------GKNFF 408
Cdd:PRK11903 306 EALYDA----VAEALAARLAkttVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFALvdadpaVAACV 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2080330760 409 EPTLLsnVTRDMLCS---HE-ETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAQIWRVA 470
Cdd:PRK11903 381 GPTLL--GASDPDAAtavHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAA 444
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
50-477 |
1.01e-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: 107.36 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 50 ESFVGGRWL-PAAAAFPVHDPASGAQLGLVADCGVPETRAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAK 128
Cdd:cd07128 2 QSYVAGQWHaGTGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 129 IiTAESGKPLKEAQGEVAYSALFLEWFSEEARR--------VYGDV-------------IYTPakeKRalvlkqplGVAA 187
Cdd:cd07128 82 L-SAATGATRRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVeplskdgtfvgqhILTP---RR--------GVAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 188 VITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAI-PPGVYNVIPCSrakakeVGEALctDPLVS 266
Cdd:cd07128 150 HINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS------VGDLL--DHLGE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 267 K--ISFTGSTATGKILLHH---AAGSVkRVSME--------LGghaPFIVFDSANVD---QAVAGAMASKfrnSGQTCVC 330
Cdd:cd07128 222 QdvVAFTGSAATAAKLRAHpniVARSI-RFNAEadslnaaiLG---PDATPGTPEFDlfvKEVAREMTVK---AGQKCTA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 331 SNRFLVQRGIHDSFVKKFAEAIKTNLhVGNGFEERTTQGPLIDEKAVEKVEKHVnDAVSKGATVVTGGKRHQLGKN---- 406
Cdd:cd07128 295 IRRAFVPEARVDAVIEALKARLAKVV-VGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDRFEVVGadae 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2080330760 407 ---FFEPTLLsnVTRDMLCS---HE-ETFGPLAPVIKFDTEEEAVAIANAADVGLAGYFYSQDPAqiwrVAERLEVGM 477
Cdd:cd07128 373 kgaFFPPTLL--LCDDPDAAtavHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPA----FARELVLGA 444
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
182-471 |
1.85e-09 |
|
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: 60.18 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 182 PLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPaeHtPFSALALA-------ELADQAAIPPGVynVIPCSRAKAKE 254
Cdd:cd07127 193 PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKP--H-PAAILPLAitvqvarEVLAEAGFDPNL--VTLAADTPEEP 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 255 VGEALCTDPLVSKISFTGSTATGKILLHHAAGsvKRVSMELGGHAPFIVfDSANVDQAVAGAMASKFR-NSGQTCVCSNR 333
Cdd:cd07127 268 IAQTLATRPEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVV-DSTDDLKAMLRNLAFSLSlYSGQMCTTPQN 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 334 FLVQR-GI-----HDSFvKKFAEAIKTNLHVGNGFEERTTQ--GPLIDEKAVEKVEKhvndaVSKGATVVTGGKrhQLGK 405
Cdd:cd07127 345 IYVPRdGIqtddgRKSF-DEVAADLAAAIDGLLADPARAAAllGAIQSPDTLARIAE-----ARQLGEVLLASE--AVAH 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2080330760 406 NFFE------PTLLSNVTRDMLCSHEETFGPLAPVIKFDTEEEAVAIANA---ADVGLAGYFYSQDPAQIWRVAE 471
Cdd:cd07127 417 PEFPdarvrtPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvrEHGAMTVGVYSTDPEVVERVQE 491
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
87-401 |
1.82e-08 |
|
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: 56.46 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 87 RAAVRAAYEAFCSWRGVSAKER----SSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQgevaysalflewfseEARRV 162
Cdd:cd07077 23 NAIANALYDTRQRLASEAVSERgayiRSLIANWIAMMGCSESKLYKNIDTERGITASVGH---------------IQDVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 163 YGDVIYTpakekraLVLKQPLGVAAVITPWNFPSAMITrKVGAALAAGCTVVVKPAEHTPFSALALAeLADQAAIPP-GV 241
Cdd:cd07077 88 LPDNGET-------YVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALA-LLFQAADAAhGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 242 YNVIPCSRAKAKEVGEALCTDPLVSKISFTGSTATGKILLHHAAGsvKRVsMELGGHAPFIVFDS-ANVDQAVAGAMASK 320
Cdd:cd07077 159 KILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHSPH--IPV-IGFGAGNSPVVVDEtADEERASGSVHDSK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 321 FRNsGQTCVCSNRFLVQRGIHDSFVKKFAE---AIKTNLHVG-----------NGFEERTTQGPLIDEKAVEKVEKHVND 386
Cdd:cd07077 236 FFD-QNACASEQNLYVVDDVLDPLYEEFKLklvVEGLKVPQEtkplskettpsFDDEALESMTPLECQFRVLDVISAVEN 314
|
330
....*....|....*
gi 2080330760 387 AVskgATVVTGGKRH 401
Cdd:cd07077 315 AW---MIIESGGGPH 326
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
51-442 |
4.58e-08 |
|
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: 55.58 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 51 SFVGGRWLPAAAAFPVHDPASGAQLGLVADCGVPETRAAVRAAyeAFCSWRG----VSAKERSSLlrkWYDLMM------ 120
Cdd:cd07126 1 NLVAGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSL--RQCPKSGlhnpLKNPERYLL---YGDVSHrvahel 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 121 ---QNKDDLAKIITAESGKPLKEAQGEVAYSALFLEWFSEEARR-------VYGDViytpaKEKRALVLKQPLGVAAVIT 190
Cdd:cd07126 76 rkpEVEDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRflarsfnVPGDH-----QGQQSSGYRWPYGPVAIIT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 191 PWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGVYNVIPCSRAKAKEVgeALCTDPLVskISF 270
Cdd:cd07126 151 PFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKI--LLEANPRM--TLF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 271 TGSTATGKILLHHAAGSVKrvsMELGGHAPFIVF-DSANVDQAVAGAMASKFRNSGQTCVC-SNRFLVQRGIHDSFVKKF 348
Cdd:cd07126 227 TGSSKVAERLALELHGKVK---LEDAGFDWKILGpDVSDVDYVAWQCDQDAYACSGQKCSAqSILFAHENWVQAGILDKL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 349 AE-AIKTNLhvgngfeERTTQGPLIdEKAVEKVEKHVNDAVS-KGATVVTGGK---RHQLGKNF--FEPT--------LL 413
Cdd:cd07126 304 KAlAEQRKL-------EDLTIGPVL-TWTTERILDHVDKLLAiPGAKVLFGGKpltNHSIPSIYgaYEPTavfvpleeIA 375
|
410 420
....*....|....*....|....*....
gi 2080330760 414 SNVTRDMLCSheETFGPLAPVIKFDTEEE 442
Cdd:cd07126 376 IEENFELVTT--EVFGPFQVVTEYKDEQL 402
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
88-350 |
6.36e-07 |
|
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: 51.88 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 88 AAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKE-------AQGEVAYSAlflEWFSEEAR 160
Cdd:cd07081 3 DAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEdkviknhFAAEYIYNV---YKDEKTCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 161 RVYGDVIYTpakekrALVLKQPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPG 240
Cdd:cd07081 80 VLTGDENGG------TLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 241 V-YNVIPCSRAKAKEVGEALCTDPLVSKISFTGstatGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQAVAGAMAS 319
Cdd:cd07081 154 ApENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKS 229
|
250 260 270
....*....|....*....|....*....|.
gi 2080330760 320 KFRNSGQTCVCSNRFLVQRGIHDSFVKKFAE 350
Cdd:cd07081 230 KTFDNGVICASEQSVIVVDSVYDEVMRLFEG 260
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
66-316 |
9.58e-06 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 47.97 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 66 VHDPASGAQLGLVADCGVPET-RAAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESGKPLKEAQGE 144
Cdd:PRK15398 17 MLSSQTVSPPAAVGEMGVFASvDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDKIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 145 ----VAYSALFLEWFSEEARRvyGDviytpakekRALVLKQ--PLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKP- 217
Cdd:PRK15398 97 knvaAAEKTPGVEDLTTEALT--GD---------NGLTLIEyaPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPh 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 218 --AEHTpfSALALAELADQAAIPPGVYNVIPCSRAKAKEVGEALCTDPLVSKISFTGstatGKILLHHAAGSVKRVSMEL 295
Cdd:PRK15398 166 pgAKKV--SLRAIELLNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTG----GPAVVKAAMKSGKKAIGAG 239
|
250 260
....*....|....*....|....*
gi 2080330760 296 GGHAPFIVFDSANVDQA----VAGA 316
Cdd:PRK15398 240 AGNPPVVVDETADIEKAardiVKGA 264
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
181-481 |
5.60e-05 |
|
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: 45.56 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 181 QPLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEHTPFSALALAELADQAAIPPGV-YNVIPCSRAKAKEVGEAL 259
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGApEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 260 CTDPLVSKISFTGSTAtgkilLHHAAGSVKRVSMELG-GHAPFIVFDSANVDQAVAGAMASK-FRNsGQTCVCSNRFLVQ 337
Cdd:cd07122 174 MKHPDVDLILATGGPG-----MVKAAYSSGKPAIGVGpGNVPAYIDETADIKRAVKDIILSKtFDN-GTICASEQSVIVD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 338 RGIHDSFVKKFAEaiktnlhvgNGfeerttqGPLIDEKAVEKVEK-------HVN-DAVSKGATVVTGgkrhQLGKNFFE 409
Cdd:cd07122 248 DEIYDEVRAELKR---------RG-------AYFLNEEEKEKLEKalfddggTLNpDIVGKSAQKIAE----LAGIEVPE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 410 PTLLsnvtrdmLCSHEETFGP--------LAPVI---KFDTEEEAVAIANAA-DVGLAGY---FYSQDPAQIWRVAERLE 474
Cdd:cd07122 308 DTKV-------LVAEETGVGPeeplsrekLSPVLafyRAEDFEEALEKARELlEYGGAGHtavIHSNDEEVIEEFALRMP 380
|
....*..
gi 2080330760 475 VGMVGVN 481
Cdd:cd07122 381 VSRILVN 387
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
88-316 |
2.28e-03 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 40.30 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 88 AAVRAAYEAFCSWRGVSAKERSSLLRKWYDLMMQNKDDLAKIITAESG------KPLKEAQgeVAYSALFLEWFSEEARR 161
Cdd:cd07121 8 DAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGmgrvedKIAKNHL--AAEKTPGTEDLTTTAWS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 162 vyGDviytpakekRALVLKQ--PLGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKP---AEHTpfSALALAELADQAA 236
Cdd:cd07121 86 --GD---------NGLTLVEyaPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKV--SAYAVELINKAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080330760 237 IPPGVYNVIPCSRAKAKEVGEALCTDPLVSKISFTGstatGKILLHHAAGSVKRVSMELGGHAPFIVFDSANVDQA---- 312
Cdd:cd07121 153 EAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTG----GPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAardi 228
|
....
gi 2080330760 313 VAGA 316
Cdd:cd07121 229 VQGA 232
|
|
| |
