|
Name |
Accession |
Description |
Interval |
E-value |
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
27-313 |
1.30e-136 |
|
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: 387.93 E-value: 1.30e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnpkagdEFVEKTLSTIATSTD 105
Cdd:COG1250 2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKlVKKGKLTE------EEADAALARITPTTD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 106 AASVVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:COG1250 76 LAALADA-DLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:COG1250 155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1483511 266 GLDTTKFIVDGWHEmDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:COG1250 235 GLDTALAVLEVLYE-ALGDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
|
|
| PLN02545 |
PLN02545 |
3-hydroxybutyryl-CoA dehydrogenase |
27-313 |
9.74e-111 |
|
3-hydroxybutyryl-CoA dehydrogenase
Pssm-ID: 215300 [Multi-domain] Cd Length: 295 Bit Score: 323.22 E-value: 9.74e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSTIATSTDA 106
Cdd:PLN02545 4 IKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKG-----KMSQEEADATLGRIRCTTNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 107 ASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PLN02545 79 EEL-RDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PLN02545 158 ADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIG 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1483511 267 LDTTKFIVDGWHEMDAENPlHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PLN02545 238 LDTCLSIMKVLHEGLGDSK-YRPCPLLVQYVDAGRLGRKSGRGVYHY 283
|
|
| 3HCDH_N |
pfam02737 |
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ... |
29-214 |
3.91e-77 |
|
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.
Pssm-ID: 397037 [Multi-domain] Cd Length: 180 Bit Score: 233.20 E-value: 3.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSTIATSTDAAS 108
Cdd:pfam02737 1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKG-----RITEEEVDAALARISFTTDLAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 109 VVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPM 188
Cdd:pfam02737 76 AVDA-DLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEK 154
|
170 180
....*....|....*....|....*.
gi 1483511 189 TSQKTFESLVDFSKALGKHPVSCKDT 214
Cdd:pfam02737 155 TSPETVATTVELAKKIGKTPVVVKDT 180
|
|
| fa_ox_alpha_mit |
TIGR02441 |
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ... |
27-313 |
2.91e-51 |
|
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: 180.03 E-value: 2.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKagdefvEKTLSTIATSTD 105
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLnKKVKRKKITSLER------DSILSNLTPTLD 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 106 AaSVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:TIGR02441 409 Y-SGFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIIT 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERG-DASKEDidtAMKLGAGYPMGPFELLDY 264
Cdd:TIGR02441 488 HDGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGvDPKKLD---KLTTKFGFPVGAATLADE 564
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1483511 265 VGLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:TIGR02441 565 VGVDVAEHVAEDLGKAFGERFGGGSAELLSELVKAGFLGRKSGKGIFIY 613
|
|
| Zn_ADH9 |
cd08269 |
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ... |
28-120 |
1.86e-04 |
|
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.
Pssm-ID: 176230 [Multi-domain] Cd Length: 312 Bit Score: 42.34 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 28 KHVTVIGGGLMGAGIAQVAAATG-HTVVLVDqtedilakskkgIEESLRKVAKKKFAENPKAGDEfvEKTLSTIATSTDA 106
Cdd:cd08269 131 KTVAVIGAGFIGLLFLQLAAAAGaRRVIAID------------RRPARLALARELGATEVVTDDS--EAIVERVRELTGG 196
|
90
....*....|....
gi 1483511 107 ASVvhstDLVVEAI 120
Cdd:cd08269 197 AGA----DVVIEAV 206
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
27-313 |
1.30e-136 |
|
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: 387.93 E-value: 1.30e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAEnpkagdEFVEKTLSTIATSTD 105
Cdd:COG1250 2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKlVKKGKLTE------EEADAALARITPTTD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 106 AASVVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:COG1250 76 LAALADA-DLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:COG1250 155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1483511 266 GLDTTKFIVDGWHEmDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:COG1250 235 GLDTALAVLEVLYE-ALGDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
|
|
| PLN02545 |
PLN02545 |
3-hydroxybutyryl-CoA dehydrogenase |
27-313 |
9.74e-111 |
|
3-hydroxybutyryl-CoA dehydrogenase
Pssm-ID: 215300 [Multi-domain] Cd Length: 295 Bit Score: 323.22 E-value: 9.74e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSTIATSTDA 106
Cdd:PLN02545 4 IKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKG-----KMSQEEADATLGRIRCTTNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 107 ASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PLN02545 79 EEL-RDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PLN02545 158 ADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIG 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1483511 267 LDTTKFIVDGWHEMDAENPlHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PLN02545 238 LDTCLSIMKVLHEGLGDSK-YRPCPLLVQYVDAGRLGRKSGRGVYHY 283
|
|
| PRK05808 |
PRK05808 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
27-313 |
6.73e-103 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 180269 [Multi-domain] Cd Length: 282 Bit Score: 302.65 E-value: 6.73e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKagdefvEKTLSTIATSTD 105
Cdd:PRK05808 3 IQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLdRLVKKGKMTEADK------EAALARITGTTD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 106 AASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:PRK05808 77 LDDL-KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:PRK05808 156 GLATSDATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLI 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1483511 266 GLDTTKFIVDGWHEmDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK05808 236 GLDTCLAIMEVLYE-GFGDSKYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
|
|
| PRK07819 |
PRK07819 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
30-313 |
4.41e-100 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181133 [Multi-domain] Cd Length: 286 Bit Score: 295.74 E-value: 4.41e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 30 VTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKagdefvEKTLSTIATSTDAAS 108
Cdd:PRK07819 8 VGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLeRAVSRGKLTERER------DAALARLRFTTDLGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 109 VVhSTDLVVEAIVENLKVKNELFKRLDKFAAE-HTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTP 187
Cdd:PRK07819 82 FA-DRQLVIEAVVEDEAVKTEIFAELDKVVTDpDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 188 MTSQKTFESLVDF-SKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PRK07819 161 VTSEATVARAEEFaSDVLGKQVVRAQDRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPMGPLRLSDLVG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1483511 267 LDTTKFIVDGWHEMDAEnPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK07819 241 LDTVKAIADSMYEEFKE-PLYAPPPLLLRMVEAGLLGKKSGRGFYTY 286
|
|
| PRK08268 |
PRK08268 |
3-hydroxy-acyl-CoA dehydrogenase; Validated |
27-313 |
6.05e-99 |
|
3-hydroxy-acyl-CoA dehydrogenase; Validated
Pssm-ID: 236211 [Multi-domain] Cd Length: 507 Bit Score: 300.22 E-value: 6.05e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSTIATSTDA 106
Cdd:PRK08268 7 IATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKG-----KLTAEQADAALARLRPVEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 107 ASVVhSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PRK08268 82 ADLA-DCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 187 PMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVG 266
Cdd:PRK08268 161 LATDPAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFELMDLIG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1483511 267 LD----TTKFIVDGWHemdaENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK08268 241 LDvnhaVMESVYRQFY----QEPRFRPSLIQQELVAAGRLGRKSGQGFYRY 287
|
|
| PRK07530 |
PRK07530 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
27-314 |
1.50e-92 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181018 [Multi-domain] Cd Length: 292 Bit Score: 276.89 E-value: 1.50e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKAgdefveKTLSTIATSTD 105
Cdd:PRK07530 4 IKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLaRQVAKGKISEEARA------AALARISTATD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 106 AASVVhSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:PRK07530 78 LEDLA-DCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAI-RLYErGDASKEDIDTAMKLGAGYPMGPFELLDY 264
Cdd:PRK07530 157 GIATDEATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIyTLYE-GVGSVEAIDTAMKLGANHPMGPLELADF 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1483511 265 VGLDTTKFIVDGWHEMDAENPlHQPSPSLNKLVAENKFGKKTGEGFYKYK 314
Cdd:PRK07530 236 IGLDTCLSIMQVLHDGLADSK-YRPCPLLVKYVEAGWLGRKTGRGFYDYR 284
|
|
| PRK08293 |
PRK08293 |
3-hydroxyacyl-CoA dehydrogenase; |
27-314 |
1.86e-79 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 181359 [Multi-domain] Cd Length: 287 Bit Score: 243.31 E-value: 1.86e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEeslrKVAKKKFAENPKAGDEFVEKTLSTIATSTDA 106
Cdd:PRK08293 3 IKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIA----KLADRYVRDLEATKEAPAEAALNRITLTTDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 107 ASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PRK08293 79 AEAVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 187 PMTSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:PRK08293 159 PGTDPEVFDTVVAFAKAIGMVPIVLkKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1483511 266 GLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKYK 314
Cdd:PRK08293 239 GLDTAYNITSNWAEATDDENAKKAAALLKEYIDKGKLGVATGEGFYNYP 287
|
|
| PRK06035 |
PRK06035 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
27-305 |
2.40e-79 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 180361 [Multi-domain] Cd Length: 291 Bit Score: 243.24 E-value: 2.40e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEES---LRKVAKK-KFAENPkagdefVEKTLSTIAT 102
Cdd:PRK06035 3 IKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGpygLRNLVEKgKMSEDE------AKAIMARIRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 103 STDAASVvHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVE 182
Cdd:PRK06035 77 STSYESL-SDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 183 VIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELL 262
Cdd:PRK06035 156 VVRAALTSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFELM 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1483511 263 DYVGLDTTKFIVDGWHEmDAENPLHQPSPSLNKLVAENKFGKK 305
Cdd:PRK06035 236 DIIGIDTVYHIAEYLYE-ETGDPQFIPPNSLKQMVLNGYVGDK 277
|
|
| PRK09260 |
PRK09260 |
3-hydroxyacyl-CoA dehydrogenase; |
27-313 |
1.37e-77 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 236434 [Multi-domain] Cd Length: 288 Bit Score: 238.54 E-value: 1.37e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRK-VAKKKFAENPKAgdefveKTLSTIATSTD 105
Cdd:PRK09260 1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQgVARGKLTEAARQ------AALARLSYSLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 106 AASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:PRK09260 75 LKAAVADADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYV 265
Cdd:PRK09260 155 GLETSDETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLELGDLV 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1483511 266 GLDTTKFIVDGWHEMDAENplHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK09260 235 GLDTRLNNLKYLHETLGEK--YRPAPLLEKYVKAGRLGRKTGRGVYDY 280
|
|
| 3HCDH_N |
pfam02737 |
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ... |
29-214 |
3.91e-77 |
|
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.
Pssm-ID: 397037 [Multi-domain] Cd Length: 180 Bit Score: 233.20 E-value: 3.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKfaenpKAGDEFVEKTLSTIATSTDAAS 108
Cdd:pfam02737 1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKG-----RITEEEVDAALARISFTTDLAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 109 VVHStDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPM 188
Cdd:pfam02737 76 AVDA-DLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEK 154
|
170 180
....*....|....*....|....*.
gi 1483511 189 TSQKTFESLVDFSKALGKHPVSCKDT 214
Cdd:pfam02737 155 TSPETVATTVELAKKIGKTPVVVKDT 180
|
|
| PRK06130 |
PRK06130 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
27-313 |
2.22e-72 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 235707 [Multi-domain] Cd Length: 311 Bit Score: 225.81 E-value: 2.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKkfaenpkagdEFVEKTLSTIATSTDA 106
Cdd:PRK06130 4 IQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPL----------GIASAGMGRIRMEAGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 107 ASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PRK06130 74 AAAVSGADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 187 PMTSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPM---GPFELL 262
Cdd:PRK06130 154 DKTSPQTVATTMALLRSIGKRPVLVkKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1483511 263 DYVGLDTTKFIVDGWHEmDAENPLhQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK06130 234 DMNGLDVHLAVASYLYQ-DLENRT-TPSPLLEEKVEAGELGAKSGQGFYAW 282
|
|
| fadJ |
PRK11154 |
fatty acid oxidation complex subunit alpha FadJ; |
27-314 |
4.60e-65 |
|
fatty acid oxidation complex subunit alpha FadJ;
Pssm-ID: 236864 [Multi-domain] Cd Length: 708 Bit Score: 217.07 E-value: 4.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVdqtEDIlakSKKGIEESLR-------KVAKKKFAenpKAGDEfvEKTLST 99
Cdd:PRK11154 309 VNKVGVLGGGLMGGGIAYVTATKAGLPVRI---KDI---NPQGINHALKyswdlldKKVKRRHL---KPSER--DKQMAL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 100 IATSTDAaSVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMK 179
Cdd:PRK11154 378 ISGTTDY-RGFKHADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMP 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 180 LVEVIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGdASKEDIDTAMkLGAGYPMGPF 259
Cdd:PRK11154 457 LVEVIPHAKTSAETIATTVALAKKQGKTPIVVRDGAGFYVNRILAPYINEAARLLLEG-EPIEHIDAAL-VKFGFPVGPI 534
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1483511 260 ELLDYVGLDT-TKFIvdgwHEMDAE-NPLHQPSPSLNKLVAENKFGKKTGEGFYKYK 314
Cdd:PRK11154 535 TLLDEVGIDVgTKII----PILEAAlGERFSAPAAFDKLLNDDRKGRKNGRGFYLYG 587
|
|
| fadB |
PRK11730 |
fatty acid oxidation complex subunit alpha FadB; |
27-314 |
8.36e-61 |
|
fatty acid oxidation complex subunit alpha FadB;
Pssm-ID: 183293 [Multi-domain] Cd Length: 715 Bit Score: 205.87 E-value: 8.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKskkGIEES---LRKVAKKKFAENPKAGdefveKTLSTIATS 103
Cdd:PRK11730 313 VKQAAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALDL---GMTEAaklLNKQVERGKIDGAKMA-----GVLSSIRPT 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 104 TDAASVVHsTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEV 183
Cdd:PRK11730 385 LDYAGFER-VDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEV 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 184 IKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGdASKEDIDTAMKLGAGYPMGPFELLD 263
Cdd:PRK11730 464 IRGEKTSDETIATVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDG-ADFRQIDKVMEKQFGWPMGPAYLLD 542
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1483511 264 YVGLDT----TKFIVDGWHE-MDAENPlhqpsPSLNKLVAENKFGKKTGEGFYKYK 314
Cdd:PRK11730 543 VVGIDTahhaQAVMAEGFPDrMKKDYR-----DAIDVLFEAKRFGQKNGKGFYRYE 593
|
|
| fa_ox_alpha_mit |
TIGR02441 |
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ... |
27-313 |
2.91e-51 |
|
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: 180.03 E-value: 2.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESL-RKVAKKKFAENPKagdefvEKTLSTIATSTD 105
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLnKKVKRKKITSLER------DSILSNLTPTLD 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 106 AaSVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIK 185
Cdd:TIGR02441 409 Y-SGFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIIT 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 186 TPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERG-DASKEDidtAMKLGAGYPMGPFELLDY 264
Cdd:TIGR02441 488 HDGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGvDPKKLD---KLTTKFGFPVGAATLADE 564
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1483511 265 VGLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:TIGR02441 565 VGVDVAEHVAEDLGKAFGERFGGGSAELLSELVKAGFLGRKSGKGIFIY 613
|
|
| 3HCDH |
pfam00725 |
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ... |
216-313 |
2.15e-44 |
|
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: 146.59 E-value: 2.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 216 GFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFIVDGWHEmDAENPLHQPSPSLNK 295
Cdd:pfam00725 1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEVLAE-EFGDRAYRPPPLLEK 79
|
90
....*....|....*...
gi 1483511 296 LVAENKFGKKTGEGFYKY 313
Cdd:pfam00725 80 LVEAGRLGRKTGKGFYKY 97
|
|
| PRK08269 |
PRK08269 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
38-313 |
1.09e-42 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181340 [Multi-domain] Cd Length: 314 Bit Score: 149.44 E-value: 1.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 38 MGAGIAQVAAATGHTVVLVD-------QTEDILAKSKKGIEESLRKVAKKKFAENPKAgDEFVEKTlsTIATSTDAASVV 110
Cdd:PRK08269 1 MGQGIALAFAFAGHDVTLIDfkprdaaGWRALDAEARAEIERTLAALVALGRIDAAQA-DAVLARI--AVVARDGAADAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 111 HSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPMTS 190
Cdd:PRK08269 78 ADADLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 191 QKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYP---MGPFELLDYVGL 267
Cdd:PRK08269 158 PAVVDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRfavLGLLEFIDWGGC 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1483511 268 DT----TKFIVDgwhEMDAENplHQPSPSLNKLVAENKFGKKTGEGFYKY 313
Cdd:PRK08269 238 DIlyyaSRYLAG---EIGPDR--FAPPAIVVRNMEEGRDGLRTGAGFYDY 282
|
|
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
29-263 |
3.02e-41 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 145.19 E-value: 3.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLrkvakKKFAENPKAGDEFVEKTLSTIATSTDAAS 108
Cdd:PRK06129 4 SVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRL-----EDLAAFDLLDGEAPDAVLARIRVTDSLAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 109 VVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPM 188
Cdd:PRK06129 79 AVADADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPW 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1483511 189 TSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYP---MGPFELLD 263
Cdd:PRK06129 159 TAPATLARAEALYRAAGQSPVRLrREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGLRwsfMGPFETID 237
|
|
| PRK07066 |
PRK07066 |
L-carnitine dehydrogenase; |
27-259 |
9.97e-22 |
|
L-carnitine dehydrogenase;
Pssm-ID: 168796 [Multi-domain] Cd Length: 321 Bit Score: 93.36 E-value: 9.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 27 VKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKFAenPKAGDEfvekTLSTIATstdA 106
Cdd:PRK07066 7 IKTFAAIGSGVIGSGWVARALAHGLDVVAWDPAPGAEAALRANVANAWPALERQGLA--PGASPA----RLRFVAT---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 107 ASVVHSTDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKT 186
Cdd:PRK07066 78 EACVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLGG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1483511 187 PMTSQKTFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYP---MGPF 259
Cdd:PRK07066 158 ERTAPEAVDAAMGIYRALGMRPLHVrKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRwsfMGTF 234
|
|
| PRK07531 |
PRK07531 |
carnitine 3-dehydrogenase; |
33-260 |
2.58e-15 |
|
carnitine 3-dehydrogenase;
Pssm-ID: 236044 [Multi-domain] Cd Length: 495 Bit Score: 75.93 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 33 IGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKSKKGIEESLRKVAKKKFAENPKAGdefvekTLSTIATSTDAasvVHS 112
Cdd:PRK07531 10 IGGGVIGGGWAARFLLAGIDVAVFDPHPEAERIIGEVLANAERAYAMLTDAPLPPEG------RLTFCASLAEA---VAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 113 TDLVVEAIVENLKVKNELFKRLDKFAAEHTIFASNTSSLHITSIANATTRQDRFAGLHFFNPVPVMKLVEVIKTPMTSQK 192
Cdd:PRK07531 81 ADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLVELVGGGKTSPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1483511 193 TFESLVDFSKALGKHPVSC-KDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGY---PMGPFE 260
Cdd:PRK07531 161 TIRRAKEILREIGMKPVHIaKEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDVIRYSFGLrwaQMGLFE 232
|
|
| PRK08268 |
PRK08268 |
3-hydroxy-acyl-CoA dehydrogenase; Validated |
188-298 |
1.50e-10 |
|
3-hydroxy-acyl-CoA dehydrogenase; Validated
Pssm-ID: 236211 [Multi-domain] Cd Length: 507 Bit Score: 61.79 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 188 MTSQKTFESLVD----FSKALGKhPVS-CKDTPGFIVNRLLVPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELL 262
Cdd:PRK08268 384 MAAPATSPAARDaahaLFQQDGK-AVSvIRDSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPLGPLAWG 462
|
90 100 110
....*....|....*....|....*....|....*.
gi 1483511 263 DYVGLDTTKFIVDGWHEMDAEnPLHQPSPSLNKLVA 298
Cdd:PRK08268 463 DRLGAARILRVLENLQALYGD-PRYRPSPWLRRRAA 497
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
29-62 |
7.26e-05 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 43.93 E-value: 7.26e-05
10 20 30
....*....|....*....|....*....|....
gi 1483511 29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDI 62
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDP 34
|
|
| Zn_ADH9 |
cd08269 |
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ... |
28-120 |
1.86e-04 |
|
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.
Pssm-ID: 176230 [Multi-domain] Cd Length: 312 Bit Score: 42.34 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 28 KHVTVIGGGLMGAGIAQVAAATG-HTVVLVDqtedilakskkgIEESLRKVAKKKFAENPKAGDEfvEKTLSTIATSTDA 106
Cdd:cd08269 131 KTVAVIGAGFIGLLFLQLAAAAGaRRVIAID------------RRPARLALARELGATEVVTDDS--EAIVERVRELTGG 196
|
90
....*....|....
gi 1483511 107 ASVvhstDLVVEAI 120
Cdd:cd08269 197 AGA----DVVIEAV 206
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
23-65 |
1.07e-03 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 40.05 E-value: 1.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1483511 23 KKIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAK 65
Cdd:COG0569 91 IKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVER 133
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
29-58 |
1.10e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 40.27 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|
gi 1483511 29 HVTVIGGGLMGAGIAQVAAATGHTVVLVDQ 58
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLER 33
|
|
| PRK13369 |
PRK13369 |
glycerol-3-phosphate dehydrogenase; Provisional |
32-58 |
1.44e-03 |
|
glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237365 [Multi-domain] Cd Length: 502 Bit Score: 39.95 E-value: 1.44e-03
10 20
....*....|....*....|....*..
gi 1483511 32 VIGGGLMGAGIAQVAAATGHTVVLVDQ 58
Cdd:PRK13369 11 VIGGGINGAGIARDAAGRGLKVLLCEK 37
|
|
| GpsA |
COG0240 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
28-120 |
8.15e-03 |
|
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440010 [Multi-domain] Cd Length: 327 Bit Score: 37.32 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483511 28 KHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDILAKskkgIEESlRkvakkkfaENPK--AGDEFVEktlsTIATSTD 105
Cdd:COG0240 1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEE----INET-R--------ENPRylPGVKLPE----NLRATSD 63
|
90
....*....|....*
gi 1483511 106 AASVVHSTDLVVEAI 120
Cdd:COG0240 64 LEEALAGADLVLLAV 78
|
|
| COG2085 |
COG2085 |
Predicted dinucleotide-binding enzyme [General function prediction only]; |
30-55 |
9.54e-03 |
|
Predicted dinucleotide-binding enzyme [General function prediction only];
Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 36.69 E-value: 9.54e-03
10 20
....*....|....*....|....*.
gi 1483511 30 VTVIGGGLMGAGIAQVAAATGHTVVL 55
Cdd:COG2085 1 IGIIGTGNIGSALARRLAAAGHEVVI 26
|
|
|