|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
1-380 |
0e+00 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 810.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 1 MDFRLNDEQELFVAGIRELMASENWESYFAQCDRDSMYPERFVKALADMEIDNLLIPEEHGGLNAGFITVAAVWMELGRL 80
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELMASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 81 GAPTYVLYQLPGGFNTVLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLQTTYQRRNGKVYLNGSKCFITSSA 160
Cdd:PRK03354 81 GAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 161 YTPYIVVMSRDADSPDKPVFTEWFLDMSKPGIKVNKLEKLGLRMDSCCEITFDNVELDEKDMFGREGNGFNRVKEEFDHE 240
Cdd:PRK03354 161 YTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 241 RFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDNGLITSGDAAMCKYF 320
Cdd:PRK03354 241 RFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYF 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 321 CANAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSVLKQYR 380
Cdd:PRK03354 321 CANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-380 |
2.68e-167 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 472.68 E-value: 2.68e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 1 MDFRLNDEQELFVAGIRELMASENWESYFAQCDRDSMYPERFVKALADMEIDNLLIPEEHGGLNAGFITVAAVWMELGRL 80
Cdd:PRK12341 1 MDFSLTEEQELLLASIRELITRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 81 GAPTYVLYQLPGgFNTVLREGTQEQIDKIM-AFRGTGKQMWNSAITEPGAGSDVGSLQTTYQRRNGKVYLNGSKCFITSS 159
Cdd:PRK12341 81 GAPAFLITNGQC-IHSMRRFGSAEQLRKTAeSTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 160 AYTPYIVVMSRDADSPD-KPVFTEWFLDMSKPGIKVNKLEKLGLRMDSCCEITFDNVELDEKDMFGREGNGFNRVKEEFD 238
Cdd:PRK12341 160 KEYPYMLVLARDPQPKDpKKAFTLWWVDSSKPGIKINPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 239 HERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDNGLITSGDAAMCK 318
Cdd:PRK12341 240 MERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAK 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757599289 319 YFCANAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSVLKQYR 380
Cdd:PRK12341 320 LYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDYQ 381
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-380 |
7.81e-116 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 341.82 E-value: 7.81e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 1 MDFRLNDEQELFVAGIRELmASENWESYFAQCDRDSMYPERFVKALADMEIDNLLIPEEHGGLNAGFITVAAVWMELGRL 80
Cdd:COG1960 1 MDFELTEEQRALRDEVREF-AEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 81 GAPTYVLYQLPGGF-NTVLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLQTTYQRRNGKVYLNGSKCFITSS 159
Cdd:COG1960 80 DASLALPVGVHNGAaEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 160 AYTPYIVVMSRDADSPDKPVFTEWFLDMSKPGIKVNKLE-KLGLRMDSCCEITFDNVELDEKDMFGREGNGFNRVKEEFD 238
Cdd:COG1960 160 PVADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEdKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 239 HERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDNGLITSGDAAMCK 318
Cdd:COG1960 240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757599289 319 YFCANAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSVLKQYR 380
Cdd:COG1960 320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
7-373 |
8.35e-100 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 298.81 E-value: 8.35e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 7 DEQELFVAGIRELMASENWEsYFAQCDRDSMYPERFVKALADMeidnllipeehgglnagfitvaavwmelgrlgaptyv 86
Cdd:cd00567 1 EEQRELRDSAREFAAEELEP-YARERRETPEEPWELLAELGLL------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 87 lyqlpGGFNTVLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLQTTYQRRNGKVYLNGSKCFITSSAYTPYIV 166
Cdd:cd00567 43 -----LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 167 VMSR-DADSPDKPVFTEWFLDMSKPGIKVNKLE-KLGLRMDSCCEITFDNVELDEKDMFGREGNGFNRVKEEFDHERFLV 244
Cdd:cd00567 118 VLARtDEEGPGHRGISAFLVPADTPGVTVGRIWdKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 245 ALTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDNGLI-TSGDAAMCKYFCAN 323
Cdd:cd00567 198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKLFATE 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 757599289 324 AAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGR 373
Cdd:cd00567 278 AAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
7-377 |
6.75e-72 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 229.08 E-value: 6.75e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 7 DEQELFVAGIRELmASENWESYFAQCDRDSMYPERFVKALADMEIDNLLIPEEHGGLNAGFITVAAVWMELGRLGAPTYV 86
Cdd:cd01158 1 EEHQMIRKTVRDF-AEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 87 LY--QLPGGFNTVLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLQTTYQRRNGKVYLNGSKCFITSSAYTPY 164
Cdd:cd01158 80 IVsvHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 165 IVVMSRdADSPDKPV-FTEWFLDMSKPGIKVNKLE-KLGLRMDSCCEITFDNVELDEKDMFGREGNGFNRVKEEFDHERF 242
Cdd:cd01158 160 YIVFAV-TDPSKGYRgITAFIVERDTPGLSVGKKEdKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 243 LVALTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDNGLITSGDAAMCKYFCA 322
Cdd:cd01158 239 GIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFAS 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 757599289 323 NAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSVLK 377
Cdd:cd01158 319 EVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
5-377 |
4.28e-70 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 224.60 E-value: 4.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 5 LNDEQELFVAGIRELmASENWESYFAQCDRDSMYPERFVKALADMEIDNLLIPEEHGGLNAGFITVAAVWMELGRLGAPT 84
Cdd:cd01156 2 LDDEIEMLRQSVREF-AQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 85 YVLYqlpGG-----FNTVLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLQTTYQRRNGKVYLNGSKCFITSS 159
Cdd:cd01156 81 ALSY---GAhsnlcINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 160 AYTPYIVVMSRDADSPDKPVFTEWFLDMSKPGIKV-NKLEKLGLRMDSCCEITFDNVELDEKDMFGREGNGFNRVKEEFD 238
Cdd:cd01156 158 PDADTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRaQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 239 HERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDNGLITSGDAAMCK 318
Cdd:cd01156 238 YERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVI 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 757599289 319 YFCANAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSVLK 377
Cdd:cd01156 318 LYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
2-379 |
7.21e-57 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 191.14 E-value: 7.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 2 DFRLNDEQ----ELFVAGIRELMASENWEsyfAQCDRDSMYPERFVKALADMEIDNLLIPEEHGGLNAGFITVAAVWMEL 77
Cdd:cd01161 20 PSVLTEEQteelNMLVGPVEKFFEEVNDP---AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 78 GRLGAPTYVLYQLPG-GFNTVLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLQTTYQRR-NGKVY-LNGSKC 154
Cdd:cd01161 97 GMDLGFSVTLGAHQSiGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSeDGKHYvLNGSKI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 155 FITSSAYTPYIVVMSR----DADSPDKPVFTEWFLDMSKPGIKVNKLE-KLGLRMDSCCEITFDNVELDEKDMFGREGNG 229
Cdd:cd01161 177 WITNGGIADIFTVFAKtevkDATGSVKDKITAFIVERSFGGVTNGPPEkKMGIKGSNTAEVYFEDVKIPVENVLGEVGDG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 230 FNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDNGLI 309
Cdd:cd01161 257 FKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLK 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757599289 310 T--SGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSVLKQY 379
Cdd:cd01161 337 AeyQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHA 408
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
8-376 |
6.74e-56 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 187.32 E-value: 6.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 8 EQELFVAGIRELMASEnWESYFAQCDRDSMYPERFVKALADMEIDNLLIPEEHGGLNAGFITVAAVWMELGRLG--APTY 85
Cdd:cd01160 2 EHDAFRDVVRRFFAKE-VAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGgsGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 86 VLYQLPGGfNTVLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLQTTYQRRNGKVYLNGSKCFITSSAYTPYI 165
Cdd:cd01160 81 SLHTDIVS-PYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 166 VVMSRdADSPDKPV--FTEWFLDMSKPG-IKVNKLEKLGLRMDSCCEITFDNVELDEKDMFGREGNGFNRVKEEFDHERF 242
Cdd:cd01160 160 IVVAR-TGGEARGAggISLFLVERGTPGfSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 243 LVALTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDNGLITSGDAAMCKYFCA 322
Cdd:cd01160 239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWAT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 757599289 323 NAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSVL 376
Cdd:cd01160 319 ELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
227-375 |
1.78e-51 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 168.59 E-value: 1.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 227 GNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDN 306
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757599289 307 GLITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSV 375
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
2-378 |
3.85e-50 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 173.14 E-value: 3.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 2 DFRLNDEQELFVAGIRELmASENWESYFAQCDRDSMYPE--RFVKALADMEIDNLLIPEEHGGLNAGFITVAAVWMELGR 79
Cdd:PLN02519 23 SLLFDDTQLQFKESVQQF-AQENIAPHAAAIDATNSFPKdvNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 80 LGAPTYVLYQLPGGF--NTVLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLQTTYQRRNGKVYLNGSKCFIT 157
Cdd:PLN02519 102 ASGSVGLSYGAHSNLciNQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 158 SSAYTPYIVVMSRDADSPDKPVFTEWFLDMSKPGIKV-NKLEKLGLRMDSCCEITFDNVELDEKDMFGREGNGFNRVKEE 236
Cdd:PLN02519 182 NGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTaQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 237 FDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDNGLITSGDAAM 316
Cdd:PLN02519 262 LDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAG 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757599289 317 CKYFCANAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSVLKQ 378
Cdd:PLN02519 342 VILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
5-378 |
1.52e-47 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 165.69 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 5 LNDEQELFVAGIRELMASEnWESYFAQCDRDSMYPERFVKALADMEIDNLLIPEEHGGLNAGFITVAAVWMEL--GRLGA 82
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKE-MAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALstGCVST 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 83 PTYV-LYQLPGGFntVLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLQTTYQRRNGKVYLNGSKCFITSSAY 161
Cdd:cd01162 80 AAYIsIHNMCAWM--IDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 162 TPYIVVMSRDADSPDKPVFTeWFLDMSKPGIKVNKLE-KLGLRMDSCCEITFDNVELDEKDMFGREGNGFNRVKEEFDHE 240
Cdd:cd01162 158 SDVYVVMARTGGEGPKGISC-FVVEKGTPGLSFGANEkKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 241 RFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDNGlitSGDA----AM 316
Cdd:cd01162 237 RLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRG---DPDAvklcAM 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757599289 317 CKYFCANAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSVLKQ 378
Cdd:cd01162 314 AKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
30-376 |
2.00e-46 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 162.76 E-value: 2.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 30 AQCDRDSMYPERFVKALADMEIDNLLIPEEHGGLNAGFITVAAVWMEL--GRLGAPTYV----LYQLPggfntVLREGTQ 103
Cdd:cd01157 25 AEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELayGCTGVQTAIeansLGQMP-----VIISGND 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 104 EQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLQTTYQRRNGKVYLNGSKCFITSSAYTPYIVVMSRDADSPDKP---VF 180
Cdd:cd01157 100 EQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKCPaskAF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 181 TEWFLDMSKPGIKVNKLEK-LGLRMDSCCEITFDNVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDA 259
Cdd:cd01157 180 TGFIVEADTPGIQPGRKELnMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 260 ARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDNGLITSGDAAMCKYFCANAAFEVVDSAMQVLGGV 339
Cdd:cd01157 260 TKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGN 339
|
330 340 350
....*....|....*....|....*....|....*..
gi 757599289 340 GIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSVL 376
Cdd:cd01157 340 GFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
34-375 |
1.00e-40 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 147.89 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 34 RDSMYPERFVKALADMeidNLL--IPEEHGGLNAGFITVAAVWMELGRL--GAPTYVLYQLPGGFNTVLREGTQEQIDKI 109
Cdd:cd01151 41 REEKFDRKIIEEMGEL---GLLgaTIKGYGCAGLSSVAYGLIAREVERVdsGYRSFMSVQSSLVMLPIYDFGSEEQKQKY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 110 MAFRGTGKQMWNSAITEPGAGSDVGSLQTTyQRRNGKVY-LNGSKCFITSSAYTPYIVVMSRDADSPDKPVFtewFLDMS 188
Cdd:cd01151 118 LPKLASGELIGCFGLTEPNHGSDPGGMETR-ARKDGGGYkLNGSKTWITNSPIADVFVVWARNDETGKIRGF---ILERG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 189 KPGIKVNKLE-KLGLRMDSCCEITFDNVELDEKDMFGrEGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRV 267
Cdd:cd01151 194 MKGLSAPKIQgKFSLRASITGEIVMDNVFVPEENLLP-GAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 268 QFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDNGLITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGEHRI 347
Cdd:cd01151 273 QFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHI 352
|
330 340
....*....|....*....|....*...
gi 757599289 348 ARFWRDLRVDRVSGGSDEMQILTLGRSV 375
Cdd:cd01151 353 IRHMVNLESVNTYEGTHDIHALILGRAI 380
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
38-371 |
2.52e-38 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 141.76 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 38 YPERFVKAL---ADMEIDNLLIPEEHGGLNAGFITVAAVWMELGRLGAPTYVLYQLPGGFNTVLREGTQEQIDKIMAFRG 114
Cdd:cd01153 34 VPPPFKEALdafAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQGAAATLLAHGTEAQREKWIPRLA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 115 TGKQMWNSAITEPGAGSDVGSLQT--TYQRrNGKVYLNGSKCFITS--SAYTPYIV--VMSRDADSPDKPVFTEWFL--- 185
Cdd:cd01153 114 EGEWTGTMCLTEPDAGSDLGALRTkaVYQA-DGSWRINGVKRFISAgeHDMSENIVhlVLARSEGAPPGVKGLSLFLvpk 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 186 ---DMSKPGIKVNKLE-KLGLRMDSCCEITFDNVEldeKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAAR 261
Cdd:cd01153 193 fldDGERNGVTVARIEeKMGLHGSPTCELVFDNAK---GELIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 262 YANQRVQFGE--------AIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSD--NGLITSGDAA------------MCKY 319
Cdd:cd01153 270 YAKERKQGGDlikaapavTIIHHPDVRRSLMTQKAYAEGSRALDLYTATVQDlaERKATEGEDRkalsaladlltpVVKG 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 757599289 320 FCANAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTL 371
Cdd:cd01153 350 FGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALDL 401
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
21-380 |
5.29e-37 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 138.53 E-value: 5.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 21 ASENWESYFAQCDRDSMYPERFVKALADMEIDNLLIPEEHGGlnAGFITVAAVWM--ELGRLGaPTYVLYQLPGGF---N 95
Cdd:PTZ00461 52 SREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGG--AGMDAVAAVIIhhELSKYD-PGFCLAYLAHSMlfvN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 96 TVLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLQTTYQR-RNGKVYLNGSKCFITSSAYTPYIVVMSRdADS 174
Cdd:PTZ00461 129 NFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKdSNGNYVLNGSKIWITNGTVADVFLIYAK-VDG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 175 PdkpvFTEWFLDMSKPGIKVN-KLEKLGLRMDSCCEITFDNVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAM 253
Cdd:PTZ00461 208 K----ITAFVVERGTKGFTQGpKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 254 CAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWK--SDNGLITSGDAAmcKYFCANAAFEVVDS 331
Cdd:PTZ00461 284 RSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNvhPGNKNRLGSDAA--KLFATPIAKKVADS 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 757599289 332 AMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSVLKQYR 380
Cdd:PTZ00461 362 AIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKGLK 410
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
7-376 |
1.84e-33 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 128.23 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 7 DEQELFVAGIRELMAS----ENWESYFAQCDRDSMYPERFVKALADMEIDNLLIPEEHGGLNAGFITVAAVWMELGRLGA 82
Cdd:cd01152 1 PSEEAFRAEVRAWLAAhlppELREESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 83 PTYVLY---QLPGgfNTVLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLQTTyQRRNGKVY-LNGSKCFITS 158
Cdd:cd01152 81 PVPFNQigiDLAG--PTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTR-AVRDGDDWvVNGQKIWTSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 159 SAYTPYIVVMSR-DADSPDKPVFTEWFLDMSKPGIKVNKLEKLGLRMDScCEITFDNVELDEKDMFGREGNGFNRVKEEF 237
Cdd:cd01152 158 AHYADWAWLLVRtDPEAPKHRGISILLVDMDSPGVTVRPIRSINGGEFF-NEVFLDDVRVPDANRVGEVNDGWKVAMTTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 238 DHERflvaLTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDNGLITSGDAAMC 317
Cdd:cd01152 237 NFER----VSIGGSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIA 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757599289 318 KYFCANAAFEVVDSAMQVLG--------GVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSVL 376
Cdd:cd01152 313 KLFGSELAQELAELALELLGtaallrdpAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAERLL 379
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
68-375 |
1.93e-30 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 120.34 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 68 ITVAAVWM-ELGRLGAP--TYVLYQLPGGFNTVLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLQTTYQRRN 144
Cdd:PLN02526 89 ITASAIATaEVARVDAScsTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 145 GKVYLNGSKCFITSSAYTPYIVVMSRDADSPDKPVFtewFLDMSKPGIKVNKLE-KLGLRMDSCCEITFDNVELDEKDMF 223
Cdd:PLN02526 169 GGWILNGQKRWIGNSTFADVLVIFARNTTTNQINGF---IVKKGAPGLKATKIEnKIGLRMVQNGDIVLKDVFVPDEDRL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 224 grEG-NGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNM------ 296
Cdd:PLN02526 246 --PGvNSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVgwrlck 323
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757599289 297 LYETawksdnGLITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSV 375
Cdd:PLN02526 324 LYES------GKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
53-377 |
1.80e-26 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 109.02 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 53 NLLIPEEHGGLNAGFITVAAVWMELGR-LGAPTYVLYQLP--GGFNTVLREGTQEQIDKIMAFRGTGKQMWNSAITEPG- 128
Cdd:cd01155 57 NLFLPEVSGLSGLTNLEYAYLAEETGRsFFAPEVFNCQAPdtGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDv 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 129 AGSDVGSLQTTYQRRNGKVYLNGSKCFiTSSAYTP----YIVVMSRDADSPDK-PVFTEWFLDMSKPGIKVnkleklgLR 203
Cdd:cd01155 137 ASSDATNIECSIERDGDDYVINGRKWW-SSGAGDPrckiAIVMGRTDPDGAPRhRQQSMILVPMDTPGVTI-------IR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 204 MDSC----------CEITFDNVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAI 273
Cdd:cd01155 209 PLSVfgyddaphghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 274 GRYQLIQEKFAHMAIKLNSMRNMLYETAWKSDngliTSGDA------AMCKYFCANAAFEVVDSAMQVLGGVGIAGEHRI 347
Cdd:cd01155 289 AQHGVVAHWIAKSRIEIEQARLLVLKAAHMID----TVGNKaarkeiAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPL 364
|
330 340 350
....*....|....*....|....*....|
gi 757599289 348 ARFWRDLRVDRVSGGSDEMQILTLGRSVLK 377
Cdd:cd01155 365 ANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
123-213 |
1.09e-23 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 93.88 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 123 AITEPGAGSDVGSLQTTYQRRNGKVY-LNGSKCFITSSAYTPYIVVMSRDADSPDKPVFTEWFLDMSKPGIKVNKL-EKL 200
Cdd:pfam02770 3 ALTEPGAGSDVASLKTTAADGDGGGWvLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIeTKL 82
|
90
....*....|...
gi 757599289 201 GLRMDSCCEITFD 213
Cdd:pfam02770 83 GVRGLPTGELVFD 95
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
119-369 |
8.27e-22 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 95.90 E-value: 8.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 119 MWnsaITEPGAGSDVGSLQTTYQRRNGKVY-LNGSKCFiTSSAYTPYIVVMSRDADSPDKPVFTEWFL------DMSKPG 191
Cdd:cd01154 151 TW---MTEKQGGSDLGANETTAERSGGGVYrLNGHKWF-ASAPLADAALVLARPEGAPAGARGLSLFLvprlleDGTRNG 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 192 IKVNKL-EKLGLRMDSCCEITFDNVEldeKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFG 270
Cdd:cd01154 227 YRIRRLkDKLGTRSVATGEVEFDDAE---AYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFG 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 271 EAIGRYQLIQEKFAHMAIKLNSMRNMLYETA------WKSDNG------LITsgdaAMCKYFCANAAFEVVDSAMQVLGG 338
Cdd:cd01154 304 KPLIDHPLMRRDLAEMEVDVEAATALTFRAArafdraAADKPVeahmarLAT----PVAKLIACKRAAPVTSEAMEVFGG 379
|
250 260 270
....*....|....*....|....*....|.
gi 757599289 339 VGIAGEHRIARFWRDLRVDRVSGGSDEMQIL 369
Cdd:cd01154 380 NGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
30-356 |
2.40e-17 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 82.76 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 30 AQCDRDSMYPERFVKALADMEIDNLLIPEEHGGLNAGFITVAAVWMELGR----LGaptyvlyQLPG---GFNTVLREGT 102
Cdd:cd01163 15 AERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAadsnIA-------QALRahfGFVEALLLAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 103 QEQIDKIMAFRGTGKQMWNSAITEPGaGSDVGSLQTTYQRRNGKVYLNGSKCFITSSAYTPYIVVmsRDADSPDKPVFTe 182
Cdd:cd01163 88 PEQFRKRWFGRVLNGWIFGNAVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTV--SALDEEGKLVFA- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 183 wFLDMSKPGIKV-NKLEKLGLRMDSCCEITFDNVELDEKDMFGRegngFNRVKEE--FDHERFLVALTNY-GTAMCAFED 258
Cdd:cd01163 164 -AVPTDRPGITVvDDWDGFGQRLTASGTVTFDNVRVEPDEVLPR----PNAPDRGtlLTAIYQLVLAAVLaGIARAALDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 259 AARYANQR-----------------VQfgEAIGRYQLiqEKFAHMAIKLNSMRnmLYETAWKSDNGLI--TSGDAAM--- 316
Cdd:cd01163 239 AVAYVRSRtrpwihsgaesarddpyVQ--QVVGDLAA--RLHAAEALVLQAAR--ALDAAAAAGTALTaeARGEAALava 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 757599289 317 -CKYFCANAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRV 356
Cdd:cd01163 313 aAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNART 353
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
92-380 |
2.58e-17 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 83.69 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 92 GGFNTVLREGTQEQIDKIMAFRGTGKQMWNSAITEPG-AGSDVGSLQTTYQRRNGKVYLNGSKCFiTSSAYTP---YIVV 167
Cdd:PLN02876 524 GNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWW-TSGAMDPrcrVLIV 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 168 MSR-DADSPDKPVFTEWFLDMSKPGIKVNK-LEKLGLrmDSC----CEITFDNVELDEKDMFGREGNGFNRVKEEFDHER 241
Cdd:PLN02876 603 MGKtDFNAPKHKQQSMILVDIQTPGVQIKRpLLVFGF--DDAphghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGR 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 242 FLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAWKSD--NGLITSGDAAMCKY 319
Cdd:PLN02876 681 LHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDrlGNKKARGIIAMAKV 760
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757599289 320 FCANAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILTLGRSVLKQYR 380
Cdd:PLN02876 761 AAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKLELQRAK 821
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
6-108 |
1.04e-15 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 72.50 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 6 NDEQELFVAGIRELMASEnWESYFAQCDRDSMYPERFVKALADMEIDNLLIPEEHGGLNAGFITVAAVWMELGRLGAPTY 85
Cdd:pfam02771 1 TEEQEALRDTVREFAEEE-IAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVA 79
|
90 100
....*....|....*....|....*
gi 757599289 86 VLYQLPGGF--NTVLREGTQEQIDK 108
Cdd:pfam02771 80 LALSVHSSLgaPPILRFGTEEQKER 104
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
124-378 |
4.97e-15 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 76.33 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 124 ITEPGAGSDVGSLQTTYQRRNGKVY-LNGSKCFITSSAYTPYIVVMSrdADSPDKPVFTEWFL-DMSKPGIKVNKL-EKL 200
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLADGSYrLVGHKWFFSVPQSDAHLVLAQ--AKGGLSCFFVPRFLpDGQRNAIRLERLkDKL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 201 GLRMDSCCEITFDNVEldeKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRYQLIQ 280
Cdd:PRK11561 262 GNRSNASSEVEFQDAI---GWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMR 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 281 EKFAHMAIKLNSMRNMLYE--TAWKSDNgliTSGDAAMCKYFCANAAFEV-------VDSAMQVLGGVGIAGEHRIARFW 351
Cdd:PRK11561 339 QVLSRMALQLEGQTALLFRlaRAWDRRA---DAKEALWARLFTPAAKFVIckrgipfVAEAMEVLGGIGYCEESELPRLY 415
|
250 260
....*....|....*....|....*..
gi 757599289 352 RDLRVDRVSGGSDEMQILTLGRSVLKQ 378
Cdd:PRK11561 416 REMPVNSIWEGSGNIMCLDVLRVLNKQ 442
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
250-356 |
2.60e-11 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 60.82 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 250 GTAMCAFEDAARYANQRVQ--FGEAIGRYQLIQEKFAHMAIKLNSMRNMLYETAW----KSDNGL----ITSGDAAMCKY 319
Cdd:pfam08028 8 GAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAArieaAAAAGKpvtpALRAEARRAAA 87
|
90 100 110
....*....|....*....|....*....|....*..
gi 757599289 320 FCANAAFEVVDSAMQVLGGVGIAGEHRIARFWRDLRV 356
Cdd:pfam08028 88 FATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHA 124
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
57-377 |
1.99e-08 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 56.03 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 57 PEEHGG----LNAGFITvaavwMELGRLGAPTYVLY--QLPGGFNTVLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAG 130
Cdd:PTZ00456 119 PEEYGGqalpLSVGFIT-----RELMATANWGFSMYpgLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCG 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 131 SDVGSLQTTYQRR-NGKVYLNGSKCFITSSAY--TPYI--VVMSRDADSPDKPVFTEWFL--------DMS---KPGIKV 194
Cdd:PTZ00456 194 TDLGQVKTKAEPSaDGSYKITGTKIFISAGDHdlTENIvhIVLARLPNSLPTTKGLSLFLvprhvvkpDGSletAKNVKC 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 195 NKLE-KLGLRMDSCCEITFDNvelDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAI 273
Cdd:PTZ00456 274 IGLEkKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMRALS 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 274 GRYQliQEKFA-----HMAIKLNSM---------RNMLYETAWKSDNGLiTSGDAA--------------MCKYFCANAA 325
Cdd:PTZ00456 351 GTKE--PEKPAdriicHANVRQNILfakavaeggRALLLDVGRLLDIHA-AAKDAAtrealdheigfytpIAKGCLTEWG 427
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 757599289 326 FEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSDEMQILT-LGRSVLK 377
Cdd:PTZ00456 428 VEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDfIGRKVLS 480
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
250-341 |
3.89e-08 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 55.21 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 250 GTAMCAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIK---LNSMRNMlyeTAWKSDNGLITSGDAAMCKYFCANAAF 326
Cdd:PRK09463 343 GGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTL---TTAAVDLGEKPSVLSAIAKYHLTERGR 419
|
90
....*....|....*
gi 757599289 327 EVVDSAMQVLGGVGI 341
Cdd:PRK09463 420 QVINDAMDIHGGKGI 434
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
54-341 |
1.79e-06 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 49.96 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 54 LLIPEEHGGLnaGF----------------ITVAAVWMELGRLGaptyvlyqlPGgfNTVLREGTQEQIDKIMAFRGTGK 117
Cdd:PRK13026 125 LIIPKEYGGK--GFsayanstivskiatrsVSAAVTVMVPNSLG---------PG--ELLTHYGTQEQKDYWLPRLADGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 118 QMWNSAITEPGAGSDVGSLQTT----YQRRNGK----VYLNGSKCFITSSaytPYIVVMS-----RDAD----SPDKPVF 180
Cdd:PRK13026 192 EIPCFALTGPEAGSDAGAIPDTgivcRGEFEGEevlgLRLTWDKRYITLA---PVATVLGlafklRDPDgllgDKKELGI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 181 TEWFLDMSKPGIKV-NKLEKLGLRmdscceitFDNVELDEKDMF--------GRE--GNGFnrvkeefdheRFLV----- 244
Cdd:PRK13026 269 TCALIPTDHPGVEIgRRHNPLGMA--------FMNGTTRGKDVFipldwiigGPDyaGRGW----------RMLVeclsa 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 245 ----ALTNYGTAM--CAFEDAARYANQRVQFGEAIGRYQLIQEKFAHMAIK---LNSMRNMlyeTAWKSDNGLITSGDAA 315
Cdd:PRK13026 331 grgiSLPALGTASghMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNtylLEAARRL---TTTGLDLGVKPSVVTA 407
|
330 340
....*....|....*....|....*.
gi 757599289 316 MCKYFCANAAFEVVDSAMQVLGGVGI 341
Cdd:PRK13026 408 IAKYHMTELARDVVNDAMDIHAGKGI 433
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
30-376 |
1.98e-05 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 46.19 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 30 AQCDRDSMYPERFVKALADMEIDNLLIPEEHGGLNAGFITVAAVWMELGRL-GAPTYVLYQLPGGFNTVLREGTQEQidk 108
Cdd:cd01159 15 PEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEAcGSAAWVASIVATHSRMLAAFPPEAQ--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 109 imafrgtgKQMWnsaiTEPGAGSDVGSLQT--TYQRRNGKVYLNGSKCFITSSAYTPYIVVMSRDADSPDKPVFTEWFLD 186
Cdd:cd01159 92 --------EEVW----GDGPDTLLAGSYAPggRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAFVVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 187 MSKPGIKVNkLEKLGLRMDSCCEITFDNVELDEKDMFGREG--NGFNRVKEEFDHERFLVALtnYGTAMCAF-------- 256
Cdd:cd01159 160 RAEYEIVDT-WHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDmmAGDGPGGSTPVYRMPLRQV--FPLSFAAVslgaaega 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 257 -EDAARYANQRVQ---FGEAIGRYQLIQEKFAHMAIKLNSMRNMLYET---AWK--SDNGLITSGDAAMCKYFCANAA-- 325
Cdd:cd01159 237 lAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERAtrdLWAhaLAGGPIDVEERARIRRDAAYAAkl 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 757599289 326 -FEVVDSAMQVLGGVGIAGEHRIARFWRDLRVDRVSGGSD-EMQILTLGRSVL 376
Cdd:cd01159 317 sAEAVDRLFHAAGGSALYTASPLQRIWRDIHAAAQHAALNpETAAEAYGRALL 369
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
80-380 |
2.83e-03 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 39.62 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 80 LGAPTYVLYQLPGgfNTVLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLQTT--YQRRNGKVYLN-----GS 152
Cdd:cd01150 98 LGAKLGLHLGLFG--NAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTatYDPLTQEFVINtpdftAT 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 153 KCFITSSAYT--------------------PYIVVMsRDADSpdkpvftewFLDMskPGIKVNKL-EKLGLR-MDScCEI 210
Cdd:cd01150 176 KWWPGNLGKTathavvfaqlitpgknhglhAFIVPI-RDPKT---------HQPL--PGVTVGDIgPKMGLNgVDN-GFL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 211 TFDNVELDEKDMFGREG----NGFNRVKEEFDHERFLVALTN---------YGTAM-----CAFedAARYANQRVQFGE- 271
Cdd:cd01150 243 QFRNVRIPRENLLNRFGdvspDGTYVSPFKDPNKRYGAMLGTrsggrvgliYDAAMslkkaATI--AIRYSAVRRQFGPk 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599289 272 ------AIGRYQLIQEK-FAHMA------IKLNSMRNMLYETAWKSDNGLITSG-----DAAMCKYFCANAAFEVVDSAM 333
Cdd:cd01150 321 psdpevQILDYQLQQYRlFPQLAaayafhFAAKSLVEMYHEIIKELLQGNSELLaelhaLSAGLKAVATWTAAQGIQECR 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 757599289 334 QVLGGVGIAGEHRIArfwrDLRVDRVSG----GSDEMQILTLGRSVLKQYR 380
Cdd:cd01150 401 EACGGHGYLAMNRLP----TLRDDNDPFctyeGDNTVLLQQTANYLLKKYA 447
|
|
| |
