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Conserved domains on  [gi|490083268|ref|WP_003985301|]
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MULTISPECIES: 3-hydroxyacyl-CoA dehydrogenase [Streptomyces]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK08268 super family cl35670
3-hydroxy-acyl-CoA dehydrogenase; Validated
1-497 0e+00

3-hydroxy-acyl-CoA dehydrogenase; Validated


The actual alignment was detected with superfamily member PRK08268:

Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 591.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   1 MTAIEAGRTVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATT 80
Cdd:PRK08268   1 MMALPSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGKLTAEQADAALARLRPVEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  81 LPELADVALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSG 160
Cdd:PRK08268  81 LADLADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 161 FATDEAAATTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFELMDLIG 240
Cdd:PRK08268 161 LATDPAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFELMDLIG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 241 QDVNEAVTRSVWEGFFRDPKFTPSLAQRRLVEAGLLGRKAGQGWYDHAEGAAEPLPHTAEPCPAPAAVaVHTQLAGPAAV 320
Cdd:PRK08268 241 LDVNHAVMESVYRQFYQEPRFRPSLIQQELVAAGRLGRKSGQGFYRYADGAKQPPAEAAPPAALPPVW-VSADVEGDLAA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 321 VQELIEEAGIKVTRERAPGEHEGCIRLPGGARLALTDGqpATGDLSGPTIRFDLALDYRAATRIALAPGAEVSSQDVREA 400
Cdd:PRK08268 320 LARLLERLGATIETGEGPSADGLVLLAPTGGDTTTAAA--REGLDAARVVLIDLLLDYAAAKRRTLMAAPATSPAARDAA 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 401 VGLFQALGKAVSVIEDVPGLIVARTVAMIVDFAADAEARGVASREDIDTAMRLGVNYPGGPSEWADGIGRHWLWHLLDSM 480
Cdd:PRK08268 398 HALFQQDGKAVSVIRDSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPLGPLAWGDRLGAARILRVLENL 477
                        490
                 ....*....|....*..
gi 490083268 481 HHQYAGGRYAPSWALRR 497
Cdd:PRK08268 478 QALYGDPRYRPSPWLRR 494
 
Name Accession Description Interval E-value
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
1-497 0e+00

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 591.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   1 MTAIEAGRTVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATT 80
Cdd:PRK08268   1 MMALPSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGKLTAEQADAALARLRPVEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  81 LPELADVALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSG 160
Cdd:PRK08268  81 LADLADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 161 FATDEAAATTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFELMDLIG 240
Cdd:PRK08268 161 LATDPAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFELMDLIG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 241 QDVNEAVTRSVWEGFFRDPKFTPSLAQRRLVEAGLLGRKAGQGWYDHAEGAAEPLPHTAEPCPAPAAVaVHTQLAGPAAV 320
Cdd:PRK08268 241 LDVNHAVMESVYRQFYQEPRFRPSLIQQELVAAGRLGRKSGQGFYRYADGAKQPPAEAAPPAALPPVW-VSADVEGDLAA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 321 VQELIEEAGIKVTRERAPGEHEGCIRLPGGARLALTDGqpATGDLSGPTIRFDLALDYRAATRIALAPGAEVSSQDVREA 400
Cdd:PRK08268 320 LARLLERLGATIETGEGPSADGLVLLAPTGGDTTTAAA--REGLDAARVVLIDLLLDYAAAKRRTLMAAPATSPAARDAA 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 401 VGLFQALGKAVSVIEDVPGLIVARTVAMIVDFAADAEARGVASREDIDTAMRLGVNYPGGPSEWADGIGRHWLWHLLDSM 480
Cdd:PRK08268 398 HALFQQDGKAVSVIRDSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPLGPLAWGDRLGAARILRVLENL 477
                        490
                 ....*....|....*..
gi 490083268 481 HHQYAGGRYAPSWALRR 497
Cdd:PRK08268 478 QALYGDPRYRPSPWLRR 494
PaaC-3OHAcCoADH TIGR02279
3-hydroxyacyl-CoA dehydrogenase PaaC; This 3-hydroxyacyl-CoA dehydrogenase is involved in the ...
9-497 1.58e-158

3-hydroxyacyl-CoA dehydrogenase PaaC; This 3-hydroxyacyl-CoA dehydrogenase is involved in the degradation of phenylacetic acid, presumably in steps following the opening of the phenyl ring. The sequences included in this model are all found in aparrent operons with other related genes such as paaA, paaB, paaD, paaE, paaF and paaN. Some genomes contain these other genes without an apparent paaC in the same operon - possibly in these cases a different dehydrogenase involved in fatty acid degradation may fill in the needed activity. This enzyme has domains which are members of the pfam02737 and pfam00725 families.


Pssm-ID: 188207 [Multi-domain]  Cd Length: 503  Bit Score: 460.18  E-value: 1.58e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268    9 TVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPELADVA 88
Cdd:TIGR02279   7 TVAVIGAGAMGAGIAQVAASAGHQVLLYDIRAEALARAIAGIEARLNSLVTKGKLTAEECERTLKRLIPVTDLHALADAG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   89 LVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDEAAA 168
Cdd:TIGR02279  87 LVIEAIVENLEVKKALFAQLEELCPADTIIASNTSSLSITAIAAGLARPERVAGLHFFNPAPVMALVEVVSGLATAAEVA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  169 TTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFELMDLIGQDVNEAVT 248
Cdd:TIGR02279 167 EQLYETALAWGKQPVHCHSTPGFIVNRVARPYYAEALRALEEQVAAPAVLDAALRDGAGFPMGPFELTDLIGHDVNFAVT 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  249 RSVWEGFFRDPKFTPSLAQRRLVEAGLLGRKAGQGWYDHAEGAAEPLPHTAEPCPAPAAVAVHTQLaGPAAVVQELIEEA 328
Cdd:TIGR02279 247 CSVFNAFWQDRRFLPSLVQQELVIAGRLGRKSGLGVYDYREEAEAVVPLEAVSDSFSPRVTVVGDI-GAAAPLLARLEAA 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  329 GIKVTRERAPGEHEgcirlPGGARLALTDGQPATG----DLSGPTIRFDLALDYRAATRIALAPGAEVSSQDVREAVGLF 404
Cdd:TIGR02279 326 GIKVEKKSGMGVTQ-----IGDALLALTDGRTAQAraieLARPNLVLFDLVLDYSTGKRIAIAAAAVNPDSATRKAIYYL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  405 QALGKAVSVIEDVPGLIVARTVAMIVDFAADAEARGVASREDIDTAMRLGVNYPGGPSEWADGIGRHWLWHLLDSMHHQY 484
Cdd:TIGR02279 401 QQAGKKVLQIADYPGLLILRTVAMLANEAADAVLQGVASAQDIDTAMRLGVNYPYGPLAWAAQLGWQRILRVLENLQHHY 480
                         490
                  ....*....|...
gi 490083268  485 AGGRYAPSWALRR 497
Cdd:TIGR02279 481 GEERYRPSSLLRR 493
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
8-286 6.81e-99

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 299.33  E-value: 6.81e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   8 RTVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPELADv 87
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAALARITPTTDLAALAD- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  88 alvveavveelsA-------------KQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPL 154
Cdd:COG1250   82 ------------AdlvieavpedldlKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 155 VEVVSGFATDEAAATTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFE 234
Cdd:COG1250  150 VEVIRGPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFE 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490083268 235 LMDLIGQDVNEAVTRSVWEGfFRDPKFTPSLAQRRLVEAGLLGRKAGQGWYD 286
Cdd:COG1250  230 LADLVGLDTALAVLEVLYEA-LGDPRYRPPPLLKKLVEAGRLGRKTGRGFYD 280
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
9-188 6.00e-46

3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 158.47  E-value: 6.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268    9 TVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPELADVA 88
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVDAALARISFTTDLAAAVDAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   89 LVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDEAAA 168
Cdd:pfam02737  81 LVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPETV 160
                         170       180
                  ....*....|....*....|
gi 490083268  169 TTAYETAAAWGKSPVRSADT 188
Cdd:pfam02737 161 ATTVELAKKIGKTPVVVKDT 180
 
Name Accession Description Interval E-value
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
1-497 0e+00

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 591.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   1 MTAIEAGRTVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATT 80
Cdd:PRK08268   1 MMALPSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGKLTAEQADAALARLRPVEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  81 LPELADVALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSG 160
Cdd:PRK08268  81 LADLADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 161 FATDEAAATTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFELMDLIG 240
Cdd:PRK08268 161 LATDPAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFELMDLIG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 241 QDVNEAVTRSVWEGFFRDPKFTPSLAQRRLVEAGLLGRKAGQGWYDHAEGAAEPLPHTAEPCPAPAAVaVHTQLAGPAAV 320
Cdd:PRK08268 241 LDVNHAVMESVYRQFYQEPRFRPSLIQQELVAAGRLGRKSGQGFYRYADGAKQPPAEAAPPAALPPVW-VSADVEGDLAA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 321 VQELIEEAGIKVTRERAPGEHEGCIRLPGGARLALTDGqpATGDLSGPTIRFDLALDYRAATRIALAPGAEVSSQDVREA 400
Cdd:PRK08268 320 LARLLERLGATIETGEGPSADGLVLLAPTGGDTTTAAA--REGLDAARVVLIDLLLDYAAAKRRTLMAAPATSPAARDAA 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 401 VGLFQALGKAVSVIEDVPGLIVARTVAMIVDFAADAEARGVASREDIDTAMRLGVNYPGGPSEWADGIGRHWLWHLLDSM 480
Cdd:PRK08268 398 HALFQQDGKAVSVIRDSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPLGPLAWGDRLGAARILRVLENL 477
                        490
                 ....*....|....*..
gi 490083268 481 HHQYAGGRYAPSWALRR 497
Cdd:PRK08268 478 QALYGDPRYRPSPWLRR 494
PaaC-3OHAcCoADH TIGR02279
3-hydroxyacyl-CoA dehydrogenase PaaC; This 3-hydroxyacyl-CoA dehydrogenase is involved in the ...
9-497 1.58e-158

3-hydroxyacyl-CoA dehydrogenase PaaC; This 3-hydroxyacyl-CoA dehydrogenase is involved in the degradation of phenylacetic acid, presumably in steps following the opening of the phenyl ring. The sequences included in this model are all found in aparrent operons with other related genes such as paaA, paaB, paaD, paaE, paaF and paaN. Some genomes contain these other genes without an apparent paaC in the same operon - possibly in these cases a different dehydrogenase involved in fatty acid degradation may fill in the needed activity. This enzyme has domains which are members of the pfam02737 and pfam00725 families.


Pssm-ID: 188207 [Multi-domain]  Cd Length: 503  Bit Score: 460.18  E-value: 1.58e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268    9 TVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPELADVA 88
Cdd:TIGR02279   7 TVAVIGAGAMGAGIAQVAASAGHQVLLYDIRAEALARAIAGIEARLNSLVTKGKLTAEECERTLKRLIPVTDLHALADAG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   89 LVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDEAAA 168
Cdd:TIGR02279  87 LVIEAIVENLEVKKALFAQLEELCPADTIIASNTSSLSITAIAAGLARPERVAGLHFFNPAPVMALVEVVSGLATAAEVA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  169 TTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFELMDLIGQDVNEAVT 248
Cdd:TIGR02279 167 EQLYETALAWGKQPVHCHSTPGFIVNRVARPYYAEALRALEEQVAAPAVLDAALRDGAGFPMGPFELTDLIGHDVNFAVT 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  249 RSVWEGFFRDPKFTPSLAQRRLVEAGLLGRKAGQGWYDHAEGAAEPLPHTAEPCPAPAAVAVHTQLaGPAAVVQELIEEA 328
Cdd:TIGR02279 247 CSVFNAFWQDRRFLPSLVQQELVIAGRLGRKSGLGVYDYREEAEAVVPLEAVSDSFSPRVTVVGDI-GAAAPLLARLEAA 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  329 GIKVTRERAPGEHEgcirlPGGARLALTDGQPATG----DLSGPTIRFDLALDYRAATRIALAPGAEVSSQDVREAVGLF 404
Cdd:TIGR02279 326 GIKVEKKSGMGVTQ-----IGDALLALTDGRTAQAraieLARPNLVLFDLVLDYSTGKRIAIAAAAVNPDSATRKAIYYL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  405 QALGKAVSVIEDVPGLIVARTVAMIVDFAADAEARGVASREDIDTAMRLGVNYPGGPSEWADGIGRHWLWHLLDSMHHQY 484
Cdd:TIGR02279 401 QQAGKKVLQIADYPGLLILRTVAMLANEAADAVLQGVASAQDIDTAMRLGVNYPYGPLAWAAQLGWQRILRVLENLQHHY 480
                         490
                  ....*....|...
gi 490083268  485 AGGRYAPSWALRR 497
Cdd:TIGR02279 481 GEERYRPSSLLRR 493
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
8-286 6.81e-99

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 299.33  E-value: 6.81e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   8 RTVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPELADv 87
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAALARITPTTDLAALAD- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  88 alvveavveelsA-------------KQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPL 154
Cdd:COG1250   82 ------------AdlvieavpedldlKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 155 VEVVSGFATDEAAATTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFE 234
Cdd:COG1250  150 VEVIRGPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFE 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490083268 235 LMDLIGQDVNEAVTRSVWEGfFRDPKFTPSLAQRRLVEAGLLGRKAGQGWYD 286
Cdd:COG1250  230 LADLVGLDTALAVLEVLYEA-LGDPRYRPPPLLKKLVEAGRLGRKTGRGFYD 280
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
8-287 1.53e-65

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 213.29  E-value: 1.53e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   8 RTVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPELADV 87
Cdd:PRK05808   4 QKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAALARITGTTDLDDLKDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  88 ALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDEAA 167
Cdd:PRK05808  84 DLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRGLATSDAT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 168 ATTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFELMDLIGQDVNEAV 247
Cdd:PRK05808 164 HEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLIGLDTCLAI 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 490083268 248 TRSVWEGfFRDPKFTPSLAQRRLVEAGLLGRKAGQGWYDH 287
Cdd:PRK05808 244 MEVLYEG-FGDSKYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
8-287 6.73e-62

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 204.58  E-value: 6.73e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   8 RTVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPELADV 87
Cdd:PLN02545   5 KKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEADATLGRIRCTTNLEELRDA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  88 ALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDEAA 167
Cdd:PLN02545  85 DFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRGADTSDEV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 168 ATTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFELMDLIGQDVNEAV 247
Cdd:PLN02545 165 FDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIGLDTCLSI 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 490083268 248 TRsVWEGFFRDPKFTPSLAQRRLVEAGLLGRKAGQGWYDH 287
Cdd:PLN02545 245 MK-VLHEGLGDSKYRPCPLLVQYVDAGRLGRKSGRGVYHY 283
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
1-296 8.07e-59

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 196.38  E-value: 8.07e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   1 MTAIeagRTVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATT 80
Cdd:PRK07530   1 MMAI---KKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLARQVAKGKISEEARAAALARISTATD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  81 LPELADVALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSG 160
Cdd:PRK07530  78 LEDLADCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIRG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 161 FATDEAAATTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFELMDLIG 240
Cdd:PRK07530 158 IATDEATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIYTLYEGVGSVEAIDTAMKLGANHPMGPLELADFIG 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490083268 241 QDVNEAVTRSVWEGfFRDPKFTPSLAQRRLVEAGLLGRKAGQGWYDHAegAAEPLP 296
Cdd:PRK07530 238 LDTCLSIMQVLHDG-LADSKYRPCPLLVKYVEAGWLGRKTGRGFYDYR--GEVPVP 290
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
10-287 1.08e-54

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 185.19  E-value: 1.08e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  10 VAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPELADVAL 89
Cdd:PRK07819   8 VGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLERAVSRGKLTERERDAALARLRFTTDLGDFADRQL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  90 VVEAVVEELSAKQELFAALEDVVSE-DCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDEAAA 168
Cdd:PRK07819  88 VIEAVVEDEAVKTEIFAELDKVVTDpDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPTLVTSEATV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 169 TTAYE-TAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFELMDLIGQDVNEAV 247
Cdd:PRK07819 168 ARAEEfASDVLGKQVVRAQDRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPMGPLRLSDLVGLDTVKAI 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 490083268 248 TRSVWEGfFRDPKFTPSLAQRRLVEAGLLGRKAGQGWYDH 287
Cdd:PRK07819 248 ADSMYEE-FKEPLYAPPPLLLRMVEAGLLGKKSGRGFYTY 286
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
8-286 2.19e-52

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 179.30  E-value: 2.19e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   8 RTVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAI--GRR-LDRLVEKGKLPAAEREAARARLLPATTLPEL 84
Cdd:PRK06035   4 KVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIesGPYgLRNLVEKGKMSEDEAKAIMARIRTSTSYESL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  85 ADVALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATD 164
Cdd:PRK06035  84 SDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIEVVRAALTS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 165 EAAATTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFELMDLIGQDVN 244
Cdd:PRK06035 164 EETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFELMDIIGIDTV 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 490083268 245 EAVTRSVWEGfFRDPKFTPSLAQRRLVEAGLLGRKAGQ-----GWYD 286
Cdd:PRK06035 244 YHIAEYLYEE-TGDPQFIPPNSLKQMVLNGYVGDKKVKygskgGWFD 289
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
10-294 5.09e-47

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 164.96  E-value: 5.09e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  10 VAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPE-LADVA 88
Cdd:PRK09260   4 LVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQGVARGKLTEAARQAALARLSYSLDLKAaVADAD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  89 LVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDEAAA 168
Cdd:PRK09260  84 LVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIRGLETSDETV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 169 TTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFELMDLIGQDVNEAVT 248
Cdd:PRK09260 164 QVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLELGDLVGLDTRLNNL 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 490083268 249 RSVWEGFfrDPKFTPSLAQRRLVEAGLLGRKAGQGWYDHAEGAAEP 294
Cdd:PRK09260 244 KYLHETL--GEKYRPAPLLEKYVKAGRLGRKTGRGVYDYTNRENVP 287
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
9-188 6.00e-46

3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 158.47  E-value: 6.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268    9 TVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPELADVA 88
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVDAALARISFTTDLAAAVDAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   89 LVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDEAAA 168
Cdd:pfam02737  81 LVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPETV 160
                         170       180
                  ....*....|....*....|
gi 490083268  169 TTAYETAAAWGKSPVRSADT 188
Cdd:pfam02737 161 ATTVELAKKIGKTPVVVKDT 180
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
8-286 4.03e-44

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 158.01  E-value: 4.03e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   8 RTVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATtlpeLADV 87
Cdd:PRK06130   5 QNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPLGIASAGMGRIRMEAGLAAA----VSGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  88 ALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDEAA 167
Cdd:PRK06130  81 DLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRGDKTSPQT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 168 ATTAYETAAAWGKSPVR-SADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRM---GPFELMDLIGQDV 243
Cdd:PRK06130 161 VATTMALLRSIGKRPVLvKKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQRDMNGLDV 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 490083268 244 NEAVTRSVWEGFfrDPKFTPSLAQRRLVEAGLLGRKAGQGWYD 286
Cdd:PRK06130 241 HLAVASYLYQDL--ENRTTPSPLLEEKVEAGELGAKSGQGFYA 281
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
8-291 1.82e-33

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 134.60  E-value: 1.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   8 RTVAVVGTGTMGQGIAQVALVAGHPVRLYD----ALPGRAAEAAGAIGRRldrlVEKGKLPAAEREAARARLLPATTLPE 83
Cdd:PRK11730 314 KQAAVLGAGIMGGGIAYQSASKGVPVIMKDinqkALDLGMTEAAKLLNKQ----VERGKIDGAKMAGVLSSIRPTLDYAG 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  84 LADVALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFAT 163
Cdd:PRK11730 390 FERVDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEVIRGEKT 469
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 164 DEAAATTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEErAADPATIDAVLRESGGFRMGPFELMDLIGQDV 243
Cdd:PRK11730 470 SDETIATVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRD-GADFRQIDKVMEKQFGWPMGPAYLLDVVGIDT 548
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490083268 244 NEAVTRSVWEGF-------FRDpkftpslAQRRLVEAGLLGRKAGQGWYDHAEGA 291
Cdd:PRK11730 549 AHHAQAVMAEGFpdrmkkdYRD-------AIDVLFEAKRFGQKNGKGFYRYEEDK 596
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
190-287 2.27e-33

3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda crystallin. Some proteins include two copies of this domain.


Pssm-ID: 395588 [Multi-domain]  Cd Length: 97  Bit Score: 121.94  E-value: 2.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  190 GFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFELMDLIGQDVNEAVTRsVWEGFFRDPKFTPSLAQRR 269
Cdd:pfam00725   1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILE-VLAEEFGDRAYRPPPLLEK 79
                          90
                  ....*....|....*...
gi 490083268  270 LVEAGLLGRKAGQGWYDH 287
Cdd:pfam00725  80 LVEAGRLGRKTGKGFYKY 97
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
8-290 1.29e-31

fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of mitochondrial multifunctional fatty acid degradation enzyme complex. Subunit activities include: enoyl-CoA hydratase (EC 4.2.1.17) _ 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35). Some characterization in human (SP:P40939), pig (SP:Q29554), and rat (SP:Q64428). The beta subunit has activity: acetyl-CoA C-acyltransferase (EC 2.3.1.16).


Pssm-ID: 131494 [Multi-domain]  Cd Length: 737  Bit Score: 129.19  E-value: 1.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268    8 RTVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPELADV 87
Cdd:TIGR02441 336 KTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDSILSNLTPTLDYSGFKNA 415
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   88 ALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDEAA 167
Cdd:TIGR02441 416 DMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITHDGTSKDT 495
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  168 ATTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEErAADPATIDAvLRESGGFRMGPFELMDLIGQDVNEAV 247
Cdd:TIGR02441 496 LASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQE-GVDPKKLDK-LTTKFGFPVGAATLADEVGVDVAEHV 573
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 490083268  248 TRSVWEGFfrDPKFTPSLAQ--RRLVEAGLLGRKAGQGWYDHAEG 290
Cdd:TIGR02441 574 AEDLGKAF--GERFGGGSAEllSELVKAGFLGRKSGKGIFIYQEG 616
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
18-288 8.74e-30

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 118.62  E-value: 8.74e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  18 MGQGIAQVALVAGHPVRLYDALPGRA-------AEAAGAIGRRLDRLVEKGKLPAAEREAARA--RLLPATTLPE-LADV 87
Cdd:PRK08269   1 MGQGIALAFAFAGHDVTLIDFKPRDAagwraldAEARAEIERTLAALVALGRIDAAQADAVLAriAVVARDGAADaLADA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  88 ALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDEAA 167
Cdd:PRK08269  81 DLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATDPAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 168 ATTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFR---MGPFELMDLIGQDVN 244
Cdd:PRK08269 161 VDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRfavLGLLEFIDWGGCDIL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 490083268 245 EAVTRSVwEGFFRDPKFTPSLAQRRLVEAGLLGRKAGQGWYDHA 288
Cdd:PRK08269 241 YYASRYL-AGEIGPDRFAPPAIVVRNMEEGRDGLRTGAGFYDYA 283
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
8-238 1.90e-27

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 112.06  E-value: 1.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   8 RTVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPE-LAD 86
Cdd:PRK06129   3 GSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLLDGEAPDAVLARIRVTDSLADaVAD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  87 VALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDEA 166
Cdd:PRK06129  83 ADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPWTAPA 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490083268 167 AATTAYETAAAWGKSPVR-SADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFR---MGPFELMDL 238
Cdd:PRK06129 163 TLARAEALYRAAGQSPVRlRREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGLRwsfMGPFETIDL 238
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
8-285 5.52e-22

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 99.59  E-value: 5.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   8 RTVAVVGTGTMGQGIAQVALV-AGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPELAD 86
Cdd:PRK11154 310 NKVGVLGGGLMGGGIAYVTATkAGLPVRIKDINPQGINHALKYSWDLLDKKVKRRHLKPSERDKQMALISGTTDYRGFKH 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  87 VALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDEA 166
Cdd:PRK11154 390 ADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMPLVEVIPHAKTSAE 469
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 167 AATTAYETAAAWGKSPVRSADTPGFIVNRIARPFYAEALRVYEErAADPATIDAVLRESgGFRMGPFELMDLIGQDVNEA 246
Cdd:PRK11154 470 TIATTVALAKKQGKTPIVVRDGAGFYVNRILAPYINEAARLLLE-GEPIEHIDAALVKF-GFPVGPITLLDEVGIDVGTK 547
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 490083268 247 VTRSVWEGFfrDPKFTPSLAQRRLVEAGLLGRKAGQGWY 285
Cdd:PRK11154 548 IIPILEAAL--GERFSAPAAFDKLLNDDRKGRKNGRGFY 584
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
8-286 3.44e-18

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 84.99  E-value: 3.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   8 RTVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPELA-- 85
Cdd:PRK08293   4 KNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIAKLADRYVRDLEATKEAPAEAALNRITLTTDLAEAvk 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  86 DVALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDE 165
Cdd:PRK08293  84 DADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGHPGTDP 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 166 AAATTAYETAAAWGKSPVRSA-DTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFRMGPFELMDLIGQDVN 244
Cdd:PRK08293 164 EVFDTVVAFAKAIGMVPIVLKkEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIVGLDTA 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 490083268 245 EAVTrSVWeGFFRDPKFTPSLAQ--RRLVEAGLLGRKAGQGWYD 286
Cdd:PRK08293 244 YNIT-SNW-AEATDDENAKKAAAllKEYIDKGKLGVATGEGFYN 285
3HCDH_RFF pfam18321
3-hydroxybutyryl-CoA dehydrogenase reduced Rossmann-fold domain; This domain is found in ...
353-418 9.07e-17

3-hydroxybutyryl-CoA dehydrogenase reduced Rossmann-fold domain; This domain is found in 3-hydroxybutyryl-CoA dehydrogenase present in E. coli. 3-hydroxybutyryl-CoA dehydrogenase catalyzes the second step in the biosynthesis of n-butanol from acetyl-CoA, in which acetoacetyl-CoA is reduced to 3-hydroxybutyryl-CoA. This domain is a reduced Rossmann-fold domain and, unlike the first Rossmann-fold domain, it is missing the catalytic residues and an NAD(H) binding cleft.


Pssm-ID: 436408 [Multi-domain]  Cd Length: 69  Bit Score: 74.59  E-value: 9.07e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490083268  353 LALTDGQPAT---GDLSGPTIRFDLALDYRAATRIALAPGAEVSSQDVREAVGLFQALGKAVSVIEDVP 418
Cdd:pfam18321   1 LALTDGRTATqraAELGRPVVLFDLALDYDSATRLAVAPAAQCSPQALAQAVALLQALGKAVLVLADAP 69
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
384-491 3.82e-14

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 72.84  E-value: 3.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 384 IALAPGAEVSSQDVREAVGLFQALGKAVSVIEDVPGLIVARTVAMIVDFAADAEARGVASREDIDTAMRLGVNYPGGPSE 463
Cdd:PLN02545 152 VEIIRGADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLH 231
                         90       100
                 ....*....|....*....|....*...
gi 490083268 464 WADGIGRHWLWHLLDSMHHQYAGGRYAP 491
Cdd:PLN02545 232 LADFIGLDTCLSIMKVLHEGLGDSKYRP 259
PRK07066 PRK07066
L-carnitine dehydrogenase;
1-242 3.18e-13

L-carnitine dehydrogenase;


Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 70.63  E-value: 3.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   1 MTAIEAGRTVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGAIGRRLDRLVEKGKLPAAEREAararLLPATT 80
Cdd:PRK07066   1 MAVITDIKTFAAIGSGVIGSGWVARALAHGLDVVAWDPAPGAEAALRANVANAWPALERQGLAPGASPAR----LRFVAT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  81 LPE-LADVALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVS 159
Cdd:PRK07066  77 IEAcVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 160 GFATDEAAATTAYETAAAWGKSPVR-SADTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFR---MGPFEL 235
Cdd:PRK07066 157 GERTAPEAVDAAMGIYRALGMRPLHvRKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRwsfMGTFLT 236

                 ....*..
gi 490083268 236 MDLIGQD 242
Cdd:PRK07066 237 YTLAGGD 243
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
388-497 1.30e-12

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 68.21  E-value: 1.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 388 PGAEVSSQDVREAVGLFQALGKAVSVIEDVPGLIVART-VAMIVDFAADAEaRGVASREDIDTAMRLGVNYPGGPSEWAD 466
Cdd:COG1250  154 RGPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRIlVPYLNEAIRLLE-EGVASPEDIDAAMRLGFGFPMGPFELAD 232
                         90       100       110
                 ....*....|....*....|....*....|.
gi 490083268 467 GIGRHWLWHLLDSMHHQYAGGRYAPSWALRR 497
Cdd:COG1250  233 LVGLDTALAVLEVLYEALGDPRYRPPPLLKK 263
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
384-503 3.45e-12

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 67.12  E-value: 3.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 384 IALAPGAEVSSQDVREAVGLFQALGKAVSVIEDVPGLIVARTVAMIVDFAADAEARGVASREDIDTAMRLGVNYPGGPSE 463
Cdd:PRK09260 150 VELIRGLETSDETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLE 229
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 490083268 464 WADGIGrhwLWHLLDSMH--HQYAGGRYAPSWALRRSLKQNR 503
Cdd:PRK09260 230 LGDLVG---LDTRLNNLKylHETLGEKYRPAPLLEKYVKAGR 268
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
419-503 5.83e-12

3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda crystallin. Some proteins include two copies of this domain.


Pssm-ID: 395588 [Multi-domain]  Cd Length: 97  Bit Score: 61.85  E-value: 5.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  419 GLIVARTVAMIVDFAADAEARGVASREDIDTAMRLGVNYPGGPSEWADGIGRHWLWHLLDSMHHQYAGGRYAPSWALRRS 498
Cdd:pfam00725   1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEVLAEEFGDRAYRPPPLLEKL 80

                  ....*
gi 490083268  499 LKQNR 503
Cdd:pfam00725  81 VEAGR 85
PRK07531 PRK07531
carnitine 3-dehydrogenase;
9-234 9.50e-12

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 67.07  E-value: 9.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268   9 TVAVVGTGTMGQGIAQVALVAGHPVRLYDALPgraaEAAGAIGRRLDRLVEKGKLPAAEREAARARLLPATTLPE-LADV 87
Cdd:PRK07531   6 KAACIGGGVIGGGWAARFLLAGIDVAVFDPHP----EAERIIGEVLANAERAYAMLTDAPLPPEGRLTFCASLAEaVAGA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268  88 ALVVEAVVEELSAKQELFAALEDVVSEDCLLATNTSSLSVTAVAGALRLPGRFVGLHFFNPAPLLPLVEVVSGFATDEAA 167
Cdd:PRK07531  82 DWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLVELVGGGKTSPET 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490083268 168 ATTAYETAAAWGKSPVRSA-DTPGFIVNRIARPFYAEALRVYEERAADPATIDAVLRESGGFR---MGPFE 234
Cdd:PRK07531 162 IRRAKEILREIGMKPVHIAkEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDVIRYSFGLRwaqMGLFE 232
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
400-469 1.74e-11

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 65.03  E-value: 1.74e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 400 AVGLFQALGKAVSVIEDVPGLIVARTVAMIVDFAADAEARGVASREDIDTAMRLGVNYPGGPSEWADGIG 469
Cdd:PRK07530 168 AKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIYTLYEGVGSVEAIDTAMKLGANHPMGPLELADFIG 237
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
393-496 7.10e-11

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 63.06  E-value: 7.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 393 SSQDVREAV-GLFQALGKAVSVIEDVPGLIVARTVAMIVDFAADAEARGVASREDIDTAMRLGVNYPGGPSEWADGIGRH 471
Cdd:PRK05808 159 TSDATHEAVeALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLIGLD 238
                         90       100
                 ....*....|....*....|....*
gi 490083268 472 WLWHLLDSMHHQYAGGRYAPSWALR 496
Cdd:PRK05808 239 TCLAIMEVLYEGFGDSKYRPCPLLR 263
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
392-497 1.35e-07

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 53.07  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 392 VSSQDVREAVGLF--QALGKAVSVIEDVPGLIVArtvAMIVDFAADA----EArGVASREDIDTAMRLGVNYPGGPSEWA 465
Cdd:PRK07819 161 VTSEATVARAEEFasDVLGKQVVRAQDRSGFVVN---ALLVPYLLSAirmvES-GFATAEDIDKAMVLGCAHPMGPLRLS 236
                         90       100       110
                 ....*....|....*....|....*....|..
gi 490083268 466 DGIGRHWLWHLLDSMHHQYAGGRYAPSWALRR 497
Cdd:PRK07819 237 DLVGLDTVKAIADSMYEEFKEPLYAPPPLLLR 268
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
384-497 4.28e-06

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 48.33  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 384 IALAPGAEVSSQDVREAVGLFQALGKAVSVIEDVPGLIVARTVAMIVDFAADAEARGVASREDIDTAMRLGVNYPGGPSE 463
Cdd:PRK06035 154 IEVVRAALTSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFE 233
                         90       100       110
                 ....*....|....*....|....*....|....
gi 490083268 464 WADGIGRHWLWHLLDSMHHQYAGGRYAPSWALRR 497
Cdd:PRK06035 234 LMDIIGIDTVYHIAEYLYEETGDPQFIPPNSLKQ 267
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
9-49 4.73e-04

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 42.02  E-value: 4.73e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 490083268   9 TVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAEAAGA 49
Cdd:COG2084    3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAA 43
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
389-457 2.04e-03

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 40.14  E-value: 2.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490083268 389 GAEVSSQDVREAVGLFQALGK-AVSVIEDVPGLIVARTVAMIVDFAADAEARGVASREDIDTAMRLGVNY 457
Cdd:PRK06130 153 GDKTSPQTVATTMALLRSIGKrPVLVKKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGI 222
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
386-454 2.94e-03

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 39.66  E-value: 2.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490083268 386 LAPGAEVS-----SQDVREAV-GLFQALGKAVSVIEDVPGLIVARTVAMIVDFAADAEARGVASREDIDTAMRLG 454
Cdd:PRK08269 144 LMPLVEVSpsdatDPAVVDRLaALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTG 218
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
9-51 3.48e-03

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 38.22  E-value: 3.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 490083268    9 TVAVVGTGTMGQGIAQVALVAGHPVRLYDALPGRAAE--AAGAIG 51
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEElvAAGAIA 45
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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