|
Name |
Accession |
Description |
Interval |
E-value |
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
23-262 |
2.87e-65 |
|
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: 207.27 E-value: 2.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 23 RKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPRRARALVALGHATEGMVERgLLELHQGRSLLQTVQD 102
Cdd:COG1250 3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADA-ALARITPTTDLAALAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 103 ADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAVA 182
Cdd:COG1250 82 ADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATSDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 183 SVTRAQEYLRALGRMPIVLkKPVPGYVVGRIAAAVWRECIDLVLTDVIAVDDLDRAVSLGpaLGWaAAGPHLTYHLAAGD 262
Cdd:COG1250 162 TVATAVAFARRLGKTPVVV-KDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLG--FGF-PMGPFELADLVGLD 237
|
|
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
22-327 |
3.36e-57 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 187.56 E-value: 3.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 22 PRKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPRRARALVALGHATEGMVERGLLELHQGRSLLQTVQ 101
Cdd:PRK06129 2 MGSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLLDGEAPDAVLARIRVTDSLADAVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 102 DADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAV 181
Cdd:PRK06129 82 DADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPWTAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 182 ASVTRAQEYLRALGRMPIVLKKPVPGYVVGRIAAAVWRECIDLVLTDVIAVDDLDRAVSLGPALGWAAAGPHLTYHLAAg 261
Cdd:PRK06129 162 ATLARAEALYRAAGQSPVRLRREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGLRWSFMGPFETIDLNA- 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125431683 262 DGGVTAFLQQLLASFEgwwgqlatwqRLEPEQQR------ALTQGVERAYKGKV--EELREA---RDRRLSAILRAL 327
Cdd:PRK06129 241 PGGVADYAQRYGPMYR----------RMAAERGQpvpwdgELVARVEAERRAALplDQLAARqawRDRRLMALAAHR 307
|
|
| 3HCDH_N |
pfam02737 |
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ... |
24-202 |
3.36e-54 |
|
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.
Pssm-ID: 397037 [Multi-domain] Cd Length: 180 Bit Score: 175.42 E-value: 3.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 24 KVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPRRARALVALGHATEGMVERgLLELHQGRSLLQTVQDA 103
Cdd:pfam02737 1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVDA-ALARISFTTDLAAAVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 104 DWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAVAS 183
Cdd:pfam02737 80 DLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPET 159
|
170
....*....|....*....
gi 1125431683 184 VTRAQEYLRALGRMPIVLK 202
Cdd:pfam02737 160 VATTVELAKKIGKTPVVVK 178
|
|
| fa_ox_alpha_mit |
TIGR02441 |
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ... |
23-237 |
1.38e-13 |
|
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: 71.41 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 23 RKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPR------RARALVALghategmvERGLLELHQGRSL 96
Cdd:TIGR02441 336 KTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKglnkkvKRKKITSL--------ERDSILSNLTPTL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 97 -LQTVQDADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVP 175
Cdd:TIGR02441 408 dYSGFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIIT 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125431683 176 GARTAVASVTRAQEYLRALGRMPIVLKKpVPGYVVGRIAAAVWRECIDLvLTDVIAVDDLDR 237
Cdd:TIGR02441 488 HDGTSKDTLASAVAVGLKQGKVVIVVKD-GPGFYTTRCLGPMLAEVIRL-LQEGVDPKKLDK 547
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
23-262 |
2.87e-65 |
|
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: 207.27 E-value: 2.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 23 RKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPRRARALVALGHATEGMVERgLLELHQGRSLLQTVQD 102
Cdd:COG1250 3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADA-ALARITPTTDLAALAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 103 ADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAVA 182
Cdd:COG1250 82 ADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATSDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 183 SVTRAQEYLRALGRMPIVLkKPVPGYVVGRIAAAVWRECIDLVLTDVIAVDDLDRAVSLGpaLGWaAAGPHLTYHLAAGD 262
Cdd:COG1250 162 TVATAVAFARRLGKTPVVV-KDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLG--FGF-PMGPFELADLVGLD 237
|
|
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
22-327 |
3.36e-57 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 187.56 E-value: 3.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 22 PRKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPRRARALVALGHATEGMVERGLLELHQGRSLLQTVQ 101
Cdd:PRK06129 2 MGSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLLDGEAPDAVLARIRVTDSLADAVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 102 DADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAV 181
Cdd:PRK06129 82 DADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPWTAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 182 ASVTRAQEYLRALGRMPIVLKKPVPGYVVGRIAAAVWRECIDLVLTDVIAVDDLDRAVSLGPALGWAAAGPHLTYHLAAg 261
Cdd:PRK06129 162 ATLARAEALYRAAGQSPVRLRREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGLRWSFMGPFETIDLNA- 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125431683 262 DGGVTAFLQQLLASFEgwwgqlatwqRLEPEQQR------ALTQGVERAYKGKV--EELREA---RDRRLSAILRAL 327
Cdd:PRK06129 241 PGGVADYAQRYGPMYR----------RMAAERGQpvpwdgELVARVEAERRAALplDQLAARqawRDRRLMALAAHR 307
|
|
| 3HCDH_N |
pfam02737 |
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ... |
24-202 |
3.36e-54 |
|
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.
Pssm-ID: 397037 [Multi-domain] Cd Length: 180 Bit Score: 175.42 E-value: 3.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 24 KVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPRRARALVALGHATEGMVERgLLELHQGRSLLQTVQDA 103
Cdd:pfam02737 1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVDA-ALARISFTTDLAAAVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 104 DWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAVAS 183
Cdd:pfam02737 80 DLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPET 159
|
170
....*....|....*....
gi 1125431683 184 VTRAQEYLRALGRMPIVLK 202
Cdd:pfam02737 160 VATTVELAKKIGKTPVVVK 178
|
|
| PRK07531 |
PRK07531 |
carnitine 3-dehydrogenase; |
19-327 |
1.26e-50 |
|
carnitine 3-dehydrogenase;
Pssm-ID: 236044 [Multi-domain] Cd Length: 495 Bit Score: 175.31 E-value: 1.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 19 IALPRKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGmERAAIDVPRRA-RALVALGHATegMVERGLLELHQgrSLL 97
Cdd:PRK07531 1 MTMIMKAACIGGGVIGGGWAARFLLAGIDVAVFDPHPEA-ERIIGEVLANAeRAYAMLTDAP--LPPEGRLTFCA--SLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 98 QTVQDADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGA 177
Cdd:PRK07531 76 EAVAGADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLVELVGGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 178 RTAVASVTRAQEYLRALGRMPIVLKKPVPGYVVGRIAAAVWRECIDLVLTDVIAVDDLDRAVSLGPALGWAAAGPHLTYH 257
Cdd:PRK07531 156 KTSPETIRRAKEILREIGMKPVHIAKEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDVIRYSFGLRWAQMGLFETYR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125431683 258 LAAGDGGVTAFLQQLLASFEGWWGQLATwqrlEPEQQRALT-----QGVERAYKGKVEELREARDRRLSAILRAL 327
Cdd:PRK07531 236 IAGGEAGMRHFLAQFGPCLKWPWTKLMD----VPDLDDALVdkiagQSDAQSGGLSIRELERIRDENLVGIMQAL 306
|
|
| PRK07066 |
PRK07066 |
L-carnitine dehydrogenase; |
23-331 |
7.99e-48 |
|
L-carnitine dehydrogenase;
Pssm-ID: 168796 [Multi-domain] Cd Length: 321 Bit Score: 163.47 E-value: 7.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 23 RKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPRRARALVALGHATEGMVERglleLHQGRSLLQTVQD 102
Cdd:PRK07066 8 KTFAAIGSGVIGSGWVARALAHGLDVVAWDPAPGAEAALRANVANAWPALERQGLAPGASPAR----LRFVATIEACVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 103 ADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAVA 182
Cdd:PRK07066 84 ADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLGGERTAPE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 183 SVTRAQEYLRALGRMPIVLKKPVPGYVVGRIAAAVWRECIDLVLTDVIAVDDLDRAVSLGPALGWAAAGPHLTYHLAAGD 262
Cdd:PRK07066 164 AVDAAMGIYRALGMRPLHVRKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRWSFMGTFLTYTLAGGD 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125431683 263 GGVTAFLQQLLASFEGWWGQLATWQRLEPEQQRALTQGVERAYKGKVEELREARDRRLSAILRALEQAR 331
Cdd:PRK07066 244 AGMRHFMQQFGPALELPWTKLVAPELTDALIDRVVEGTAEQQGPRSIKALERYRDECITEVLEAIAAVK 312
|
|
| PRK06130 |
PRK06130 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
23-252 |
2.78e-44 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 235707 [Multi-domain] Cd Length: 311 Bit Score: 153.77 E-value: 2.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 23 RKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPRRARALVALGHATEGMverGLLELHQGrsLLQTVQD 102
Cdd:PRK06130 5 QNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPLGIASAGM---GRIRMEAG--LAAAVSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 103 ADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAVA 182
Cdd:PRK06130 80 ADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRGDKTSPQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 183 SVTRAQEYLRALGRMPIVLKKPVPGYVVGRIAAAVWRECIDLVLTDVIAVDDLDRAVSLGPALGWAAAGP 252
Cdd:PRK06130 160 TVATTMALLRSIGKRPVLVKKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLALTGP 229
|
|
| PRK09260 |
PRK09260 |
3-hydroxyacyl-CoA dehydrogenase; |
24-242 |
3.07e-38 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 236434 [Multi-domain] Cd Length: 288 Bit Score: 137.61 E-value: 3.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 24 KVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPRRARALVALGHATEGMVERGLLELHQGRSLLQTVQDA 103
Cdd:PRK09260 3 KLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQGVARGKLTEAARQAALARLSYSLDLKAAVADA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 104 DWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAVAS 183
Cdd:PRK09260 83 DLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIRGLETSDET 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1125431683 184 VTRAQEYLRALGRMPIVLKKpVPGYVVGRIAAAVWRECIDLVLTDVIAVDDLDRAVSLG 242
Cdd:PRK09260 163 VQVAKEVAEQMGKETVVVNE-FPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLG 220
|
|
| PLN02545 |
PLN02545 |
3-hydroxybutyryl-CoA dehydrogenase |
23-242 |
1.44e-34 |
|
3-hydroxybutyryl-CoA dehydrogenase
Pssm-ID: 215300 [Multi-domain] Cd Length: 295 Bit Score: 127.92 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 23 RKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPRRARALVALGHATEGMVERGLLELHQGRSLlQTVQD 102
Cdd:PLN02545 5 KKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEADATLGRIRCTTNL-EELRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 103 ADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAVA 182
Cdd:PLN02545 84 ADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRGADTSDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 183 SVTRAQEYLRALGRMPIVlKKPVPGYVVGRIAAAVWRECIDLVLTDVIAVDDLDRAVSLG 242
Cdd:PLN02545 164 VFDATKALAERFGKTVVC-SQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLG 222
|
|
| PRK05808 |
PRK05808 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
23-242 |
4.10e-30 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 180269 [Multi-domain] Cd Length: 282 Bit Score: 115.83 E-value: 4.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 23 RKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPRRARALVALGHATEGMVERGLLELHqGRSLLQTVQD 102
Cdd:PRK05808 4 QKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAALARIT-GTTDLDDLKD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 103 ADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAVA 182
Cdd:PRK05808 83 ADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRGLATSDA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125431683 183 SVTRAQEYLRALGRMPIVLKKpVPGYVVGRIAAAVWRECIdLVLTDVIA-VDDLDRAVSLG 242
Cdd:PRK05808 163 THEAVEALAKKIGKTPVEVKN-APGFVVNRILIPMINEAI-FVLAEGVAtAEDIDEGMKLG 221
|
|
| PRK07530 |
PRK07530 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
23-242 |
7.93e-29 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181018 [Multi-domain] Cd Length: 292 Bit Score: 112.41 E-value: 7.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 23 RKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPRRARALVALGHATEGMVERGLLELhQGRSLLQTVQD 102
Cdd:PRK07530 5 KKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLARQVAKGKISEEARAAALARI-STATDLEDLAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 103 ADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAVA 182
Cdd:PRK07530 84 CDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIRGIATDEA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 183 SVTRAQEYLRALGRMPIVlKKPVPGYVVGRIAAAVWRECIDLVLTDVIAVDDLDRAVSLG 242
Cdd:PRK07530 164 TFEAAKEFVTKLGKTITV-AEDFPAFIVNRILLPMINEAIYTLYEGVGSVEAIDTAMKLG 222
|
|
| PRK08268 |
PRK08268 |
3-hydroxy-acyl-CoA dehydrogenase; Validated |
23-238 |
1.36e-26 |
|
3-hydroxy-acyl-CoA dehydrogenase; Validated
Pssm-ID: 236211 [Multi-domain] Cd Length: 507 Bit Score: 109.55 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 23 RKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPRRARALVALGHATEGMVERGLLELHQGRSLlQTVQD 102
Cdd:PRK08268 8 ATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGKLTAEQADAALARLRPVEAL-ADLAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 103 ADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAVA 182
Cdd:PRK08268 87 CDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSGLATDPA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1125431683 183 SVTRAQEYLRALGRMPiVLKKPVPGYVVGRIAAAVWRECIDLVLTDVIAVDDLDRA 238
Cdd:PRK08268 167 VADALYALARAWGKTP-VRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAI 221
|
|
| PRK08269 |
PRK08269 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
33-251 |
2.80e-26 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181340 [Multi-domain] Cd Length: 314 Bit Score: 105.91 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 33 IGCGWAALCAAAGWPVTLFDASSRGMErAAIDVPRRARA--------LVALGHATEGMVER--GLLELHQGRSLLQTVQD 102
Cdd:PRK08269 1 MGQGIALAFAFAGHDVTLIDFKPRDAA-GWRALDAEARAeiertlaaLVALGRIDAAQADAvlARIAVVARDGAADALAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 103 ADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAVA 182
Cdd:PRK08269 80 ADLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATDPA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125431683 183 SVTRAQEYLRALGRMPIVLkKPVPGYVVGRIAAAVWRECIDLVLTDVIAVDDLDRAVSLGPALGWAAAG 251
Cdd:PRK08269 160 VVDRLAALLERIGKVPVVC-GPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRFAVLG 227
|
|
| PRK06035 |
PRK06035 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
23-259 |
4.78e-25 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 180361 [Multi-domain] Cd Length: 291 Bit Score: 102.26 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 23 RKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERA--AI-DVPRRARALVALGHATEGMVERGLLELHQGRSLlQT 99
Cdd:PRK06035 4 KVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAmeLIeSGPYGLRNLVEKGKMSEDEAKAIMARIRTSTSY-ES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 100 VQDADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGART 179
Cdd:PRK06035 83 LSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIEVVRAALT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 180 AVASVTRAQEYLRALGRMPIVLKKpVPGYVVGRIAAAVWRECIDLVLTDVIAVDDLDRAVSL------GPALGWAAAGPH 253
Cdd:PRK06035 163 SEETFNTTVELSKKIGKIPIEVAD-VPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLafgfpmGPFELMDIIGID 241
|
....*.
gi 1125431683 254 LTYHLA 259
Cdd:PRK06035 242 TVYHIA 247
|
|
| PRK08293 |
PRK08293 |
3-hydroxyacyl-CoA dehydrogenase; |
23-243 |
3.94e-24 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 181359 [Multi-domain] Cd Length: 287 Bit Score: 99.63 E-value: 3.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 23 RKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPRRARALVALGHAT-EGMVERGLLELHQGRSLLQTVQ 101
Cdd:PRK08293 4 KNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIAKLADRYVRDLEATkEAPAEAALNRITLTTDLAEAVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 102 DADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPGARTAV 181
Cdd:PRK08293 84 DADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGHPGTDP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125431683 182 ASVTRAQEYLRALGRMPIVLKKPVPGYV-----VGRIAAAvwrecIDLVLTDVIAVDDLDRA------VSLGP 243
Cdd:PRK08293 164 EVFDTVVAFAKAIGMVPIVLKKEQPGYIlnsllVPFLSAA-----LALWAKGVADPETIDKTwmiatgAPMGP 231
|
|
| PRK07819 |
PRK07819 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
23-244 |
4.51e-19 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181133 [Multi-domain] Cd Length: 286 Bit Score: 85.81 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 23 RKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAaidvprRARALVALGHATE-GMVERGLLELHQGR----SLL 97
Cdd:PRK07819 6 QRVGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAG------RNRIEKSLERAVSrGKLTERERDAALARlrftTDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 98 QTVQDADWVIEAIHEELGAKQKLFHAIEEVAG-PETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVPG 176
Cdd:PRK07819 80 GDFADRQLVIEAVVEDEAVKTEIFAELDKVVTdPDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125431683 177 ARTAVASVTRAQEYLRAlgrmpiVLKKPV------PGYVVGRIAAAVWRECIDLVLTDVIAVDDLDRAVSLGPA 244
Cdd:PRK07819 160 LVTSEATVARAEEFASD------VLGKQVvraqdrSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCA 227
|
|
| fadJ |
PRK11154 |
fatty acid oxidation complex subunit alpha FadJ; |
23-238 |
5.67e-16 |
|
fatty acid oxidation complex subunit alpha FadJ;
Pssm-ID: 236864 [Multi-domain] Cd Length: 708 Bit Score: 78.78 E-value: 5.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 23 RKVAVIGAGDIGCGWAALCAA-AGWPVTLFDASSRGMERA------AIDVPRRARALVALghategmvER-GLLELHQGR 94
Cdd:PRK11154 310 NKVGVLGGGLMGGGIAYVTATkAGLPVRIKDINPQGINHAlkyswdLLDKKVKRRHLKPS--------ERdKQMALISGT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 95 SLLQTVQDADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELV 174
Cdd:PRK11154 382 TDYRGFKHADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMPLVEVI 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125431683 175 PGARTAVASVTRAQEYLRALGRMPIVLKKPvPGYVVGRIAAAVWRECIDLVLTDViAVDDLDRA 238
Cdd:PRK11154 462 PHAKTSAETIATTVALAKKQGKTPIVVRDG-AGFYVNRILAPYINEAARLLLEGE-PIEHIDAA 523
|
|
| fadB |
PRK11730 |
fatty acid oxidation complex subunit alpha FadB; |
22-213 |
1.08e-13 |
|
fatty acid oxidation complex subunit alpha FadB;
Pssm-ID: 183293 [Multi-domain] Cd Length: 715 Bit Score: 71.82 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 22 PRKVAVIGAGDIGCGWAALCAAAGWPVTLFD----ASSRGMERAAidvprrarALVAlghateGMVERGLLELHQGRSLL 97
Cdd:PRK11730 313 VKQAAVLGAGIMGGGIAYQSASKGVPVIMKDinqkALDLGMTEAA--------KLLN------KQVERGKIDGAKMAGVL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 98 QTVQ---------DADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLI 168
Cdd:PRK11730 379 SSIRptldyagfeRVDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRM 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1125431683 169 PLVELVPGARTAVASVTRAQEYLRALGRMPIVLKKpVPGYVVGRI 213
Cdd:PRK11730 459 PLVEVIRGEKTSDETIATVVAYASKMGKTPIVVND-CPGFFVNRV 502
|
|
| fa_ox_alpha_mit |
TIGR02441 |
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ... |
23-237 |
1.38e-13 |
|
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: 71.41 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 23 RKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMERAAIDVPR------RARALVALghategmvERGLLELHQGRSL 96
Cdd:TIGR02441 336 KTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKglnkkvKRKKITSL--------ERDSILSNLTPTL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 97 -LQTVQDADWVIEAIHEELGAKQKLFHAIEEVAGPETLVTSSSSGIPPTELFSRCRRQDRCLVAHPLNPPQLIPLVELVP 175
Cdd:TIGR02441 408 dYSGFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIIT 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125431683 176 GARTAVASVTRAQEYLRALGRMPIVLKKpVPGYVVGRIAAAVWRECIDLvLTDVIAVDDLDR 237
Cdd:TIGR02441 488 HDGTSKDTLASAVAVGLKQGKVVIVVKD-GPGFYTTRCLGPMLAEVIRL-LQEGVDPKKLDK 547
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
18-113 |
3.00e-05 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 45.51 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125431683 18 LIALPRKVAVIGAGDIGCGWAALCAAAGWPVTLFDASSRGMeraaidvPRRARALVALghATEGMVERGlLELHQGRSLL 97
Cdd:PRK07251 153 LETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTIL-------PREEPSVAAL--AKQYMEEDG-ITFLLNAHTT 222
|
90
....*....|....*.
gi 1125431683 98 QTVQDADWVIEAIHEE 113
Cdd:PRK07251 223 EVKNDGDQVLVVTEDE 238
|
|
| 3HCDH |
pfam00725 |
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ... |
207-258 |
2.42e-04 |
|
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: 39.51 E-value: 2.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1125431683 207 GYVVGRIAAAVWRECIDLVLTDVIAVDDLDRAVSLGPALGWAAAGPHLTYHL 258
Cdd:pfam00725 1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGL 52
|
|
| ApbA |
pfam02558 |
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ... |
25-63 |
1.64e-03 |
|
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.
Pssm-ID: 426831 [Multi-domain] Cd Length: 147 Bit Score: 38.37 E-value: 1.64e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1125431683 25 VAVIGAGDIGCGWAALCAAAGWPVTLFDassRGMERAAI 63
Cdd:pfam02558 1 IAILGAGAIGSLLGARLAKAGHDVTLIL---RGAELAAI 36
|
|
| PRK06522 |
PRK06522 |
2-dehydropantoate 2-reductase; Reviewed |
24-52 |
3.81e-03 |
|
2-dehydropantoate 2-reductase; Reviewed
Pssm-ID: 235821 [Multi-domain] Cd Length: 304 Bit Score: 38.68 E-value: 3.81e-03
10 20
....*....|....*....|....*....
gi 1125431683 24 KVAVIGAGDIGCGWAALCAAAGWPVTLFD 52
Cdd:PRK06522 2 KIAILGAGAIGGLFGAALAQAGHDVTLVA 30
|
|
| PanE |
COG1893 |
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ... |
24-52 |
5.16e-03 |
|
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 441497 [Multi-domain] Cd Length: 305 Bit Score: 38.30 E-value: 5.16e-03
10 20
....*....|....*....|....*....
gi 1125431683 24 KVAVIGAGDIGCGWAALCAAAGWPVTLFD 52
Cdd:COG1893 2 KIAILGAGAIGGLLGARLARAGHDVTLVA 30
|
|
|