|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
28-479 |
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: 780.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEI 107
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 108 LYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSA 187
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 188 LALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDA 267
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPA-EIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 268 DLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDAT 347
Cdd:cd07103 240 DLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 348 AKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWR 427
Cdd:cd07103 320 AKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 505740937 428 VSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIKYLCL 479
Cdd:cd07103 400 VAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
5-479 |
0e+00 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 714.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 5 SLLKTKAYINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIEN 84
Cdd:PLN02278 21 GLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIAN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 85 QEELAQLLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRK 164
Cdd:PLN02278 101 KEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 165 AAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQS 244
Cdd:PLN02278 181 VGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMG-DAPEIGDALLASPKVRKITFTGSTAVGKKLMAGA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 245 ASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAG 324
Cdd:PLN02278 260 AATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 325 VNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIE 404
Cdd:PLN02278 340 VTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIA 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505740937 405 MANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIKYLCL 479
Cdd:PLN02278 420 IANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
28-475 |
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: 684.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEI 107
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 108 LYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSA 187
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 188 LALAELAHQAGLPAGLFNVITSTRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDA 267
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGSRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 268 DLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDAT 347
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 348 AKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWR 427
Cdd:TIGR01780 321 EKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 505740937 428 VSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:TIGR01780 401 VAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
5-481 |
0e+00 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 664.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 5 SLLKTKAYINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIEN 84
Cdd:PRK11241 7 TLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 85 QEELAQLLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRK 164
Cdd:PRK11241 87 QDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 165 AAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQS 244
Cdd:PRK11241 167 AGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAG-AVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 245 ASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAG 324
Cdd:PRK11241 246 AKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 325 VNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIE 404
Cdd:PRK11241 326 VTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505740937 405 MANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIKYLCLKV 481
Cdd:PRK11241 406 QANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
5-480 |
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: 626.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 5 SLLKTKAYINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIEN 84
Cdd:COG1012 2 TTPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 85 QEELAQLLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRK 164
Cdd:COG1012 82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 165 AAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITsTRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQS 244
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVT-GDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 245 ASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAG 324
Cdd:COG1012 241 AENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 325 VNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTR-GGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVI 403
Cdd:COG1012 321 TDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505740937 404 EMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNE-MAPFGGVKESGLGREGSRYGIDEFLEIKYLCLK 480
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVpQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
22-475 |
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: 573.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 22 DHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPIN 101
Cdd:pfam00171 5 ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 102 ESRGEILYGASFIEWFAEEAKRIYGDVLPQDKeNHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQ 181
Cdd:pfam00171 85 EARGEVDRAIDVLRYYAGLARRLDGETLPSDP-GRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 182 ETPLSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPS 261
Cdd:pfam00171 164 LTPLTALLLAELFEEAGLPAGVLNVVTGSGA-EVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 262 IVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQE 341
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 342 HIDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQD 421
Cdd:pfam00171 323 YVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSD 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 505740937 422 ISRIWRVSEALEYGIVGINEGLISN-EMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:pfam00171 403 LERALRVARRLEAGMVWINDYTTGDaDGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
49-479 |
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: 514.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 49 EYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDV 128
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 129 LPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVIT 208
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 209 STRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTC 288
Cdd:cd07078 161 GDGD-EVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 289 VCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGK-LHTRGGTFF 367
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKrLEGGKGYFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 368 EPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNE 447
Cdd:cd07078 320 PPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAE 399
|
410 420 430
....*....|....*....|....*....|...
gi 505740937 448 M-APFGGVKESGLGREGSRYGIDEFLEIKYLCL 479
Cdd:cd07078 400 PsAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
12-475 |
1.59e-175 |
|
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: 501.02 E-value: 1.59e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQL 91
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 92 LSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAA 171
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 172 GCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSVeIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKL 251
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSV-VGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 252 SLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLI 331
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 332 SQSAVNKIQEHIDDATAKGANLVIGGK-LHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTE 410
Cdd:cd07088 320 NEAALDKVEEMVERAVEAGATLLTGGKrPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSE 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505740937 411 FGLASYLYTQDISRIWRVSEALEYGIVGINEGlisNEMAPFG---GVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07088 400 YGLTSYIYTENLNTAMRATNELEFGETYINRE---NFEAMQGfhaGWKKSGLGGADGKHGLEEYLQTK 464
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
28-475 |
1.70e-156 |
|
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: 452.01 E-value: 1.70e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKK--WQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRG 105
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 106 EILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPL 185
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 186 SALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFD 265
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGP-ETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 266 DADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDD 345
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 346 ATAKGANLVIGGKLHT----RGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQD 421
Cdd:cd07114 320 AREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 505740937 422 ISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
28-479 |
2.66e-152 |
|
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: 441.23 E-value: 2.66e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESR-GE 106
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 107 ILYGASFIEWFAEEAKRIYGDVLPQDKeNHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLS 186
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDG-GALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 187 ALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDD 266
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGP-EAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 267 ADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDA 346
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 347 TAKGANLVIGGKLHT----RGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDI 422
Cdd:cd07093 319 RAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 505740937 423 SRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIKYLCL 479
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
9-475 |
8.98e-152 |
|
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: 440.88 E-value: 8.98e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 9 TKAYINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQA--QKKWQKVTPKERANLLRRWYNLVIENQE 86
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIERDRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 87 ELAQLLSLEQGKPINES-RGEILYGASFIEWFAEEAKRIYGDVLPQDKENHrLLVIKQGIGVVAAITPWNFPNAMITRKA 165
Cdd:cd07091 84 ELAALESLDNGKPLEESaKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFL-AYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 166 APAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSVeIGKVLTEHPTVRKVTFTGSTRVGKILM-AQS 244
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPT-AGAAISSHMDVDKIAFTGSTAVGRTIMeAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 245 ASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAG 324
Cdd:cd07091 242 KSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 325 VNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIE 404
Cdd:cd07091 322 TFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505740937 405 MANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07091 402 RANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
26-477 |
2.71e-148 |
|
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: 430.98 E-value: 2.71e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 26 FAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRG 105
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 106 EILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPL 185
Cdd:cd07150 81 ETTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 186 SALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFD 265
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGA-EVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 266 DADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDD 345
Cdd:cd07150 240 DADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 346 ATAKGANLVIGGKlhtRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRI 425
Cdd:cd07150 320 AVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 505740937 426 WRVSEALEYGIVGINEGLISNEM-APFGGVKESGLGREGSRYGIDEFLEIKYL 477
Cdd:cd07150 397 FKLAERLESGMVHINDPTILDEAhVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
12-475 |
1.27e-141 |
|
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: 414.59 E-value: 1.27e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQL 91
Cdd:cd07138 2 YIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 92 LSLEQGKPINESRG-EILYGASFIEWFAEEAKRIygdvlPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFA 170
Cdd:cd07138 82 ITLEMGAPITLARAaQVGLGIGHLRAAADALKDF-----EFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 171 AGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSVeIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKK 250
Cdd:cd07138 157 AGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPV-VGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 251 LSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPL 330
Cdd:cd07138 236 VALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 331 ISQSAVNKIQEHIDDATAKGANLVIGGKLHTRG---GTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMAN 407
Cdd:cd07138 316 ASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEGlerGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIAN 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505740937 408 DTEFGLASYLYTQDISRIWRVSEALEYGIVGINeGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07138 396 DTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
28-475 |
1.27e-141 |
|
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: 413.85 E-value: 1.27e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEI 107
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 108 LYGASFIEWFAEEAKRiygDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSA 187
Cdd:cd07106 81 GGAVAWLRYTASLDLP---DEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 188 LALAELAHQAgLPAGLFNVITStrSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDA 267
Cdd:cd07106 158 LKLGELAQEV-LPPGVLNVVSG--GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 268 DLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDAT 347
Cdd:cd07106 235 DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 348 AKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWR 427
Cdd:cd07106 315 AKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEA 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 505740937 428 VSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07106 395 VARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
51-477 |
2.58e-141 |
|
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: 412.31 E-value: 2.58e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 51 AIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLP 130
Cdd:cd07104 5 AYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 131 QDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSA-LALAELAHQAGLPAGLFNVITS 209
Cdd:cd07104 85 SDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKGVLNVVPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 210 TRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCV 289
Cdd:cd07104 165 GGS-EIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 290 CTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGklhTRGGTFFEP 369
Cdd:cd07104 244 AAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGG---TYEGLFYQP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 370 TVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNE-M 448
Cdd:cd07104 321 TVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDEpH 400
|
410 420
....*....|....*....|....*....
gi 505740937 449 APFGGVKESGLGREGSRYGIDEFLEIKYL 477
Cdd:cd07104 401 VPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
28-479 |
6.68e-138 |
|
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: 404.67 E-value: 6.68e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEI 107
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 108 LYGASFIEWFAEEAKRIYGDVLPQDK----ENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQET 183
Cdd:cd07149 83 DRAIETLRLSAEEAKRLAGETIPFDAspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 184 PLSALALAELAHQAGLPAGLFNVITSTRSVeIGKVLTEHPTVRKVTFTGSTRVGKILmaQSASTVKKLSLELGGNAPSIV 263
Cdd:cd07149 163 PLSALKLAELLLEAGLPKGALNVVTGSGET-VGDALVTDPRVRMISFTGSPAVGEAI--ARKAGLKKVTLELGSNAAVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 264 FDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHI 343
Cdd:cd07149 240 DADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 344 DDATAKGANLVIGGKlhtRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDIS 423
Cdd:cd07149 320 EEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQ 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 424 RIWRVSEALEYGIVGINEglISN----EMaPFGGVKESGLGREGSRYGIDEFLEIKYLCL 479
Cdd:cd07149 397 KALKAARELEVGGVMIND--SSTfrvdHM-PYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
12-475 |
6.29e-137 |
|
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: 402.88 E-value: 6.29e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHKTFAVTNPAN-QQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQ 90
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADlEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 91 LLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFA 170
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 171 AGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKK 250
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHG-RGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 251 LSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPL 330
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 331 ISQSAVNKIQEHIDDATAKGANLVIGGKLHTRG----GTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMA 406
Cdd:cd07131 321 INEAQLEKVLNYNEIGKEEGATLLLGGERLTGGgyekGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505740937 407 NDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEM-APFGGVKESGLG-REGSRYGIDEFLEIK 475
Cdd:cd07131 401 NDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVhLPFGGVKKSGNGhREAGTTALDAFTEWK 471
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
12-475 |
1.99e-135 |
|
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: 399.38 E-value: 1.99e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQA--QKKWQKVTPKERANLLRRWYNLVIENQEELA 89
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 90 QLLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQDKENHRLlVIKQGIGVVAAITPWNFPNAMITRKAAPAF 169
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISR-TVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 170 AAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVK 249
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGA-TVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 250 KLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGP 329
Cdd:cd07119 239 KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 330 LISQSAVNKIQEHIDDATAKGANLVIGGKLHTRG----GTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEM 405
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505740937 406 ANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINE-GLISNEmAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDyHPYFAE-APWGGYKQSGIGRELGPTGLEEYQETK 468
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
26-479 |
2.81e-135 |
|
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: 397.87 E-value: 2.81e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 26 FAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRG 105
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 106 EILYGASFIEWFAEEAKRIYGDVLPQD----KENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQ 181
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 182 ETPLSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPS 261
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGS-EVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 262 IVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQE 341
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 342 HIDDATAKGANLVIGGKlhTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQD 421
Cdd:cd07145 320 LVNDAVEKGGKILYGGK--RDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTND 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 505740937 422 ISRIWRVSEALEYGIVGINE-GLISNEMAPFGGVKESGLGREGSRYGIDEFLEIKYLCL 479
Cdd:cd07145 398 INRALKVARELEAGGVVINDsTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
55-479 |
9.10e-134 |
|
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: 390.82 E-value: 9.10e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 55 AAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQDKE 134
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 135 NHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITStRSVE 214
Cdd:cd06534 83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPG-GGDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 215 IGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRI 294
Cdd:cd06534 162 VGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 295 YVQAGIYDRFVEQFSakvaafkvgsaneagvnigplisqsavnkiqehiddatakganlviggklhtrggtffepTVLRD 374
Cdd:cd06534 242 LVHESIYDEFVEKLV------------------------------------------------------------TVLVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 375 VTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNE-MAPFGG 453
Cdd:cd06534 262 VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGpEAPFGG 341
|
410 420
....*....|....*....|....*.
gi 505740937 454 VKESGLGREGSRYGIDEFLEIKYLCL 479
Cdd:cd06534 342 VKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
12-475 |
2.41e-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: 393.54 E-value: 2.41e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDhkTFAVTNPAN-QQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQ 90
Cdd:cd07097 4 YIDGEWVAGGD--GEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 91 LLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFA 170
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 171 AGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKK 250
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGS-EVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 251 LSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPL 330
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 331 ISQSAVNKIQEHIDDATAKGANLVIGGKLHTRG--GTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMAND 408
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAND 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505740937 409 TEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEM-APFGGVKESGLG-REGSRYGIDEFLEIK 475
Cdd:cd07097 401 TEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYhVPFGGRKGSSYGpREQGEAALEFYTTIK 469
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
24-475 |
6.09e-133 |
|
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: 392.35 E-value: 6.09e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 24 KTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKK--WQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPIN 101
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 102 ESRGEILYG-ASFIEWFAEEAKRIYGDVLPQDKENHRLlVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPA 180
Cdd:cd07112 82 DALAVDVPSaANTFRWYAEAIDKVYGEVAPTGPDALAL-ITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 181 QETPLSALALAELAHQAGLPAGLFNVITSTrSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSA-STVKKLSLELGGNA 259
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGF-GHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 260 PSIVFDDA-DLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNK 338
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 339 IQEHIDDATAKGANLVIGGK--LHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASY 416
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKrvLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505740937 417 LYTQDISRIWRVSEALEYGIVGIN---EGLISnemAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNcfdEGDIT---TPFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
9-475 |
1.16e-130 |
|
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: 387.15 E-value: 1.16e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 9 TKAYINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQA-QKKWQKVTPKERANLLRRWYNLVIENQEE 87
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 88 LAQLLSLEQGKPINE-SRGEILYGASFIEWFAEEAKRIYGDVLPQDKENHRLlVIKQGIGVVAAITPWNFPNAMITRKAA 166
Cdd:cd07144 88 LAAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAY-TLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 167 PAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSVeIGKVLTEHPTVRKVTFTGSTRVGKILMAQSAS 246
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAV-AGSALAEHPDVDKIAFTGSTATGRLVMKAAAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 247 TVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVA-AFKVGSANEAGV 325
Cdd:cd07144 246 NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 326 NIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRG---GTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQV 402
Cdd:cd07144 326 VVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGlgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505740937 403 IEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07144 406 IKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
9-475 |
1.43e-128 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 381.56 E-value: 1.43e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 9 TKAYINGEYVqAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEEL 88
Cdd:PRK13473 3 TKLLINGELV-AGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 89 AQLLSLEQGKPINESRG-EILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAP 167
Cdd:PRK13473 82 ARLESLNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 168 AFAAGCAMVLKPAQETPLSALALAELAHQAgLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSAST 247
Cdd:PRK13473 162 ALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTG-RGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 248 VKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNI 327
Cdd:PRK13473 240 VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 328 GPLISQSAVNKIQEHIDDATAKG-ANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMA 406
Cdd:PRK13473 320 GPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 407 NDTEFGLASYLYTQDISRIWRVSEALEYGIVGINE-GLISNEMaPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:PRK13473 400 NDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNThFMLVSEM-PHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
51-475 |
1.66e-128 |
|
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: 379.88 E-value: 1.66e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 51 AIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVlP 130
Cdd:cd07100 4 ALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLADE-P 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 131 QDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLF-NVITS 209
Cdd:cd07100 83 IETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFqNLLID 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 210 TRSVEIgkvLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCV 289
Cdd:cd07100 163 SDQVEA---IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 290 CTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEP 369
Cdd:cd07100 240 AAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 370 TVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMA 449
Cdd:cd07100 320 TVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRL 399
|
410 420
....*....|....*....|....*.
gi 505740937 450 PFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07100 400 PFGGVKRSGYGRELGRFGIREFVNIK 425
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
30-481 |
2.41e-127 |
|
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: 377.55 E-value: 2.41e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 30 NPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRG-EIL 108
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 109 YGASFIEWFAEEAKRIYGDVLPQDKE--NHrllVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLS 186
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRGPflNY---TVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 187 ALALAELAHQAGLPAGLFNVITSTRSVeIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDD 266
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEV-AGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 267 ADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDA 346
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 347 TAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIW 426
Cdd:cd07115 319 REEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 505740937 427 RVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIKYLCLKV 481
Cdd:cd07115 399 RVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
27-479 |
6.21e-127 |
|
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: 376.77 E-value: 6.21e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 27 AVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGE 106
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 107 ILYGASFIEWFAEEAKRIYGDVLPQD----KENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQE 182
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGEEIPLDatqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 183 TPLSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSAstVKKLSLELGGNAPSI 262
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGERE-VLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 263 VFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEH 342
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 343 IDDATAKGANLVIGGKlhtRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDI 422
Cdd:cd07094 319 VEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 505740937 423 SRIWRVSEALEYGIVGINEGLI--SNEMaPFGGVKESGLGREGSRYGIDEFLEIKYLCL 479
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDSSAfrTDWM-PFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
5-475 |
1.66e-126 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 376.53 E-value: 1.66e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 5 SLLKTKAYINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIEN 84
Cdd:PRK13252 3 RQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 85 QEELAQLLSLEQGKPINESR-GEILYGASFIEWFAEEAKRIYGDVLPQdKENHRLLVIKQGIGVVAAITPWNFPNAMITR 163
Cdd:PRK13252 83 NDELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPL-RGGSFVYTRREPLGVCAGIGAWNYPIQIACW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 164 KAAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSVeiGKVLTEHPTVRKVTFTGSTRVGKILMAQ 243
Cdd:PRK13252 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV--GAWLTEHPDIAKVSFTGGVPTGKKVMAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 244 SASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQtcVCTN--RIYVQAGIYDRFVEQFSAKVAAFKVGSAN 321
Cdd:PRK13252 240 AAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQ--VCTNgtRVFVQKSIKAAFEARLLERVERIRIGDPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 322 EAGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRG----GTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFD 397
Cdd:PRK13252 318 DPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGgfanGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFD 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505740937 398 TEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINE-GLISNEMaPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:PRK13252 398 DEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwGESPAEM-PVGGYKQSGIGRENGIATLEHYTQIK 475
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
29-477 |
3.53e-125 |
|
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: 371.94 E-value: 3.53e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 29 TNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEIL 108
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 109 YGASFIEWFAEEAKRIYGD-------VLPqdkeNHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQ 181
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPrkvptglLMP----NKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 182 ETPLSALALAELAHQAGLPAGLFNVITSTRSVeiGKVLTEHPtVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPS 261
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGAT--GAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 262 IVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQE 341
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 342 HIDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQD 421
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 505740937 422 ISRIWRVSEALEYGIVGINEGLISNEM--APFGGVKESGLGREGSRYGIDEFLEIKYL 477
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGIpaLPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
12-475 |
4.90e-125 |
|
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: 372.67 E-value: 4.90e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVqAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQL 91
Cdd:cd07086 2 VIGGEWV-GSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 92 LSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAA 171
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 172 GCAMVLKPAQETPLSALALAELAHQA----GLPAGLFNVITStrSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSAST 247
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG--GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 248 VKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNI 327
Cdd:cd07086 239 FGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 328 GPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRG--GTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEM 405
Cdd:cd07086 319 GPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGepGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505740937 406 ANDTEFGLASYLYTQDISRI--WRVSEALEYGIVGINEGLISNEM-APFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07086 399 NNDVPQGLSSSIFTEDLREAfrWLGPKGSDCGIVNVNIPTSGAEIgGAFGGEKETGGGRESGSDAWKQYMRRS 471
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
28-477 |
3.73e-124 |
|
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: 369.76 E-value: 3.73e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEI 107
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 108 LYGASFIEWFAEEAKRI---YGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETP 184
Cdd:cd07110 81 DDVAGCFEYYADLAEQLdakAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 185 LSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVF 264
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGD-EAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 265 DDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHID 344
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 345 DATAKGANLVIGGKL--HTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDI 422
Cdd:cd07110 320 RGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 505740937 423 SRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIKYL 477
Cdd:cd07110 400 ERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
28-476 |
4.73e-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: 368.96 E-value: 4.73e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESR-GE 106
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 107 ILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLS 186
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 187 ALALAELAhQAGLPAGLFNVITSTRSVeIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDD 266
Cdd:cd07092 161 TLLLAELA-AEVLPPGVVNVVCGGGAS-AGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 267 ADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDA 346
Cdd:cd07092 239 ADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 347 tAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIW 426
Cdd:cd07092 319 -PAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAM 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 505740937 427 RVSEALEYGIVGINE-GLISNEMaPFGGVKESGLGREGSRYGIDEFLEIKY 476
Cdd:cd07092 398 RLSARLDFGTVWVNThIPLAAEM-PHGGFKQSGYGKDLSIYALEDYTRIKH 447
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
15-476 |
1.35e-123 |
|
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: 368.56 E-value: 1.35e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 15 GEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSL 94
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 95 EQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQD---KENHrllVIKQGIGVVAAITPWNFPNAMITRKAAPAFAA 171
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDvpgKENR---VYREPLGVVGVISPWNFPLHLSMRSVAPALAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 172 GCAMVLKPAQETPLSA-LALAELAHQAGLPAGLFNVITsTRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKK 250
Cdd:cd07151 158 GNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVV-GAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 251 LSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPL 330
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 331 ISQSAVNKIQEHIDDATAKGANLVIGGKlhtRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTE 410
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLVGGE---AEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505740937 411 FGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNE-MAPFGGVKESGLGREGSRYGIDEFLEIKY 476
Cdd:cd07151 394 YGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEpHVPFGGEKNSGLGRFNGEWALEEFTTDKW 460
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
51-475 |
3.33e-123 |
|
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: 366.13 E-value: 3.33e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 51 AIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLP 130
Cdd:cd07105 5 AVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 131 QDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITS- 209
Cdd:cd07105 85 SDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHs 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 210 -TRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTC 288
Cdd:cd07105 165 pEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQIC 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 289 VCTNRIYVQAGIYDRFVEQFSAKVAAFKVGsaneaGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGK-LHTRGGTFF 367
Cdd:cd07105 245 MSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLaDESPSGTSM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 368 EPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNE 447
Cdd:cd07105 320 PPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDE 399
|
410 420
....*....|....*....|....*....
gi 505740937 448 -MAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07105 400 pTLPHGGVKSSGYGRFNGKWGIDEFTETK 428
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
28-477 |
8.18e-123 |
|
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: 366.19 E-value: 8.18e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEI 107
Cdd:cd07147 3 VTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 108 LYGASFIEWFAEEAKRIYGDVLPQD----KENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQET 183
Cdd:cd07147 83 ARAIDTFRIAAEEATRIYGEVLPLDisarGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 184 PLSALALAELAHQAGLPAGLFNVITSTRsvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSAStvKKLSLELGGNAPSIV 263
Cdd:cd07147 163 PLSALILGEVLAETGLPKGAFSVLPCSR--DDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 264 FDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHI 343
Cdd:cd07147 239 DSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 344 DDATAKGANLVIGGKlhtRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDIS 423
Cdd:cd07147 319 NEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLE 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 505740937 424 RIWRVSEALEYGIVGINE--GLISNEMaPFGGVKESGLGREGSRYGIDEFLEIKYL 477
Cdd:cd07147 396 KALRAWDELEVGGVVINDvpTFRVDHM-PYGGVKDSGIGREGVRYAIEEMTEPRLL 450
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
28-475 |
9.10e-123 |
|
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: 366.18 E-value: 9.10e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKKW-QKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPI-NESRG 105
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVmTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 106 EILYGASFIEWFAEEAKRIYG----DVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQ 181
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWefdlPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 182 ETPLSALALAELAHQAGLPAGLFNVITSTrSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPS 261
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGS-DNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 262 IVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQE 341
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 342 HIDDATAKGANLVIGGK--LHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYT 419
Cdd:cd07089 320 YIARGRDEGARLVTGGGrpAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWS 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 505740937 420 QDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07089 400 ADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
28-478 |
4.25e-122 |
|
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: 364.32 E-value: 4.25e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEI 107
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 108 LYGASFIEWFAEEAKRIYGDVLPQDKENH---RllviKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETP 184
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPGGSFaytR----REPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 185 LSALALAELAHQAGLPAGLFNVITStrSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVF 264
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQG--GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 265 DDADLENAIEGIIASKFRNSGQtcVCTN--RIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEH 342
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQ--VCSNgtRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 343 IDDATAKGANLVIGG-----KLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYL 417
Cdd:cd07090 313 IESAKQEGAKVLCGGervvpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505740937 418 YTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIKYLC 478
Cdd:cd07090 393 FTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
9-480 |
6.35e-122 |
|
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: 364.75 E-value: 6.35e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 9 TKAYINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKK---WQKVTPKERANLLRRWYNLVIENQ 85
Cdd:cd07141 7 TKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 86 EELAQLLSLEQGKPINESRGEILYGA-SFIEWFAEEAKRIYGDVLPQDKeNHRLLVIKQGIGVVAAITPWNFPNAMITRK 164
Cdd:cd07141 87 AYLASLETLDNGKPFSKSYLVDLPGAiKVLRYYAGWADKIHGKTIPMDG-DFFTYTRHEPVGVCGQIIPWNFPLLMAAWK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 165 AAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSVEiGKVLTEHPTVRKVTFTGSTRVGKILM-AQ 243
Cdd:cd07141 166 LAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTA-GAAISSHPDIDKVAFTGSTEVGKLIQqAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 244 SASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEA 323
Cdd:cd07141 245 GKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 324 GVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVI 403
Cdd:cd07141 325 KTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505740937 404 EMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIKYLCLK 480
Cdd:cd07141 405 ERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
31-475 |
2.99e-121 |
|
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: 362.04 E-value: 2.99e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 31 PANQQIICELPDLSAEETEYAIACAAQAQKK--WQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEIL 108
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 109 YGASFIEWFAEEAKRIYGDV---LPQDKENhrlLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPL 185
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSynnLGDDMLG---LVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 186 SALALAELAHQAGLPAGLFNVITSTRSVeIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFD 265
Cdd:cd07118 161 TTLMLAELLIEAGLPAGVVNIVTGYGAT-VGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 266 DADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDD 345
Cdd:cd07118 240 DADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 346 ATAKGANLVIGGK-LHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISR 424
Cdd:cd07118 320 GRAEGATLLLGGErLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 505740937 425 IWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07118 400 ALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELK 450
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
12-475 |
6.39e-121 |
|
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: 362.23 E-value: 6.39e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQA-QKKW-QKVTPKERANLLRRWYNLVIENQEELA 89
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWgLKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 90 QLLSLEQGKPINE-SRGEILYGASFIEWFAEEAKRIYGDVLPQDKEnhRLLVIK-QGIGVVAAITPWNFPNAMITRKAAP 167
Cdd:cd07143 90 SIEALDNGKTFGTaKRVDVQASADTFRYYGGWADKIHGQVIETDIK--KLTYTRhEPIGVCGQIIPWNFPLLMCAWKIAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 168 AFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSVeIGKVLTEHPTVRKVTFTGSTRVG-KILMAQSAS 246
Cdd:cd07143 168 ALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRT-CGNAISSHMDIDKVAFTGSTLVGrKVMEAAAKS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 247 TVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVN 326
Cdd:cd07143 247 NLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 327 IGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMA 406
Cdd:cd07143 327 QGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRA 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505740937 407 NDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07143 407 NDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIK 475
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
10-475 |
6.73e-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: 361.89 E-value: 6.73e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 10 KAYINGEYVQAKDhKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTP-KERANLLRRWYNLVIENQEEL 88
Cdd:cd07082 3 KYLINGEWKESSG-KTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 89 AQLLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQDKENHRL----LVIKQGIGVVAAITPWNFP-NAMITr 163
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKgkiaQVRREPLGVVLAIGPFNYPlNLTVS- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 164 KAAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITsTRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQ 243
Cdd:cd07082 161 KLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVT-GRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 244 SAstVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEA 323
Cdd:cd07082 240 HP--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 324 GVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKlhTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVI 403
Cdd:cd07082 318 GVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAI 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505740937 404 EMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINE----GLisnEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07082 396 ELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSkcqrGP---DHFPFLGRKDSGIGTQGIGDALRSMTRRK 468
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
28-475 |
7.31e-121 |
|
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: 361.17 E-value: 7.31e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKK-WQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGE 106
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 107 ILYGASFIEWFAEEAKRIYGDVLPQDKENHrLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLS 186
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLGPGYF-VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 187 ALALAELAHQAGLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDD 266
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTG-LGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 267 ADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSAnEAGVNIGPLISQSAVNKIQEHIDDA 346
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPG-LEDPDLGPLISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 347 TAKGANLVIGG---KLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDIS 423
Cdd:cd07109 318 RARGARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 505740937 424 RIWRVSEALEYGIVGINE----GLIsnEMaPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07109 398 RALRVARRLRAGQVFVNNygagGGI--EL-PFGGVKKSGHGREKGLEALYNYTQTK 450
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
28-475 |
1.83e-120 |
|
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: 360.14 E-value: 1.83e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPI-NESRGE 106
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 107 ILYGASFIEWFAEEAKRIYGDVLPQDkENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLS 186
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFG-PDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 187 ALALAELAHQAgLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDD 266
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGE-ECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 267 ADLENAIEGIIAS-KFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDD 345
Cdd:cd07108 238 ADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 346 A-TAKGANLVIGGKLHTRG----GTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQ 420
Cdd:cd07108 318 GlSTSGATVLRGGPLPGEGpladGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 505740937 421 DISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYG-IDEFLEIK 475
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKK 453
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
12-475 |
7.52e-120 |
|
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: 359.20 E-value: 7.52e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQA--QKKWQKVTPKERANLLRRWYNLVIENQEELA 89
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 90 QLLSLEQGKPINESR-GEILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPA 168
Cdd:cd07139 82 RLWTAENGMPISWSRrAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 169 FAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRsvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTV 248
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADR--EVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 249 KKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIG 328
Cdd:cd07139 240 ARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 329 PLISQSAVNKIQEHIDDATAKGANLVIGGKL--HTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMA 406
Cdd:cd07139 320 PLASARQRERVEGYIAKGRAEGARLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIA 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505740937 407 NDTEFGLASYLYTQDISRIWRVSEALEYGIVGINeGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07139 400 NDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETK 467
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
9-475 |
2.23e-117 |
|
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: 352.95 E-value: 2.23e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 9 TKAYINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQA--QKKWQKVTPKERANLLRRWYNLVIENQE 86
Cdd:cd07142 4 TKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 87 ELAQLLSLEQGKPINESR-GEILYGASFIEWFAEEAKRIYGDVLPQDKeNHRLLVIKQGIGVVAAITPWNFPNAMITRKA 165
Cdd:cd07142 84 ELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADG-PHHVYTLHEPIGVVGQIIPWNFPLLMFAWKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 166 APAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSVeIGKVLTEHPTVRKVTFTGSTRVGKILM-AQS 244
Cdd:cd07142 163 GPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPT-AGAAIASHMDVDKVAFTGSTEVGKIIMqLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 245 ASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAG 324
Cdd:cd07142 242 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 325 VNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIE 404
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505740937 405 MANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
74-477 |
7.41e-117 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 349.42 E-value: 7.41e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 74 LRRWYNLVIENQEELAQLLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITP 153
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 154 WNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGS 233
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLG-RGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 234 TRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVA 313
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 314 AFKVGS-ANEAGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAP 392
Cdd:PRK10090 240 AVQFGNpAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 393 VFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGivginEGLISNE----MAPF-GGVKESGLGREGSRYG 467
Cdd:PRK10090 320 VVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFG-----ETYINREnfeaMQGFhAGWRKSGIGGADGKHG 394
|
410
....*....|..
gi 505740937 468 IDEFLEIK--YL 477
Cdd:PRK10090 395 LHEYLQTQvvYL 406
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
12-477 |
2.65e-116 |
|
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: 350.49 E-value: 2.65e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQL 91
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 92 LSLEQGKPINESRG-EILYGASFIEWFAeEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFA 170
Cdd:cd07559 84 ETLDNGKPIRETLAaDIPLAIDHFRYFA-GVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 171 AGCAMVLKPAQETPLSALALAELAHQAgLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKK 250
Cdd:cd07559 163 AGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTG-FGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 251 LSLELGGNAPSIVFDDA-----DLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGV 325
Cdd:cd07559 241 VTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 326 NIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRG----GTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQ 401
Cdd:cd07559 321 MMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEE 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505740937 402 VIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIKYL 477
Cdd:cd07559 401 AIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
30-479 |
8.17e-116 |
|
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: 348.18 E-value: 8.17e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 30 NPANQQIICELPDLSAEETEYAIACAAQAQKK--WqKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEI 107
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 108 LYGASFIEWFAEEAKRIYGDVlpQDKENHRL-LVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLS 186
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRM--IEPEPGSFsLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 187 ALALAELAHQA-GLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFD 265
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGS-EGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 266 DADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDD 345
Cdd:cd07120 239 DADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVER 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 346 ATAKGANLVI-GGKLHTR--GGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDI 422
Cdd:cd07120 319 AIAAGAEVVLrGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 505740937 423 SRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIKYLCL 479
Cdd:cd07120 399 ARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
10-475 |
3.07e-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: 344.82 E-value: 3.07e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 10 KAYINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELA 89
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 90 QLLSLEQGKPINESRG-EILYGASFIEWFAEEAKRIYGDVLPQDKENHRLlVIKQGIGVVAAITPWNFPNAMITRKAAPA 168
Cdd:cd07117 82 MVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSI-VLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 169 FAAGCAMVLKPAQETPLSALALAELAHQAgLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTV 248
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTG-KGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 249 KKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIG 328
Cdd:cd07117 239 IPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 329 PLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRG----GTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIE 404
Cdd:cd07117 319 AQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVID 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505740937 405 MANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07117 399 MANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMK 469
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
12-480 |
3.12e-114 |
|
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: 344.81 E-value: 3.12e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQA-QKKWQKVTPKERANLLRRWYNLVIENQEELAQ 90
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 91 LLSLEQGKPINESRG-EILYGASFIEWFAEEAKRIYGDVL------PQDkENHRLLVIKQGIGVVAAITPWNFPNAMITR 163
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETLapsipsMQG-ERYTAFTRREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 164 KAAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRsvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQ 243
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG--AVGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 244 SASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEA 323
Cdd:cd07113 240 AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 324 GVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVL--RDVTQAMLvaKDETFAPLAPVFKFDTEAQ 401
Cdd:cd07113 320 SVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVlaRSADSRLM--REETFGPVVSFVPYEDEEE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505740937 402 VIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIKYLCLK 480
Cdd:cd07113 398 LIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
31-474 |
2.08e-113 |
|
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: 341.98 E-value: 2.08e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 31 PANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEILYG 110
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 111 ASFIEWFAEEAKRIYGD--------VLPQDKENHRLLvikqgiGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQE 182
Cdd:cd07101 83 AIVARYYARRAERLLKPrrrrgaipVLTRTTVNRRPK------GVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 183 TPLSALALAELAHQAGLPAGLFNVITStRSVEIGKVLTEHptVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSI 262
Cdd:cd07101 157 TALTALWAVELLIEAGLPRDLWQVVTG-PGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 263 VFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEH 342
Cdd:cd07101 234 VLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 343 IDDATAKGANLVIGGKlhTR---GGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYT 419
Cdd:cd07101 314 VDDAVAKGATVLAGGR--ARpdlGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 505740937 420 QDISRIWRVSEALEYGIVGINEGLIS---NEMAPFGGVKESGLGREGSRYGIDEFLEI 474
Cdd:cd07101 392 RDGARGRRIAARLRAGTVNVNEGYAAawaSIDAPMGGMKDSGLGRRHGAEGLLKYTET 449
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
12-475 |
1.74e-112 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 341.33 E-value: 1.74e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKK-----WQKVTPKERANLLRRWYNLVIENQE 86
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 87 ELAQLLSLEQGKPINESRGEILYGASFIEWFAEEA----KRIYGDV-LPQdkENHRLLVIKQGIGVVAAITPWNFPNAMI 161
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAealdAKQKAPVsLPM--ETFKGYVLKEPLGVVGLITPWNYPLLMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 162 TRKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILM 241
Cdd:PLN02467 169 TWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGT-EAGAPLASHPGVDKIAFTGSTATGRKIM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 242 AQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSAN 321
Cdd:PLN02467 248 TAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 322 EAGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKL--HTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTE 399
Cdd:PLN02467 328 EEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRpeHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505740937 400 AQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:PLN02467 408 DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
28-472 |
3.56e-112 |
|
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: 338.97 E-value: 3.56e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEI 107
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 108 LYGASFIEWFAEEAKRIYGDVLPQDKENHRLLViKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSA 187
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLHYTL-REPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 188 LALAELAHQAgLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDA 267
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGA-TAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 268 DLENAIEGIIAS-KFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDA 346
Cdd:cd07107 238 DPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 347 TAKGANLVIGGKLHT----RGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDI 422
Cdd:cd07107 318 KREGARLVTGGGRPEgpalEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 505740937 423 SRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREgsrYGIDEFL 472
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGRE---ECLEELL 444
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
18-476 |
1.61e-111 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 339.55 E-value: 1.61e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 18 VQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQG 97
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 98 KPINESRGEILYGASFIEWFAEEAKRIYGD--------VLPQDKENHrllvikQGIGVVAAITPWNFP------------ 157
Cdd:PRK09407 106 KARRHAFEEVLDVALTARYYARRAPKLLAPrrragalpVLTKTTELR------QPKGVVGVISPWNYPltlavsdaipal 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 158 ---NAMitrkaapafaagcamVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSVeIGKVLTEHptVRKVTFTGST 234
Cdd:PRK09407 180 lagNAV---------------VLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPV-VGTALVDN--ADYLMFTGST 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 235 RVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAA 314
Cdd:PRK09407 242 ATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 315 FKVGSANEAGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKlhTR---GGTFFEPTVLRDVTQAMLVAKDETFAPLA 391
Cdd:PRK09407 322 MRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGK--ARpdlGPLFYEPTVLTGVTPDMELAREETFGPVV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 392 PVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLIS---NEMAPFGGVKESGLGRegsRYGI 468
Cdd:PRK09407 400 SVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAawgSVDAPMGGMKDSGLGR---RHGA 476
|
....*...
gi 505740937 469 DEFLeiKY 476
Cdd:PRK09407 477 EGLL--KY 482
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
12-475 |
2.55e-111 |
|
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: 337.93 E-value: 2.55e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQA--QKKWQKVTPKERANLLRRWYNLVIENQEELA 89
Cdd:cd07140 9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 90 QLLSLEQGKPINES-RGEILYGASFIEWFAEEAKRIYGDVLP--QDKENHRL-LVIKQGIGVVAAITPWNFPNAMITRKA 165
Cdd:cd07140 89 TIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLAWKM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 166 APAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSVeIGKVLTEHPTVRKVTFTGSTRVGKILMAQSA 245
Cdd:cd07140 169 AACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSL-VGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 246 -STVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAG 324
Cdd:cd07140 248 vSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 325 VNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKF---DTEAq 401
Cdd:cd07140 328 TDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFddgDVDG- 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505740937 402 VIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07140 407 VLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
28-479 |
1.07e-110 |
|
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: 335.10 E-value: 1.07e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQKKwqkVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEI 107
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALAASYRST---LTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 108 LYGASFIEWFAEEAKRIYGDVLPQDKENH----RLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQET 183
Cdd:cd07146 80 GRAADVLRFAAAEALRDDGESFSCDLTANgkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 184 PLSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSAstVKKLSLELGGNAPSIV 263
Cdd:cd07146 160 PLSAIYLADLLYEAGLPPDMLSVVTGEPG-EIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 264 FDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHI 343
Cdd:cd07146 237 MDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 344 DDATAKGANLVIGGKlhtRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDIS 423
Cdd:cd07146 317 EEAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 505740937 424 RIWRVSEALEYGIVGINEGL-ISNEMAPFGGVKESGLG-REGSRYGIDEFLEIKYLCL 479
Cdd:cd07146 394 TIKRLVERLDVGTVNVNEVPgFRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
30-475 |
2.20e-110 |
|
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: 334.21 E-value: 2.20e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 30 NPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEILY 109
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 110 GASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFP-----NAMITrkaapAFAAGCAMVLKPAQETP 184
Cdd:cd07102 82 MLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPyltavNAVIP-----ALLAGNAVILKHSPQTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 185 LSALALAELAHQAGLPAGLFNVITStrSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVF 264
Cdd:cd07102 157 LCGERFAAAFAEAGLPEGVFQVLHL--SHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 265 DDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHID 344
Cdd:cd07102 235 PDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 345 DATAKGANLVIGGKLHTR---GGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQD 421
Cdd:cd07102 315 DAIAKGARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 505740937 422 ISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:cd07102 395 IARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPK 448
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
9-475 |
4.78e-110 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 334.87 E-value: 4.78e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 9 TKAYINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQA--QKKWQKVTPKERANLLRRWYNLVIENQE 86
Cdd:PLN02766 21 TKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 87 ELAQLLSLEQGKPINESRG-EILYGASFIEWFAEEAKRIYGDVLPQDKENHRLlVIKQGIGVVAAITPWNFPNAMITRKA 165
Cdd:PLN02766 101 ELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGY-TLKEPIGVVGHIIPWNFPSTMFFMKV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 166 APAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSVEiGKVLTEHPTVRKVTFTGSTRVGKILM-AQS 244
Cdd:PLN02766 180 APALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTA-GAAIASHMDVDKVSFTGSTEVGRKIMqAAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 245 ASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAG 324
Cdd:PLN02766 259 TSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 325 VNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIE 404
Cdd:PLN02766 339 ARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIK 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505740937 405 MANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:PLN02766 419 KANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVK 489
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
44-473 |
3.05e-105 |
|
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: 320.78 E-value: 3.05e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 44 SAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEILYGASFIEWFAEEAKR 123
Cdd:cd07152 11 DAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 124 IYGDVLPQdkENHRL-LVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSA-LALAELAHQAGLPA 201
Cdd:cd07152 91 PQGEILPS--APGRLsLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 202 GLFNVITStrSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKF 281
Cdd:cd07152 169 GVLHVLPG--GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 282 RNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGklhT 361
Cdd:cd07152 247 LHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGG---T 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 362 RGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINE 441
Cdd:cd07152 324 YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHIND 403
|
410 420 430
....*....|....*....|....*....|....
gi 505740937 442 GLISNE-MAPFGGVKESGLG-REGSRYGIDEFLE 473
Cdd:cd07152 404 QTVNDEpHNPFGGMGASGNGsRFGGPANWEEFTQ 437
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
12-473 |
5.67e-104 |
|
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: 318.57 E-value: 5.67e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQL 91
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 92 LSLEQGKPINESR-GEILYGASFIEWFAeeakrIYGDVLPQDKENHrllvikQGIGVVAAITPWNFPNAMITRKAAPAFA 170
Cdd:cd07111 105 ESLDNGKPIRESRdCDIPLVARHFYHHA-----GWAQLLDTELAGW------KPVGVVGQIVPWNFPLLMLAWKICPALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 171 AGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSVeiGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKK 250
Cdd:cd07111 174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF--GSALANHPGVDKVAFTGSTEVGRALRRATAGTGKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 251 LSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPL 330
Cdd:cd07111 252 LSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 331 ISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTE 410
Cdd:cd07111 332 VDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTP 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505740937 411 FGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLE 473
Cdd:cd07111 412 YGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLR 474
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
9-475 |
1.17e-103 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 319.83 E-value: 1.17e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 9 TKAYINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQA--QKKWQKVTPKERANLLRRWYNLVIENQE 86
Cdd:PLN02466 58 TQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 87 ELAQLLSLEQGKPINESRG-EILYGASFIEWFAEEAKRIYGDVLPQDKeNHRLLVIKQGIGVVAAITPWNFPNAMITRKA 165
Cdd:PLN02466 138 ELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADG-PHHVQTLHEPIGVAGQIIPWNFPLLMFAWKV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 166 APAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVItSTRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSA 245
Cdd:PLN02466 217 GPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVV-SGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 246 -STVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAG 324
Cdd:PLN02466 296 kSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 325 VNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIE 404
Cdd:PLN02466 376 VEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIR 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505740937 405 MANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:PLN02466 456 RANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
12-475 |
5.20e-102 |
|
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: 314.55 E-value: 5.20e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDhkTFAVTNPAN-QQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQ 90
Cdd:cd07124 36 VIGGKEVRTEE--KIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 91 LLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKqGIGVVAAITPWNFPNAMITRKAAPAFA 170
Cdd:cd07124 114 WMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTTAALV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 171 AGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSAST--- 247
Cdd:cd07124 193 TGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPG-PGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqpg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 248 ---VKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAG 324
Cdd:cd07124 272 qkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 325 VNIGPLISQSAVNKIQEHIDDATaKGANLVIGGKL--HTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQV 402
Cdd:cd07124 352 VYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEVleLAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEA 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505740937 403 IEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGlISNEMA---PFGGVKESGLG-REGSRYGIDEFLEIK 475
Cdd:cd07124 431 LEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRK-ITGALVgrqPFGGFKMSGTGsKAGGPDYLLQFMQPK 506
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
30-468 |
8.48e-101 |
|
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: 310.00 E-value: 8.48e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 30 NPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKP-INESRGEIL 108
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 109 YGASFIEWFA---EEAKRiygdvlPQDKENHRLLVIKQG------IGVVAAITPWNFP-----NAMITrkaapAFAAGCA 174
Cdd:cd07098 82 VTCEKIRWTLkhgEKALR------PESRPGGLLMFYKRArveyepLGVVGAIVSWNYPfhnllGPIIA-----ALFAGNA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 175 MVLKPAQETPLSALALAELAHQA----GLPAGLFNVITSTrsVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKK 250
Cdd:cd07098 151 IVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCL--PETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 251 LSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPL 330
Cdd:cd07098 229 VVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 331 ISQSAVNKIQEHIDDATAKGANLVIGGKLHTR----GGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMA 406
Cdd:cd07098 309 ISPARFDRLEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505740937 407 NDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEgLISNEMA---PFGGVKESGLGREGSRYGI 468
Cdd:cd07098 389 NSTEYGLGASVFGKDIKRARRIASQLETGMVAIND-FGVNYYVqqlPFGGVKGSGFGRFAGEEGL 452
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
27-475 |
1.87e-99 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 306.28 E-value: 1.87e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 27 AVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGE 106
Cdd:PRK09406 4 ATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 107 ILYGASFIEWFAEEAKRIYGDVlPQDKEN---HRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQET 183
Cdd:PRK09406 84 ALKCAKGFRYYAEHAEALLADE-PADAAAvgaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 184 PLSALALAELAHQAGLPAGLFN-VITSTRSVEigKVLTEhPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSI 262
Cdd:PRK09406 163 PQTALYLADLFRRAGFPDGCFQtLLVGSGAVE--AILRD-PRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 263 VFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEH 342
Cdd:PRK09406 240 VMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 343 IDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDI 422
Cdd:PRK09406 320 VDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 505740937 423 SRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:PRK09406 400 AEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIK 452
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
7-475 |
2.40e-97 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 302.20 E-value: 2.40e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 7 LKTKAYINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKK--WQKVTPKERANLLRRWYNLVIEN 84
Cdd:PRK09847 18 IENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 85 QEELAQLLSLEQGKPINES-RGEILYGASFIEWFAEEAKRIYGDVLPQDkeNHRL-LVIKQGIGVVAAITPWNFPNAMIT 162
Cdd:PRK09847 98 AEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTS--SHELaMIVREPVGVIAAIVPWNFPLLLTC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 163 RKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMA 242
Cdd:PRK09847 176 WKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGH-EAGQALSRHNDIDAIAFTGSTRTGKQLLK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 243 QSA-STVKKLSLELGGNAPSIVFDDA-DLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSA 320
Cdd:PRK09847 255 DAGdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 321 NEAGVNIGPLISQSAVNKIQEHIDDATAKGaNLVIGGKLHTRGGtFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEA 400
Cdd:PRK09847 335 LDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505740937 401 QVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:PRK09847 413 QALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 487
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
9-469 |
7.22e-97 |
|
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: 300.20 E-value: 7.22e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 9 TKAYINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEEL 88
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 89 AQLLSLEQGKPINESRGEILYGASFIEwFAEEAKRIY-GDVLPQDKENHRLLVIKQGIGVVAAITPWNFPnAMI------ 161
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVE-FACSIPHLLkGEYLENVARGIDTYSYRQPLGVVAGITPFNFP-AMIplwmfp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 162 -------TrkaapafaagcaMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRsvEIGKVLTEHPTVRKVTFTGST 234
Cdd:cd07085 159 maiacgnT------------FVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGK--EAVNALLDHPDIKAVSFVGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 235 RVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAA 314
Cdd:cd07085 225 PVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 315 FKVGSANEAGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHT----RGGTFFEPTVLRDVTQAMLVAKDETFAPL 390
Cdd:cd07085 305 LKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKvpgyENGNFVGPTILDNVTPDMKIYKEEIFGPV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 391 APVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGL-ISNEMAPFGGVKESGLGrEGSRYGID 469
Cdd:cd07085 385 LSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIpVPLAFFSFGGWKGSFFG-DLHFYGKD 463
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
25-475 |
6.60e-92 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 287.14 E-value: 6.60e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 25 TFAVT-NPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINES 103
Cdd:PRK13968 7 THAISvNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 104 RGEILYGASFIEWFAEEAKRIYgDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQET 183
Cdd:PRK13968 87 RAEVAKSANLCDWYAEHGPAML-KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 184 PLSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEhPTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIV 263
Cdd:PRK13968 166 MGCAQLIAQVFKDAGIPQGVYGWLNADND-GVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 264 FDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHI 343
Cdd:PRK13968 244 LNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 344 DDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDIS 423
Cdd:PRK13968 324 EATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDET 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 505740937 424 RIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:PRK13968 404 QARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQ 455
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
25-475 |
1.53e-85 |
|
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: 271.25 E-value: 1.53e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 25 TFAVTNPANQQIICELPDLSAEETEYAIACAAQA--QKKWQKVTpKERANLLRRWYNLVIENQEELAQLLSLEQGKPINE 102
Cdd:TIGR04284 16 TFPTVNPATEEVLGVAADATAADMDAAIAAARRAfdETDWSRDT-ALRVRCLRQLRDALRAHVEELRELTIAEVGAPRML 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 103 SRGEILYG-ASFIEWFAEEA-----KRIYGDVLPQDKENHRLLViKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMV 176
Cdd:TIGR04284 95 TAGAQLEGpVDDLGFAADLAesyawTTDLGVASPMGIPTRRTLR-REAVGVVGAITPWNFPHQINLAKLGPALAAGNTVV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 177 LKPAQETP-LSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLSLEL 255
Cdd:TIGR04284 174 LKPAPDTPwCAAVLGELIAEHTDFPPGVVNIVTSSDH-RLGALLAKDPRVDMVSFTGSTATGRAVMADAAATLKKVFLEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 256 GGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSA 335
Cdd:TIGR04284 253 GGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADPGTVCGPVISARQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 336 VNKIQEHIDDATAKGANLVIGG--KLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGL 413
Cdd:TIGR04284 333 RDRVQSYLDLAVAEGGRFACGGgrPADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGL 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505740937 414 ASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:TIGR04284 413 SGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETK 474
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
12-458 |
2.29e-85 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 271.81 E-value: 2.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDhkTFAVTNPAN-QQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQ 90
Cdd:PRK03137 40 IIGGERITTED--KIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 91 LLSLEQGKPINESRGEILYGASFIEWFAEEAKRiYGD---VLPQDKENHRLLVIKQGIGVVaaITPWNFPNAMITRKAAP 167
Cdd:PRK03137 118 WLVKEAGKPWAEADADTAEAIDFLEYYARQMLK-LADgkpVESRPGEHNRYFYIPLGVGVV--ISPWNFPFAIMAGMTLA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 168 AFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSAST 247
Cdd:PRK03137 195 AIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGS-EVGDYLVDHPKTRFITFTGSREVGLRIYERAAKV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 248 ------VKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSAN 321
Cdd:PRK03137 274 qpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 322 EAGvNIGPLISQSAVNKIQEHIDDATAKGaNLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQ 401
Cdd:PRK03137 354 DNA-YMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDH 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505740937 402 VIEMANDTEFGLASYLYTQDISRIWRVSEALEYG-----------IVGINeglisnemaPFGGVKESG 458
Cdd:PRK03137 432 ALEIANNTEYGLTGAVISNNREHLEKARREFHVGnlyfnrgctgaIVGYH---------PFGGFNMSG 490
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
24-464 |
5.54e-84 |
|
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: 266.77 E-value: 5.54e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 24 KTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINES 103
Cdd:cd07130 12 GVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 104 RGEIlygASFIEW--FAEEAKR-IYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFP------NAMITrkaapaFAAGCA 174
Cdd:cd07130 92 LGEV---QEMIDIcdFAVGLSRqLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPvavwgwNAAIA------LVCGNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 175 MVLKPAQETP----LSALALAELAHQAGLPAGLFNVITStrSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKK 250
Cdd:cd07130 163 VVWKPSPTTPltaiAVTKIVARVLEKNGLPGAIASLVCG--GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 251 LSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPL 330
Cdd:cd07130 241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 331 ISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVLRDVTQAMLVaKDETFAPLAPVFKFDTEAQVIEMANDTE 410
Cdd:cd07130 321 HTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSDAPIV-KEETFAPILYVLKFDTLEEAIAWNNEVP 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 505740937 411 FGLASYLYTQDISRIWRVSEAL--EYGIVGINEGLISNEM-APFGGVKESGLGRE-GS 464
Cdd:cd07130 400 QGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTSGAEIgGAFGGEKETGGGREsGS 457
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
12-460 |
4.16e-83 |
|
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: 265.58 E-value: 4.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHktFAVTNPAN-QQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQ 90
Cdd:TIGR01237 36 VINGERVETENK--IVSINPCDkSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 91 LLSLEQGKPINESRGEILYGASFIEWFAEEAKRIY--GDVLPQDKENHRLLVIKQGIGVVaaITPWNFPNAMITRKAAPA 168
Cdd:TIGR01237 114 LLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAkgKPVNSREGETNQYVYTPTGVTVV--ISPWNFPFAIMVGMTVAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 169 FAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSAST- 247
Cdd:TIGR01237 192 IVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGS-EVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVq 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 248 -----VKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANE 322
Cdd:TIGR01237 271 pgqkhLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDS 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 323 AGVNIGPLISQSAVNKIQEHIDDATAKGaNLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQV 402
Cdd:TIGR01237 351 ADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEA 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505740937 403 IEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINE---GLISNeMAPFGGVKESGLG 460
Cdd:TIGR01237 430 LEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRnitGAIVG-YQPFGGFKMSGTD 489
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
12-477 |
2.63e-82 |
|
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: 262.77 E-value: 2.63e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQL 91
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 92 LSLEQGKPINESRGEIL--------YGASFIEwfAEEAKriygdvLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITR 163
Cdd:cd07116 84 ETWDNGKPVRETLAADIplaidhfrYFAGCIR--AQEGS------ISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 164 KAAPAFAAGCAMVLKPAQETPLSALALAELAHQAgLPAGLFNVITSTrSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQ 243
Cdd:cd07116 156 KLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGF-GLEAGKPLASSKRIAKVAFTGETTTGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 244 SASTVKKLSLELGGNAPSIVF------DDADLENAIEGIIASKFrNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKV 317
Cdd:cd07116 234 ASENIIPVTLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 318 GSANEAGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRG----GTFFEPTVLRDvTQAMLVAKDETFAPLAPV 393
Cdd:cd07116 313 GNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGgllgGGYYVPTTFKG-GNKMRIFQEEIFGPVLAV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 394 FKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMAPFGGVKESGLGREGSRYGIDEFLE 473
Cdd:cd07116 392 TTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQ 471
|
....
gi 505740937 474 IKYL 477
Cdd:cd07116 472 TKNL 475
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
10-475 |
1.48e-76 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 248.13 E-value: 1.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 10 KAYINGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELA 89
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 90 QLLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYG-------DVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMIT 162
Cdd:PLN00412 97 ECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGegkflvsDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 163 RKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGSTRvgKILMA 242
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTG-KGSEIGDFLTMHPGVNCISFTGGDT--GIAIS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 243 QSASTVkKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGsANE 322
Cdd:PLN00412 254 KKAGMV-PLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVG-PPE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 323 AGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKlhtRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQV 402
Cdd:PLN00412 332 DDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWK---REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEG 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505740937 403 IEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISN-EMAPFGGVKESGLGREGSRYGIDEFLEIK 475
Cdd:PLN00412 409 IHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGpDHFPFQGLKDSGIGSQGITNSINMMTKVK 482
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
51-469 |
1.14e-70 |
|
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: 231.01 E-value: 1.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 51 AIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGEILYGASFIEwFAEEAKRIYGDVLP 130
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKID-ISIKAYHERTGERA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 131 QDKENHRLLVIKQGIGVVAAITPWNFP----NAMITrkaaPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNV 206
Cdd:cd07095 84 TPMAQGRAVLRHRPHGVMAVFGPFNFPghlpNGHIV----PALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 207 ITSTRsvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKK-LSLELGGNAPSIVFDDADLENAIEGIIASKFRNSG 285
Cdd:cd07095 160 VQGGR--ETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 286 QTCVCTNRIYVQAGIY-DRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGG 364
Cdd:cd07095 238 QRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 365 TFFEPTVLrDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYT---QDISRIWRVSEAleyGIVGINE 441
Cdd:cd07095 318 AFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSddeALFERFLARIRA---GIVNWNR 393
|
410 420
....*....|....*....|....*....
gi 505740937 442 GLI-SNEMAPFGGVKESGLGREGSRYGID 469
Cdd:cd07095 394 PTTgASSTAPFGGVGLSGNHRPSAYYAAD 422
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
27-460 |
1.50e-68 |
|
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: 227.85 E-value: 1.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 27 AVTNPA-NQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRG 105
Cdd:cd07125 49 PVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 106 EILYGASFIEWFAEEAKRIYGDVL---PQDKENHrllVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQE 182
Cdd:cd07125 129 EVREAIDFCRYYAAQARELFSDPElpgPTGELNG---LELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 183 TPLSALALAELAHQAGLPAGLFNVITSTRSvEIGKVLTEHPTVRKVTFTGSTRVGKIL---MAQSASTVKKLSLELGG-N 258
Cdd:cd07125 206 TPLIAARAVELLHEAGVPRDVLQLVPGDGE-EIGEALVAHPRIDGVIFTGSTETAKLInraLAERDGPILPLIAETGGkN 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 259 ApSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNK 338
Cdd:cd07125 285 A-MIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 339 IQEHIDDATAKgANLVIGGKLHTRGGTFFEPTVLRDVTQAMLvaKDETFAPLAPVFKFDTE--AQVIEMANDTEFGLASY 416
Cdd:cd07125 364 LRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGIFDL--TTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLG 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 505740937 417 LYTQDISRIWRVSEALEYGIVGINEGLISN--EMAPFGGVKESGLG 460
Cdd:cd07125 441 IHSRDEREIEYWRERVEAGNLYINRNITGAivGRQPFGGWGLSGTG 486
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
28-470 |
3.58e-68 |
|
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: 224.99 E-value: 3.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQIICELPDLSAEETEYAIACAAQAQK---KWqkVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESR 104
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLdrnNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 105 GEILYGASFIEWFAEEAKRIYGDVLPQD----KENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPA 180
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGGREIPMGltpaSAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 181 QETPLSALALAELAHQAGLPAGLFN-VITSTRSVEigKVLTEhPTVRKVTFTGSTRVGKILMAQSASTVKkLSLELGGNA 259
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQaVPCENAVAE--KLVTD-PRVAFFSFIGSARVGWMLRSKLAPGTR-CALEHGGAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 260 PSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKI 339
Cdd:cd07148 237 PVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 340 QEHIDDATAKGANLVIGGKLhtRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYT 419
Cdd:cd07148 317 EEWVNEAVAAGARLLCGGKR--LSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 505740937 420 QDISRIWRVSEALEYGIVGINE--GLISNEMaPFGGVKESGLGREGSRYGIDE 470
Cdd:cd07148 395 KDLDVALKAVRRLDATAVMVNDhtAFRVDWM-PFAGRRQSGYGTGGIPYTMHD 446
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
12-469 |
2.50e-66 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 220.99 E-value: 2.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHkTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQL 91
Cdd:PRK09457 4 WINGDWIAGQGE-AFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 92 LSLEQGKPINESRGEIlygASF-------IEWFAE---EAKRIYGD---VLpqdkeNHRLLvikqgiGVVAAITPWNFP- 157
Cdd:PRK09457 83 IARETGKPLWEAATEV---TAMinkiaisIQAYHErtgEKRSEMADgaaVL-----RHRPH------GVVAVFGPYNFPg 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 158 ---NAMITrkaaPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRsvEIGKVLTEHPTVRKVTFTGST 234
Cdd:PRK09457 149 hlpNGHIV----PALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGR--ETGKALAAHPDIDGLLFTGSA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 235 RVGKILMAQSASTVKK-LSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIY-DRFVEQFSAKV 312
Cdd:PRK09457 223 NTGYLLHRQFAGQPEKiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 313 AAFKVGSAN-EAGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVLrDVTQAMLVAKDETFAPLA 391
Cdd:PRK09457 303 KRLTVGRWDaEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 392 PVFKFDTEAQVIEMANDTEFGLASYLYT---QDISRIWRVSEAleyGIVGINEGLI-SNEMAPFGGVKESGLGREGSRYG 467
Cdd:PRK09457 382 QVVRYDDFDEAIRLANNTRFGLSAGLLSddrEDYDQFLLEIRA---GIVNWNKPLTgASSAAPFGGVGASGNHRPSAYYA 458
|
..
gi 505740937 468 ID 469
Cdd:PRK09457 459 AD 460
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
12-475 |
6.19e-65 |
|
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: 217.83 E-value: 6.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHKTfaVTNPANQ-QIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQ 90
Cdd:cd07083 22 VIGGEWVDTKERMV--SVSPFAPsEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 91 LLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGD---VLPQDKENHRLLVikQGIGVVAAITPWNFPNAMITRKAAP 167
Cdd:cd07083 100 TLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPaveVVPYPGEDNESFY--VGLGAGVVISPWNFPVAIFTGMIVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 168 AFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTrSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSA-- 245
Cdd:cd07083 178 PVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGV-GEEVGAYLTEHERIRGINFTGSLETGKKIYEAAArl 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 246 ----STVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSAN 321
Cdd:cd07083 257 apgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 322 EAGVNIGPLISQSAVNKIQEHIDDATAKGaNLVIGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPV--FKFDTE 399
Cdd:cd07083 337 ENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVirYKDDDF 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505740937 400 AQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMA--PFGGVKESGLG-REGSRYGIDEFLEIK 475
Cdd:cd07083 416 AEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGvqPFGGFKLSGTNaKTGGPHYLRRFLEMK 494
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
11-462 |
2.59e-57 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 197.75 E-value: 2.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 11 AYINGEYvqAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQ 90
Cdd:PLN02315 23 CYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 91 LLSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFA 170
Cdd:PLN02315 101 LVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 171 AGCAMVLKPAQETP----LSALALAELAHQAGLPAGLFNVITStrSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSAS 246
Cdd:PLN02315 181 CGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIFTSFCG--GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 247 TVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVN 326
Cdd:PLN02315 259 RFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 327 IGPLISQSAVNKIQEHIDDATAKGANLVIGGKLHTRGGTFFEPTVLrDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMA 406
Cdd:PLN02315 339 LGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEIN 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 505740937 407 NDTEFGLASYLYTQDISRI--WRVSEALEYGIVGINEGLISNEM-APFGGVKESGLGRE 462
Cdd:PLN02315 418 NSVPQGLSSSIFTRNPETIfkWIGPLGSDCGIVNVNIPTNGAEIgGAFGGEKATGGGRE 476
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
70-471 |
1.48e-56 |
|
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: 193.98 E-value: 1.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 70 RANLLRRWYNLVIENQEELAQLLSLEQGKPINESR--------GEILYGASFIEWFAEEAKRiyGDVLPQDKeNHRLLVI 141
Cdd:cd07135 29 RLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLltevsgvkNDILHMLKNLKKWAKDEKV--KDGPLAFM-FGKPRIR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 142 KQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAgLPAGLFNVITStrSV-EIGKVLT 220
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQG--GVpETTALLE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 221 EHptVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGI 300
Cdd:cd07135 183 QK--FDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 301 YDRFVEQFSAKVAAFKVGSANEAGvNIGPLISQSAVNKIQEHIDDATAKganLVIGGKlHTRGGTFFEPTVLRDVTQAML 380
Cdd:cd07135 261 YDEFVEELKKVLDEFYPGGANASP-DYTRIVNPRHFNRLKSLLDTTKGK---VVIGGE-MDEATRFIPPTIVSDVSWDDS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 381 VAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLI--SNEMAPFGGVKESG 458
Cdd:cd07135 336 LMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVDNAPFGGVGDSG 415
|
410
....*....|...
gi 505740937 459 LGREGSRYGIDEF 471
Cdd:cd07135 416 YGAYHGKYGFDTF 428
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
70-471 |
3.67e-55 |
|
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: 190.04 E-value: 3.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 70 RANLLRRWYNLVIENQEELAQLLSLEQGKPINES--------RGEILYgasfiewfaeeAKRIYGDVL-PQDKENHRLL- 139
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylteiavvLGEIDH-----------ALKHLKKWMkPRRVSVPLLLq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 140 -----VIKQGIGVVAAITPWNFP---------NAMI---TrkaapafaagcaMVLKPAQETPlsalalaelaHQAGLPAG 202
Cdd:cd07087 91 pakayVIPEPLGVVLIIGPWNYPlqlalapliGAIAagnT------------VVLKPSELAP----------ATSALLAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 203 LFN---------VITSTrsVEIGKVLTEHPtVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAI 273
Cdd:cd07087 149 LIPkyfdpeavaVVEGG--VEVATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 274 EGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFkVGSANEAGVNIGPLISQSAVNKIQEHIDDATakganL 353
Cdd:cd07087 226 RRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDGK-----V 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 354 VIGGKLHtRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALE 433
Cdd:cd07087 300 VIGGQVD-KEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETS 378
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 505740937 434 YGIVGINEGLI--SNEMAPFGGVKESGLGREGSRYGIDEF 471
Cdd:cd07087 379 SGGVCVNDVLLhaAIPNLPFGGVGNSGMGAYHGKAGFDTF 418
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
146-471 |
5.27e-55 |
|
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: 189.74 E-value: 5.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 146 GVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPlsalalaelaHQAGLPAGL----FN---VITSTRSVEIGKV 218
Cdd:cd07134 102 GVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTP----------HTSAVIAKIireaFDedeVAVFEGDAEVAQA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 219 LTEHPtVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQA 298
Cdd:cd07134 172 LLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 299 GIYDRFVEQFSAKVAAF-KVGSANEAGVNIGPLISQSAVNKIQEHIDDATAKGANLVIGGKlHTRGGTFFEPTVLRDVTQ 377
Cdd:cd07134 251 SVKDAFVEHLKAEIEKFyGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQ-FDAAQRYIAPTVLTNVTP 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 378 AMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLI--SNEMAPFGGVK 455
Cdd:cd07134 330 DMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLhfLNPNLPFGGVN 409
|
330
....*....|....*.
gi 505740937 456 ESGLGREGSRYGIDEF 471
Cdd:cd07134 410 NSGIGSYHGVYGFKAF 425
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
13-475 |
7.70e-53 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 187.65 E-value: 7.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 13 INGEYVQAKDHKTFAVTNPANQQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLL 92
Cdd:PLN02419 118 IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 93 SLEQGKPINESRGEILYGASFIEWFAEEAKRIYGDVLPQDKENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAG 172
Cdd:PLN02419 198 TTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 173 CAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRsvEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKKLS 252
Cdd:PLN02419 278 NTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTN--DTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQ 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 253 LELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIyVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLIS 332
Cdd:PLN02419 356 SNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTV-VFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVIS 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 333 QSAVNKIQEHIDDATAKGANLVIGGK-LHTRG---GTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMAND 408
Cdd:PLN02419 435 KQAKERICRLIQSGVDDGAKLLLDGRdIVVPGyekGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINK 514
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 409 TEFGLASYLYTQDISRIWRVSEALEYGIVGINEGL-ISNEMAPFGGVKESGLGREG--SRYGIDEFLEIK 475
Cdd:PLN02419 515 NKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIpVPLPFFSFTGNKASFAGDLNfyGKAGVDFFTQIK 584
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
13-476 |
6.58e-52 |
|
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: 183.19 E-value: 6.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 13 INGEYVQakDHKTFAVTNPANQQIIC-ELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQL 91
Cdd:TIGR01238 42 IGHSYKA--DGEAQPVTNPADRRDIVgQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 92 LSLEQGKPINESRGEILYGASFIEWFAEEAKriygDVLPQDKENHRllvikqgiGVVAAITPWNFPNAMITRKAAPAFAA 171
Cdd:TIGR01238 120 CVREAGKTIHNAIAEVREAVDFCRYYAKQVR----DVLGEFSVESR--------GVFVCISPWNFPLAIFTGQISAALAA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 172 GCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGSTRVGKIL---MAQSASTV 248
Cdd:TIGR01238 188 GNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPG-RGADVGAALTSDPRIAGVAFTGSTEVAQLInqtLAQREDAP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 249 KKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIG 328
Cdd:TIGR01238 267 VPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 329 PLISQSAVNKIQEHIDDATAKG---ANLVIGGKLHTRGGTFFEPTVLRDVTQAMLvaKDETFAPLAPV--FKFDTEAQVI 403
Cdd:TIGR01238 347 PVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFELDDIAEL--SEEVFGPVLHVvrYKARELDQIV 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505740937 404 EMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMA--PFGGVKESGLG-REGSRYGIDEFLEIKY 476
Cdd:TIGR01238 425 DQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGvqPFGGQGLSGTGpKAGGPHYLYRLTQVQY 500
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
68-480 |
2.28e-49 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 175.99 E-value: 2.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 68 KERANLLRRWYNLVIENQEELAQLLSLEQGKPINES--------RGEILYGASFI-EWFAEEAKRIYGDVLPQDKEnhrl 138
Cdd:PTZ00381 29 EFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETkmtevlltVAEIEHLLKHLdEYLKPEKVDTVGVFGPGKSY---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 139 lVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPlsalalaelaHQAGLPAGLFN---------VITs 209
Cdd:PTZ00381 105 -IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSP----------HTSKLMAKLLTkyldpsyvrVIE- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 210 tRSVEIGKVLTEHPtVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCV 289
Cdd:PTZ00381 173 -GGVEVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 290 CTNRIYVQAGIYDRFVEQFSAKVAAFkVGSANEAGVNIGPLISQSAVNKIQEHIDDataKGANLVIGGK--LHTRggtFF 367
Cdd:PTZ00381 251 APDYVLVHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEvdIENK---YV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 368 EPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGL--IS 445
Cdd:PTZ00381 324 APTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVfhLL 403
|
410 420 430
....*....|....*....|....*....|....*
gi 505740937 446 NEMAPFGGVKESGLGREGSRYGIDEFLEIKYLCLK 480
Cdd:PTZ00381 404 NPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
66-471 |
1.16e-48 |
|
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: 172.67 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 66 TPKERANLLRRWYNLVIENQEELAQLLSLEQGkpiNESRGEILygasfiewFAEeakrIYGDVL--------------PQ 131
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADFG---HRSRHETL--------LAE----ILPSIAgikharkhlkkwmkPS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 132 DKENHRLL------VIKQGIGVVAAITPWNFP---------------N-AMItrkaapafaagcamvlKPAQETPlsala 189
Cdd:cd07133 83 RRHVGLLFlpakaeVEYQPLGVVGIIVPWNYPlylalgpliaalaagNrVMI----------------KPSEFTP----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 190 laelaHQAGLPAGLFN---------VITSTrsVEIGKVLTEHPtVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAP 260
Cdd:cd07133 142 -----RTSALLAELLAeyfdedevaVVTGG--ADVAAAFSSLP-FDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 261 SIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAA-FKVGSANEagvNIGPLISQSAVNKI 339
Cdd:cd07133 214 AIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKmYPTLADNP---DYTSIINERHYARL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 340 QEHIDDATAKGANLV--IGGKLHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYL 417
Cdd:cd07133 291 QGLLEDARAKGARVIelNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYY 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 505740937 418 YTQDISRIWRVSEALEYGIVGINEGL--ISNEMAPFGGVKESGLGREGSRYGIDEF 471
Cdd:cd07133 371 FGEDKAEQDRVLRRTHSGGVTINDTLlhVAQDDLPFGGVGASGMGAYHGKEGFLTF 426
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
25-460 |
1.89e-45 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 170.43 E-value: 1.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 25 TFAVTNPANQ-QIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINES 103
Cdd:PRK11905 568 TRPVLNPADHdDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANA 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 104 RGEILYGASFIEWFAEEAKRiygdvLPQDKEnHRLLvikqgiGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQET 183
Cdd:PRK11905 648 IAEVREAVDFLRYYAAQARR-----LLNGPG-HKPL------GPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQT 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 184 PLSALALAELAHQAGLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTVKK---LSLELGG-NA 259
Cdd:PRK11905 716 PLIAARAVRLLHEAGVPKDALQLLPG-DGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPpvpLIAETGGqNA 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 260 pSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKI 339
Cdd:PRK11905 795 -MIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANI 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 340 QEHIDDATAKGAnlviggKLH-------TRGGTFFEPTV-----LRDVtqamlvaKDETFAPLAPVFKFDTE--AQVIEM 405
Cdd:PRK11905 874 EAHIEAMRAAGR------LVHqlplpaeTEKGTFVAPTLieidsISDL-------EREVFGPVLHVVRFKADelDRVIDD 940
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 406 ANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISnemA-----PFGGVKESGLG 460
Cdd:PRK11905 941 INATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIG---AvvgvqPFGGEGLSGTG 997
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
230-471 |
4.05e-44 |
|
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: 160.75 E-value: 4.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 230 FTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFS 309
Cdd:cd07136 182 FTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELK 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 310 AKVAAFKvGSANEAGVNIGPLISQSAVNKIQEHIDDatakgANLVIGGKlHTRGGTFFEPTVLRDVTQAMLVAKDETFAP 389
Cdd:cd07136 262 EEIKKFY-GEDPLESPDYGRIINEKHFDRLAGLLDN-----GKIVFGGN-TDRETLYIEPTILDNVTWDDPVMQEEIFGP 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 390 LAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLI--SNEMAPFGGVKESGLGREGSRYG 467
Cdd:cd07136 335 ILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMhlANPYLPFGGVGNSGMGSYHGKYS 414
|
....
gi 505740937 468 IDEF 471
Cdd:cd07136 415 FDTF 418
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
28-460 |
8.20e-42 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 159.59 E-value: 8.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPAN-QQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGE 106
Cdd:PRK11904 566 VVSPADrRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAE 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 107 ILYGASFIEWFAEEAKRIYGD--VLP-QDKENHRLlvIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQET 183
Cdd:PRK11904 646 VREAVDFCRYYAAQARRLFGApeKLPgPTGESNEL--RLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQT 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 184 PLSALALAELAHQAGLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGSTRVGKI----LMAQSASTVkKLSLELGG-N 258
Cdd:PRK11904 724 PLIAAEAVKLLHEAGIPKDVLQLLPG-DGATVGAALTADPRIAGVAFTGSTETARIinrtLAARDGPIV-PLIAETGGqN 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 259 ApSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNK 338
Cdd:PRK11904 802 A-MIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKAN 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 339 IQEHIDDATaKGANLVIGGKL--HTRGGTFFEPTVLRdvTQAMLVAKDETFAPLAPVFKFDTE--AQVIEMANDTEFGLa 414
Cdd:PRK11904 881 LDAHIERMK-REARLLAQLPLpaGTENGHFVAPTAFE--IDSISQLEREVFGPILHVIRYKASdlDKVIDAINATGYGL- 956
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 505740937 415 sylyTQDI-SRI----WRVSEALEYGIVGINEGLISN--EMAPFGGVKESGLG 460
Cdd:PRK11904 957 ----TLGIhSRIeetaDRIADRVRVGNVYVNRNQIGAvvGVQPFGGQGLSGTG 1005
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
13-459 |
4.55e-41 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 157.41 E-value: 4.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 13 INGEYVQAKDHktfAVTNPAN-QQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQL 91
Cdd:COG4230 562 IAGEAASGEAR---PVRNPADhSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMAL 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 92 LSLEQGKPINESRGEILYGASFIEWFAEEAKRIYGdvlpqdkeNHRLLvikQGIGVVAAITPWNFP-------------- 157
Cdd:COG4230 639 LVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFA--------APTVL---RGRGVFVCISPWNFPlaiftgqvaaalaa 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 158 -NAmitrkaapafaagcamVL-KPAQETPLSALALAELAHQAGLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGSTR 235
Cdd:COG4230 708 gNT----------------VLaKPAEQTPLIAARAVRLLHEAGVPADVLQLLPG-DGETVGAALVADPRIAGVAFTGSTE 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 236 VGKIL---MAQSASTVKKLSLELGG-NApSIVfdD--ADLENAIEGIIASKFRNSGQTCvctN--RI-YVQAGIYDRFVE 306
Cdd:COG4230 771 TARLInrtLAARDGPIVPLIAETGGqNA-MIV--DssALPEQVVDDVLASAFDSAGQRC---SalRVlCVQEDIADRVLE 844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 307 QFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDATAKGaNLVIGGKL--HTRGGTFFEPTV-----LRDVTQam 379
Cdd:COG4230 845 MLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG-RLVHQLPLpeECANGTFVAPTLieidsISDLER-- 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 380 lvakdETFAPLAPVFKFDTE--AQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISnemA-----PFG 452
Cdd:COG4230 922 -----EVFGPVLHVVRYKADelDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIG---AvvgvqPFG 993
|
....*..
gi 505740937 453 GvkeSGL 459
Cdd:COG4230 994 G---EGL 997
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
28-460 |
2.57e-39 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 152.44 E-value: 2.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 28 VTNPANQQ-IICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPINESRGE 106
Cdd:PRK11809 663 VINPADPRdIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAE 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 107 ILYGASFIEWFAEEAKRIYgdvlpqDKENHRLLvikqgiGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLS 186
Cdd:PRK11809 743 VREAVDFLRYYAGQVRDDF------DNDTHRPL------GPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 187 ALALAELAHQAGLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGSTRVGKILM--------AQSASTVkkLSLELGGN 258
Cdd:PRK11809 811 AAQAVRILLEAGVPAGVVQLLPG-RGETVGAALVADARVRGVMFTGSTEVARLLQrnlagrldPQGRPIP--LIAETGGQ 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 259 APSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNK 338
Cdd:PRK11809 888 NAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKAN 967
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 339 IQEHIDDATAKGAN---LVIGGKLHTRGGTFFEPTV--LRDVTQamlvAKDETFAPLAPVFKFDTEA--QVIEMANDTEF 411
Cdd:PRK11809 968 IERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTLieLDSFDE----LKREVFGPVLHVVRYNRNQldELIEQINASGY 1043
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 505740937 412 GLASYLYTQDISRIWRVSEALEYGIVGINEGLISNEMA--PFGGVKESGLG 460
Cdd:PRK11809 1044 GLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvqPFGGEGLSGTG 1094
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
11-458 |
2.07e-34 |
|
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: 135.41 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 11 AYINGEYVQAKDHKTfaVTNPAN-QQIICELPDLSAEETEYAIACAAQAQKKWQKVTPKERANLLRRWYNLVI-ENQEEL 88
Cdd:cd07123 35 LVIGGKEVRTGNTGK--QVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 89 AQLLSLEQGKPINESrgEILYGASFIEWF---AEEAKRIYGDVLPQDKENHRLLVIKQGI-GVVAAITPWNF-------- 156
Cdd:cd07123 113 NAATMLGQGKNVWQA--EIDAACELIDFLrfnVKYAEELYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFtaiggnla 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 157 --PNAMitrkaapafaaGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTRSVeIGKVLTEHPTVRKVTFTGST 234
Cdd:cd07123 191 gaPALM-----------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPV-VGDTVLASPHLAGLHFTGST 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 235 RVGKILMAQSAS------TVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRFVEQF 308
Cdd:cd07123 259 PTFKSLWKQIGEnldryrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 309 SAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDA-TAKGANLVIGGKLHTRGGTFFEPTVLR--DVTQAMLvaKDE 385
Cdd:cd07123 339 LEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAkSDPEAEIIAGGKCDDSVGYFVEPTVIEttDPKHKLM--TEE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 386 TFAPLAPVFKFDTE--AQVIEMANDT-EFGLASYLYTQDISRIWRVSEALEY--GIVGINE---GLISNEMaPFGGVKES 457
Cdd:cd07123 417 IFGPVLTVYVYPDSdfEETLELVDTTsPYALTGAIFAQDRKAIREATDALRNaaGNFYINDkptGAVVGQQ-PFGGARAS 495
|
.
gi 505740937 458 G 458
Cdd:cd07123 496 G 496
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
70-471 |
1.23e-33 |
|
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: 131.76 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 70 RANLLRRWYNLVIENQEELAQLLSLEQGKPINES-RGEI--------LYGASFIEWFAEEAKRIYGDVLPQDKEnhrllV 140
Cdd:cd07137 23 RKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVsvlvssckLAIKELKKWMAPEKVKTPLTTFPAKAE-----I 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 141 IKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAgLPAGLFNVITStrSVEIGKVLT 220
Cdd:cd07137 98 VSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG--GVPETTALL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 221 EHpTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKF-RNSGQTCVCTNRIYVQAG 299
Cdd:cd07137 175 EQ-KWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEES 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 300 IYDRFVEQFSAKVAAFkvgsaneAGVNigPLISQSA---VNKIQ----EHIDDATAKGANLVIGGKLhTRGGTFFEPTVL 372
Cdd:cd07137 254 FAPTLIDALKNTLEKF-------FGEN--PKESKDLsriVNSHHfqrlSRLLDDPSVADKIVHGGER-DEKNLYIEPTIL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 373 RDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLI--SNEMAP 450
Cdd:cd07137 324 LDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVqyAIDTLP 403
|
410 420
....*....|....*....|.
gi 505740937 451 FGGVKESGLGREGSRYGIDEF 471
Cdd:cd07137 404 FGGVGESGFGAYHGKFSFDAF 424
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
72-471 |
8.14e-33 |
|
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: 129.65 E-value: 8.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 72 NLLRrwynLVIENQEELAQLLSLEQGKPINES--------RGEILYGASFI-EWFAEE--AKRIygdVLPQDkenhRLLV 140
Cdd:cd07132 28 ALLR----MLEENEDEIVEALAKDLRKPKFEAvlseillvKNEIKYAISNLpEWMKPEpvKKNL---ATLLD----DVYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 141 IKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPlsalalaelaHQAGLPAGL---------FNVITStr 211
Cdd:cd07132 97 YKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSP----------ATAKLLAELipkyldkecYPVVLG-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 212 SVEIGKVLTEHpTVRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCT 291
Cdd:cd07132 165 GVEETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 292 NRIYVQAGIYDRFVEQFSAKVAAFkVGSANEAGVNIGPLISQSAVNKIQEHIddataKGANLVIGGKlHTRGGTFFEPTV 371
Cdd:cd07132 244 DYVLCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVAIGGQ-TDEKERYIAPTV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 372 LRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGL--ISNEMA 449
Cdd:cd07132 317 LTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTImhYTLDSL 396
|
410 420
....*....|....*....|..
gi 505740937 450 PFGGVKESGLGREGSRYGIDEF 471
Cdd:cd07132 397 PFGGVGNSGMGAYHGKYSFDTF 418
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
116-471 |
4.10e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 110.91 E-value: 4.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 116 WFAEEAKRIYGDVLPQDKEnhrllVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSALALAELAH 195
Cdd:PLN02174 89 WMAPEKAKTSLTTFPASAE-----IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 196 QAGLPaglfnviTSTRSVEigKVLTEHPTV-----RKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIVFDDADLE 270
Cdd:PLN02174 164 QYLDS-------SAVRVVE--GAVTETTALleqkwDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLK 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 271 NAIEGIIASKFR-NSGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGvNIGPLISQSAVNKIQEHIDDATAK 349
Cdd:PLN02174 235 VTVRRIIAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLDEKEVS 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 350 GaNLVIGGKlHTRGGTFFEPTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVS 429
Cdd:PLN02174 314 D-KIVYGGE-KDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFA 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 505740937 430 EALEYGIVGINEglISNEMA----PFGGVKESGLGREGSRYGIDEF 471
Cdd:PLN02174 392 ATVSAGGIVVND--IAVHLAlhtlPFGGVGESGMGAYHGKFSFDAF 435
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
70-471 |
2.50e-25 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 108.66 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 70 RANLLRRWYNLVIENQEELAQLLSLEQGKPINES-RGEI--------LYGASFIEWFAEEAKRIYGDVLPQDKEnhrllV 140
Cdd:PLN02203 30 RKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyRDEVgvltksanLALSNLKKWMAPKKAKLPLVAFPATAE-----V 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 141 IKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSALALAelahqAGLPAGLfnvitSTRSV------- 213
Cdd:PLN02203 105 VPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA-----ANIPKYL-----DSKAVkvieggp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 214 EIGKVLTEHPTvRKVTFTGSTRVGKILMAQSASTVKKLSLELGGNAPSIV--FDDA-DLENAIEGIIASKFRN-SGQTCV 289
Cdd:PLN02203 175 AVGEQLLQHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 290 CTNRIYVQAGIYDRFVEQFSAKVAAFKVGSANEAGvNIGPLISQSAVNKIQEHIDDATAKgANLVIGGKLHTRgGTFFEP 369
Cdd:PLN02203 254 AIDYVLVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVA-ASIVHGGSIDEK-KLFIEP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 370 TVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQDISRIWRVSEALEYGIVGINEGLISN--E 447
Cdd:PLN02203 331 TILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYacD 410
|
410 420
....*....|....*....|....
gi 505740937 448 MAPFGGVKESGLGREGSRYGIDEF 471
Cdd:PLN02203 411 SLPFGGVGESGFGRYHGKYSFDTF 434
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
49-433 |
6.03e-21 |
|
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: 95.00 E-value: 6.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 49 EYAIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPiNESRGEILYGASFIEWFAeeaKRIYGDV 128
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG-WMFAENICGDQVQLRARA---FVIYSYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 129 LPQDKENHRLLVIKQ-------GIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAG-LP 200
Cdd:cd07084 78 IPHEPGNHLGQGLKQqshgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 201 AGLFNVITStrSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSASTvkKLSLELGGNAPSIVFDDADLENA-IEGIIAS 279
Cdd:cd07084 158 PEDVTLING--DGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYvAWQCVQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 280 KFRNSGQTCVCTNRIYVQAGIYDR-FVEQFSAKVAAFKVGSAneagvNIGPLISQSAVNKIQEHIDDAtakGANLVIGGK 358
Cdd:cd07084 234 MTACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLEDL-----LLGPVQTFTTLAMIAHMENLL---GSVLLFSGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 359 LHTRGGTFFEPTVLrdVTQAMLVAKD-----------ETFAPLAPVFKF--DTEAQVIEMANDTEFGLASYLYTQDISRI 425
Cdd:cd07084 306 ELKNHSIPSIYGAC--VASALFVPIDeilktyelvteEIFGPFAIVVEYkkDQLALVLELLERMHGSLTAAIYSNDPIFL 383
|
....*...
gi 505740937 426 WRVSEALE 433
Cdd:cd07084 384 QELIGNLW 391
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
10-421 |
2.76e-19 |
|
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: 90.41 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 10 KAYINGEYVQAKDHKTfAVTNPANQQIICELpdlSAEETEYAIACA---AQAQKKWQKVTPKERANLLRRWYNLVIENQE 86
Cdd:cd07128 2 QSYVAGQWHAGTGDGR-TLHDAVTGEVVARV---SSEGLDFAAAVAyarEKGGPALRALTFHERAAMLKALAKYLMERKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 87 ELAQLlSLEQGKPINESRGEILYGASFIEWFAEEAKR--------IYGDVLPQDKEN----HRLLVIKQGIGVvaAITPW 154
Cdd:cd07128 78 DLYAL-SAATGATRRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPLSKDGtfvgQHILTPRRGVAV--HINAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 155 NFPNAMITRKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAG-LPAGLFNVIT-STRSveigkvLTEHPTVRK-VTFT 231
Cdd:cd07128 155 NFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICgSVGD------LLDHLGEQDvVAFT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 232 GSTRVGKILMAQSAS-------TVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDRF 304
Cdd:cd07128 229 GSAATAAKLRAHPNIvarsirfNAEADSLNAAILGPDATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 305 VEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIDDATAkGANLVIGGK-------LHTRGGTFFEPTVLR--DV 375
Cdd:cd07128 309 IEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLA-EAEVVFGGPdrfevvgADAEKGAFFPPTLLLcdDP 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 505740937 376 TQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQD 421
Cdd:cd07128 388 DAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
8-421 |
7.08e-15 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 76.67 E-value: 7.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 8 KTKAYINGEYVQAKDHKTfAVTNPANQQiicELPDLSAEETEYAIACA---AQAQKKWQKVTPKERANLLRRWYNLVIEN 84
Cdd:PRK11903 4 LLANYVAGRWQAGSGAGT-PLFDPVTGE---ELVRVSATGLDLAAAFAfarEQGGAALRALTYAQRAALLAAIVKVLQAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 85 QEELAQLLSLEQGKPINESRGEIlYGASF-IEWFAEEAKRIyGDV-LPQDKENHRL-----------LVIKQGIGVVaaI 151
Cdd:PRK11903 80 RDAYYDIATANSGTTRNDSAVDI-DGGIFtLGYYAKLGAAL-GDArLLRDGEAVQLgkdpafqgqhvLVPTRGVALF--I 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 152 TPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAG-LPAGLFNVITSTRsveiGKVLTEHPTVRKVTF 230
Cdd:PRK11903 156 NAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSS----AGLLDHLQPFDVVSF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 231 TGSTRVGKILMAQSA-------STVKKLSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYVQAGIYDR 303
Cdd:PRK11903 232 TGSAETAAVLRSHPAvvqrsvrVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 304 FVEQFSAKVAAFKVGSANEAGVNIGPLISQSAVNKIQEHIdDATAKGANLVIGGKLHT------RGGTFFEPTVL--RDV 375
Cdd:PRK11903 312 VAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLgaSDP 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 505740937 376 TQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGLASYLYTQD 421
Cdd:PRK11903 391 DAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
197-407 |
1.27e-13 |
|
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: 72.57 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 197 AGLPAGLFNVITStRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMAQSAS--TVKKLSLELGGNAPSIVFDDADLENA-- 272
Cdd:cd07129 164 TGLPAGVFSLLQG-GGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILPGALAERGea 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 273 -IEGIIASKFRNSGQTCVCTNRIYVQAGI-YDRFVEQFSAKVAAFKvgsaneAGVNIGPLIsQSAVNKIQEHIddATAKG 350
Cdd:cd07129 243 iAQGFVGSLTLGAGQFCTNPGLVLVPAGPaGDAFIAALAEALAAAP------AQTMLTPGI-AEAYRQGVEAL--AAAPG 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505740937 351 ANLVIGGK------------LHTRGGTFFEPTVLRdvtqamlvakDETFAPLAPVFKFDTEAQVIEMAN 407
Cdd:cd07129 314 VRVLAGGAaaeggnqaaptlFKVDAAAFLADPALQ----------EEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
51-313 |
1.51e-09 |
|
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: 59.97 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 51 AIACAAQAQKKWQKVTPKERANLLRRWYNLVIENQEELAQLLSLEQGKPI-------NESRGEILYGAsfiewfaeEAKR 123
Cdd:cd07081 4 AVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRvedkvikNHFAAEYIYNV--------YKDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 124 IYGDVLPQDkENHRLLVIKQGIGVVAAITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGL 203
Cdd:cd07081 76 KTCGVLTGD-ENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 204 FNVITST---RSVEIGKVLTEHPTVRKVTFTGstrvGKILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIASK 280
Cdd:cd07081 155 PENLIGWidnPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSK 230
|
250 260 270
....*....|....*....|....*....|...
gi 505740937 281 FRNSGQTCVCTNRIYVQAGIYDRFVEQFSAKVA 313
Cdd:cd07081 231 TFDNGVICASEQSVIVVDSVYDEVMRLFEGQGA 263
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
47-451 |
1.06e-08 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 57.49 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 47 ETEYAIACAAQAQKKWQKVTPKERANL----LRRWYnlviENQEELAQ----------LLSLEQGKPINESRG--EILYG 110
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGVcleiLQRLN----ARSFEMAHavmhttgqafMMAFQAGGPHAQDRGleAVAYA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 111 A---SFI----EWFAEEAKRiygDVLPQDKenhRLLVIKQGIGVV---AAITPWN-FP---------NAMITrKAAPAFA 170
Cdd:cd07127 161 WremSRIpptaEWEKPQGKH---DPLAMEK---TFTVVPRGVALVigcSTFPTWNgYPglfaslatgNPVIV-KPHPAAI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 171 AGCAMVLKPAQETplsalalaelAHQAGLPAGLFNVITSTRSVEIGKVLTEHPTVRKVTFTGSTRVGKILmaQSASTVKK 250
Cdd:cd07127 234 LPLAITVQVAREV----------LAEAGFDPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWL--EANARQAQ 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 251 LSLELGGNAPSIVFDDADLENAIEGIIASKFRNSGQTCVCTNRIYV-QAGI--------YDRFVEQFSAKVAAFKVGSAN 321
Cdd:cd07127 302 VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAIDGLLADPAR 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 322 EAGVnIGPLISQSAVNKIQEhiddATAKGANLVIGGKL-HTRggtfFEPTVLRdvtQAMLVAKD---------ETFAPLA 391
Cdd:cd07127 382 AAAL-LGAIQSPDTLARIAE----ARQLGEVLLASEAVaHPE----FPDARVR---TPLLLKLDasdeaayaeERFGPIA 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505740937 392 PVFKFDTEAQVIEMANDT--EFG-LASYLYTQDISRIWRVSE-ALEYGI---VGINEGLISNEMAPF 451
Cdd:cd07127 450 FVVATDSTDHSIELARESvrEHGaMTVGVYSTDPEVVERVQEaALDAGValsINLTGGVFVNQSAAF 516
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
195-315 |
1.53e-08 |
|
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: 56.73 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 195 HQAGLPAGLFNVITsTRSVEIGKVLTEHPTVRKVTFTGSTRvgkilMAQSASTVKKLSLELG-GNAPSIVFDDADLENAI 273
Cdd:cd07122 150 VAAGAPEGLIQWIE-EPSIELTQELMKHPDVDLILATGGPG-----MVKAAYSSGKPAIGVGpGNVPAYIDETADIKRAV 223
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 505740937 274 EGIIASK-FRNsGQTCVCTNRIYVQAGIYDRFVEQFSAKVAAF 315
Cdd:cd07122 224 KDIILSKtFDN-GTICASEQSVIVDDEIYDEVRAELKRRGAYF 265
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
12-358 |
2.37e-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: 56.35 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 12 YINGEYVQAKDHKTfaVTNPANQQIICELPDLSAEETEYAIACAAQAQKK--WQKVTPKERanllrrwYNLVIENQEELA 89
Cdd:cd07126 2 LVAGKWKGASNYTT--LLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSglHNPLKNPER-------YLLYGDVSHRVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 90 QLLSLEQ-------------GKPINESRGEILYGASFIEWFAEEAKR-------IYGDVLPQDKENHRLlvikqGIGVVA 149
Cdd:cd07126 73 HELRKPEvedffarliqrvaPKSDAQALGEVVVTRKFLENFAGDQVRflarsfnVPGDHQGQQSSGYRW-----PYGPVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 150 AITPWNFPNAMITRKAAPAFAAGCAMVLKPAQETPLSALALAELAHQAGLPAGLFNVITSTrSVEIGKVLTEhPTVRKVT 229
Cdd:cd07126 148 IITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSD-GPTMNKILLE-ANPRMTL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 230 FTGSTRVGkilmaqsastvKKLSLELGGNapsIVFDDADLENAIEGIIASKFRN------------SGQTCVCTNRIY-- 295
Cdd:cd07126 226 FTGSSKVA-----------ERLALELHGK---VKLEDAGFDWKILGPDVSDVDYvawqcdqdayacSGQKCSAQSILFah 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505740937 296 ---VQAGIYDRFveqfsAKVAAFKvgsaNEAGVNIGPLISQSAvNKIQEHIDDATA-KGANLVIGGK 358
Cdd:cd07126 292 enwVQAGILDKL-----KALAEQR----KLEDLTIGPVLTWTT-ERILDHVDKLLAiPGAKVLFGGK 348
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
123-317 |
9.67e-06 |
|
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: 47.60 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 123 RIYGDVLPQDKEnhrLLVIKQGIGVVAAITPWNFPNAMITrKAAPAFAAGCAMVLKPAQETPLSALALAELAhQAGLPAG 202
Cdd:cd07077 82 HIQDVLLPDNGE---TYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLF-QAADAAH 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 203 ---LFNVITSTRSVEIGKVLTEHPTVRKVTFTGSTRVgkILMAQSASTVKKLSLELGGNAPSIVFDDADLENAIEGIIAS 279
Cdd:cd07077 157 gpkILVLYVPHPSDELAEELLSHPKIDLIVATGGRDA--VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505740937 280 KFRNsGQTCVCTNRIYVQAGIYDRFVEQFSAK--VAAFKV 317
Cdd:cd07077 235 KFFD-QNACASEQNLYVVDDVLDPLYEEFKLKlvVEGLKV 273
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
128-450 |
9.69e-05 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 45.18 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 128 VLPQDKEnHRLLVIKQGIGVVAAITPWNFPN------AMI---TR---------KAAPAFAAGCAMVLKPAQEtplsala 189
Cdd:PRK13805 93 VIEEDDE-FGIIEIAEPVGVIAGITPTTNPTstaifkALIalkTRnpiifsfhpRAQKSSIAAAKIVLDAAVA------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 190 laelahqAGLPAGLFNVItSTRSVEIGKVLTEHPTVRKVTFTGSTRvgkilMAQSASTVKKLSLELG-GNAPSIVFDDAD 268
Cdd:PRK13805 165 -------AGAPKDIIQWI-EEPSVELTNALMNHPGIALILATGGPG-----MVKAAYSSGKPALGVGaGNVPAYIDKTAD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 269 LENAIEGIIASK-FRNsGQTCVCTNRIYVQAGIYDRFVEQFS------------AKVAAFKVGSANeAGVNiGPLISQSA 335
Cdd:PRK13805 232 IKRAVNDILLSKtFDN-GMICASEQAVIVDDEIYDEVKEEFAshgayflnkkelKKLEKFIFGKEN-GALN-ADIVGQSA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 336 VnKIQEHIDDATAKGANLVIGgklhtrggtffEPTvlrdvtqamLVAKDETFA--PLAPV---FKFDTEAQVIEMAND-T 409
Cdd:PRK13805 309 Y-KIAEMAGFKVPEDTKILIA-----------EVK---------GVGESEPLSheKLSPVlamYKAKDFEDAVEKAEKlV 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 505740937 410 EFGLA---SYLYTQDISRIWRVSEALEYGIVGINE-------GLISNEMAP 450
Cdd:PRK13805 368 EFGGLghtAVIYTNDDELIKEFGLRMKACRILVNTpssqggiGDLYNKLAP 418
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
196-425 |
5.10e-04 |
|
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: 42.22 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 196 QAGLPAGLFNVITsTRSVEIGKVLTEHPTVRKVTFTGSTRVGKILMaqsaSTVKKLSLELGGNAPSIVFDDADLENAIEG 275
Cdd:cd07121 153 EAGGPDNLVVTVE-EPTIETTNELMAHPDINLLVVTGGPAVVKAAL----SSGKKAIGAGAGNPPVVVDETADIEKAARD 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 276 IIAS-KFRNSgQTCVCTNRIYVQAGIYDRFVEQFSaKVAAFKVGSANEAGV-------NIGPLISQSAVNKiqehidDAT 347
Cdd:cd07121 228 IVQGaSFDNN-LPCIAEKEVIAVDSVADYLIAAMQ-RNGAYVLNDEQAEQLlevvlltNKGATPNKKWVGK------DAS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 348 --AKGANLVIGGKLhtrggtffePTVLRDVTQAMLVAKDETFAPLAPVFKFDTEAQVIEMANDTEFGL--ASYLYTQDIS 423
Cdd:cd07121 300 kiLKAAGIEVPADI---------RLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVE 370
|
..
gi 505740937 424 RI 425
Cdd:cd07121 371 NL 372
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
202-308 |
8.98e-04 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 41.81 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505740937 202 GLFNVITSTR--SVEIGKVLTEHPTVRKVTFTGSTRVGKILMaqsaSTVKKLSLELGGNAPSIVFDDADLENAIEGII-- 277
Cdd:PRK15398 188 GPENLVVTVAepTIETAQRLMKHPGIALLVVTGGPAVVKAAM----KSGKKAIGAGAGNPPVVVDETADIEKAARDIVkg 263
|
90 100 110
....*....|....*....|....*....|.
gi 505740937 278 ASkFRNSgQTCVCTNRIYVQAGIYDRFVEQF 308
Cdd:PRK15398 264 AS-FDNN-LPCIAEKEVIVVDSVADELMRLM 292
|
|
| |
