|
Name |
Accession |
Description |
Interval |
E-value |
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
3-359 |
1.05e-123 |
|
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: 361.28 E-value: 1.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 3 EEEYRLKLREWIRNNAPESLKGRKILFETVEFDDYnelRSWQRKLADAGYLGITWPKEYGGQGLDPIYEVIAYEEFIRAG 82
Cdd:cd01152 3 EEAFRAEVRAWLAAHLPPELREESALGYREGREDR---RRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 83 LPYgrSLGSIGLMVVAPAILKHGNEEQKRKYLPRILRAEDIWCQGFSEPQAGSDLASATTRAEDKGDYFLVNGQKIWSSY 162
Cdd:cd01152 80 APV--PFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 163 AHIANYMILLARTG--EDKYKGLTMFILNMKQEGIRVSPINQLTGKSDFNTVYFNNAKVPKENIIGNVGDGWKVAMTVLN 240
Cdd:cd01152 158 AHYADWAWLLVRTDpeAPKHRGISILLVDMDSPGVTVRPIRSINGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 241 HERfmlgVTMLFTSKIALESLRGVKEREELEDEVE------------------GLEAFYRRILVKLRRGEDIDVEGSMLK 302
Cdd:cd01152 238 FER----VSIGGSAATFFELLLARLLLLTRDGRPLiddplvrqrlarleaeaeALRLLVFRLASALAAGKPPGAEASIAK 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2205656470 303 LLASELLQRIYEIAVTNYDLETVMKE---------KWYLGMLASRGRTIAGGTSEILRNVVGERAL 359
Cdd:cd01152 314 LFGSELAQELAELALELLGTAALLRDpapgaelagRWEADYLRSRATTIYGGTSEIQRNIIAERLL 379
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
3-363 |
2.27e-94 |
|
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: 286.35 E-value: 2.27e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 3 EEEYRLKLREWIRnnapeslkgRKILFETVEFDDYNEL-RSWQRKLADAGYLGITWPKEYGGQGLDPIYEVIAYEEFIRA 81
Cdd:COG1960 9 QRALRDEVREFAE---------EEIAPEAREWDREGEFpRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 82 GLPYGRSLGSigLMVVAPAILKHGNEEQKRKYLPRILRAEDIWCQGFSEPQAGSDLASATTRAEDKGDYFLVNGQKIWSS 161
Cdd:COG1960 80 DASLALPVGV--HNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 162 YAHIANYMILLARTGEDK-YKGLTMFILNMKQEGIRVSPINQLTG--KSDFNTVYFNNAKVPKENIIGNVGDGWKVAMTV 238
Cdd:COG1960 158 NAPVADVILVLARTDPAAgHRGISLFLVPKDTPGVTVGRIEDKMGlrGSDTGELFFDDVRVPAENLLGEEGKGFKIAMST 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 239 LNHERFMLGVTMLFTSKIALE-SLRGVKEREEL-----------------EDEVEGLEAFYRRILVKLRRGEDIDVEGSM 300
Cdd:COG1960 238 LNAGRLGLAAQALGIAEAALElAVAYAREREQFgrpiadfqavqhrladmAAELEAARALVYRAAWLLDAGEDAALEAAM 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2205656470 301 LKLLASELLQRIYEIAV---------TNYDLEtvmkekwyLGMLASRGRTIAGGTSEILRNVVGERALKLPK 363
Cdd:COG1960 318 AKLFATEAALEVADEALqihggygytREYPLE--------RLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
45-360 |
2.72e-56 |
|
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: 187.86 E-value: 2.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 45 RKLADAGYLGITWPKEYGGQGLDPIYEVIAYEEFIRAGlpygrslGSIGLMV------VAPAILKHGNEEQKRKYLPRIL 118
Cdd:cd01158 37 KEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVD-------ASVAVIVsvhnslGANPIIKFGTEEQKKKYLPPLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 119 RAEDIWCQGFSEPQAGSDLASATTRAEDKGDYFLVNGQKIWSSYAHIANYMILLARTGEDK-YKGLTMFILNMKQEGIRV 197
Cdd:cd01158 110 TGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFYIVFAVTDPSKgYRGITAFIVERDTPGLSV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 198 S-PINQLTGK-SDFNTVYFNNAKVPKENIIGNVGDGWKVAMTVLNHERFMLGVTMLFTSKIALE---------------- 259
Cdd:cd01158 190 GkKEDKLGIRgSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDaavdyakerkqfgkpi 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 260 -SLRGVKEREELEDEVegLEAfyRRILV-----KLRRGEDIDVEGSMLKLLASELLQRIYEIAV---------TNYDLET 324
Cdd:cd01158 270 aDFQGIQFKLADMATE--IEA--ARLLTykaarLKDNGEPFIKEAAMAKLFASEVAMRVTTDAVqifggygytKDYPVER 345
|
330 340 350
....*....|....*....|....*....|....*.
gi 2205656470 325 VMKEkwylgmlaSRGRTIAGGTSEILRNVVGERALK 360
Cdd:cd01158 346 YYRD--------AKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
71-356 |
1.44e-53 |
|
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: 179.40 E-value: 1.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 71 EVIAYEEFIRAGLPYG--RSLGSIGLMVVAPAILKHGNEEQKRKYLPRILRAEDIWCQGFSEPQAGSDLASATTRAEDKG 148
Cdd:cd00567 16 EELEPYARERRETPEEpwELLAELGLLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 149 DYFLVNGQKIWSSYAHIANYMILLARTGED--KYKGLTMFILNMKQEGIRVSPINQLTG--KSDFNTVYFNNAKVPKENI 224
Cdd:cd00567 96 DGYVLNGRKIFISNGGDADLFIVLARTDEEgpGHRGISAFLVPADTPGVTVGRIWDKMGmrGSGTGELVFDDVRVPEDNL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 225 IGNVGDGWKVAMTVLNHERFMLGVTMLFTSKIALESLR---------GVKEREE---------LEDEVEGLEAFYRRILV 286
Cdd:cd00567 176 LGEEGGGFELAMKGLNVGRLLLAAVALGAARAALDEAVeyakqrkqfGKPLAEFqavqfkladMAAELEAARLLLYRAAW 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 287 KLRRGED-IDVEGSMLKLLASELLQRIYEIAV---------TNYDLETVMKEkwylgmlaSRGRTIAGGTSEILRNVVGE 356
Cdd:cd00567 256 LLDQGPDeARLEAAMAKLFATEAAREVADLAMqihggrgysREYPVERYLRD--------ARAARIAEGTAEIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
5-246 |
2.74e-45 |
|
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: 159.11 E-value: 2.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 5 EYRLKLREWIRNNAPESLKGRKilfetVEFDDYNE-LRSWQRKLADAGYLGITWPKEYGGQGLDPIYEVIAYEEFiragl 83
Cdd:cd01156 4 DEIEMLRQSVREFAQKEIAPLA-----AKIDRDNEfPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEI----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 84 pyGRSLGSIGLMVVAPA------ILKHGNEEQKRKYLPRILRAEDIWCQGFSEPQAGSDLASATTRAEDKGDYFLVNGQK 157
Cdd:cd01156 74 --SRASGSVALSYGAHSnlcinqIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 158 IWSSYAHIANYMILLARTGEDKY-KGLTMFILNMKQEGIRVSPINQLTGK--SDFNTVYFNNAKVPKENIIGNVGDGWKV 234
Cdd:cd01156 152 MWITNGPDADTLVVYAKTDPSAGaHGITAFIVEKGMPGFSRAQKLDKLGMrgSNTCELVFEDCEVPEENILGGENKGVYV 231
|
250
....*....|..
gi 2205656470 235 AMTVLNHERFML 246
Cdd:cd01156 232 LMSGLDYERLVL 243
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
41-357 |
2.22e-43 |
|
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: 154.20 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 41 RSWQRKLADAGYLGITWPKEYGGQGLDPIYEVIAYEEFIRAGlpyGRSLG-SIGLMVVAPAILKHGNEEQKRKYLPRILR 119
Cdd:cd01160 33 REVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAG---GSGPGlSLHTDIVSPYITRAGSPEQKERVLPQMVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 120 AEDIWCQGFSEPQAGSDLASATTRAEDKGDYFLVNGQKIWSSYAHIANYMILLARTGEDK--YKGLTMFILNMKQEG-IR 196
Cdd:cd01160 110 GKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGGEArgAGGISLFLVERGTPGfSR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 197 VSPINQLTGK-SDFNTVYFNNAKVPKENIIGNVGDGWKVAMTVLNHERFMLGVTML-FTSKIALESLRGVKEREELEDEV 274
Cdd:cd01160 190 GRKLKKMGWKaQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALaAAEFMLEETRNYVKQRKAFGKTL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 275 EGLE-----------------AFYRRILVKLRRGEDIDVEGSMLKLLASELLQRIYEIAVTNYDLETVMKEKWYLGMLA- 336
Cdd:cd01160 270 AQLQvvrhkiaelatkvavtrAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRd 349
|
330 340
....*....|....*....|.
gi 2205656470 337 SRGRTIAGGTSEILRNVVGER 357
Cdd:cd01160 350 ARVQPIYGGTTEIMKELISRQ 370
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
46-259 |
6.30e-42 |
|
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: 151.08 E-value: 6.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 46 KLADAGYLGITWPKEYGGQGLDPI-YEVIAyeEFIRAGLPYGRSLG---SIGLMvvapAILKHGNEEQKRKYLPRILRAE 121
Cdd:cd01161 64 QLKELGLFGLQVPEEYGGLGLNNTqYARLA--EIVGMDLGFSVTLGahqSIGFK----GILLFGTEAQKEKYLPKLASGE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 122 DIWCQGFSEPQAGSDLASATTRAE--DKGDYFLVNGQKIWSSYAHIANYMILLART------GEDKYKgLTMFILNMKQE 193
Cdd:cd01161 138 WIAAFALTEPSSGSDAASIRTTAVlsEDGKHYVLNGSKIWITNGGIADIFTVFAKTevkdatGSVKDK-ITAFIVERSFG 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2205656470 194 GIRVSPINQLTG--KSDFNTVYFNNAKVPKENIIGNVGDGWKVAMTVLNHERFMLGVTMLFTSKIALE 259
Cdd:cd01161 217 GVTNGPPEKKMGikGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIE 284
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
45-246 |
6.28e-33 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 126.92 E-value: 6.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 45 RKLADAGYLGITWPKEYGGQGLDPIYEVIAYEEFIRAGLPYGRSLGSIGLMVVApAILKHGNEEQKRKYLPRILRAEDIW 124
Cdd:PLN02519 66 KLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCIN-QLVRNGTPAQKEKYLPKLISGEHVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 125 CQGFSEPQAGSDLASATTRAEDKGDYFLVNGQKIWSSYAHIANYMILLARTG-EDKYKGLTMFILNMKQEGIRVS-PINQ 202
Cdd:PLN02519 145 ALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDvAAGSKGITAFIIEKGMPGFSTAqKLDK 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2205656470 203 LTGK-SDFNTVYFNNAKVPKENIIGNVGDGWKVAMTVLNHERFML 246
Cdd:PLN02519 225 LGMRgSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVL 269
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
58-243 |
3.48e-28 |
|
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: 113.06 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 58 PKEYGGQGLDPIYEVIAYEEfiragLPYGRSLGSIGLMV----VAPAILKhGNEEQKRKYLPRILrAEDIWCQ-GFSEPQ 132
Cdd:cd01157 52 PEDCGGLGLGTFDTCLITEE-----LAYGCTGVQTAIEAnslgQMPVIIS-GNDEQKKKYLGRMT-EEPLMCAyCVTEPG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 133 AGSDLASATTRAEDKGDYFLVNGQKIWSSYAHIANYMILLARTGED----KYKGLTMFILNMKQEGIRV--SPINQLTGK 206
Cdd:cd01157 125 AGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDpkcpASKAFTGFIVEADTPGIQPgrKELNMGQRC 204
|
170 180 190
....*....|....*....|....*....|....*..
gi 2205656470 207 SDFNTVYFNNAKVPKENIIGNVGDGWKVAMTVLNHER 243
Cdd:cd01157 205 SDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTR 241
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
3-262 |
1.20e-27 |
|
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: 111.68 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 3 EEEyrLKLREWIRNNAPESLKGRKIL-FETVEFDdynelRSWQRKLADAGYLGITwPKEYGGQGLDPI-YEVIAYE-EFI 79
Cdd:cd01151 15 EEE--RAIRDTAREFCQEELAPRVLEaYREEKFD-----RKIIEEMGELGLLGAT-IKGYGCAGLSSVaYGLIAREvERV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 80 RAGLpygRSLGSIGLMVVAPAILKHGNEEQKRKYLPRILRAEDIWCQGFSEPQAGSDLASATTRAEDKGDYFLVNGQKIW 159
Cdd:cd01151 87 DSGY---RSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 160 SSYAHIANYMILLAR-TGEDKYKGltmFILNMKQEGIRvspINQLTGKSDF-----NTVYFNNAKVPKENIIGNVgDGWK 233
Cdd:cd01151 164 ITNSPIADVFVVWARnDETGKIRG---FILERGMKGLS---APKIQGKFSLrasitGEIVMDNVFVPEENLLPGA-EGLR 236
|
250 260
....*....|....*....|....*....
gi 2205656470 234 VAMTVLNHERFMLGVTMLFTSKIALESLR 262
Cdd:cd01151 237 GPFKCLNNARYGIAWGALGAAEDCYHTAR 265
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
41-121 |
1.64e-27 |
|
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: 104.47 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 41 RSWQRKLADAGYLGITWPKEYGGQGLDPIYEVIAYEEFIRAGLPYGRSLgSIGLMVVAPAILKHGNEEQKRKYLPRILRA 120
Cdd:pfam02771 34 RELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVALAL-SVHSSLGAPPILRFGTEEQKERYLPKLASG 112
|
.
gi 2205656470 121 E 121
Cdd:pfam02771 113 E 113
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-259 |
6.42e-27 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 109.82 E-value: 6.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 1 MNEEEYRL--KLREWIRNNAPESlkgrkilfetvEFDDYNELRSWQRKLADA------GYLGItwPKEYGGQGLDPIYEV 72
Cdd:PRK12341 5 LTEEQELLlaSIRELITRNFPEE-----------YFRTCDENGTYPREFMRAladngiSMLGV--PEEFGGTPADYVTQM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 73 IAYEEFIRAGLPYgrSLGSIGLMVvaPAILKHGNEEQKRKYLPRILRAEDI-WCQGFSEPQAGSDLASATTRAEDKGDYF 151
Cdd:PRK12341 72 LVLEEVSKCGAPA--FLITNGQCI--HSMRRFGSAEQLRKTAESTLETGDPaYALALTEPGAGSDNNSATTTYTRKNGKV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 152 LVNGQKIWSSYAHIANYMILLARTGE--DKYKGLTMFILNMKQEGIRVSPINQLTGK-SDFNTVYFNNAKVPKENIIGNV 228
Cdd:PRK12341 148 YLNGQKTFITGAKEYPYMLVLARDPQpkDPKKAFTLWWVDSSKPGIKINPLHKIGWHmLSTCEVYLDNVEVEESDLVGEE 227
|
250 260 270
....*....|....*....|....*....|.
gi 2205656470 229 GDGWKVAMTVLNHERFMLGVTMLFTSKIALE 259
Cdd:PRK12341 228 GMGFLNVMYNFEMERLINAARSLGFAECAFE 258
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
45-258 |
1.17e-26 |
|
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: 109.40 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 45 RKLADAGYLGITWPKEYGGQGLdPIYEVIAYEEFIRAGLPYgrSLGSIGLMVVAPAILKHGNEEQKRKYLPRILRAEDIW 124
Cdd:cd01153 43 DAFAEAGWMALGVPEEYGGQGL-PITVYSALAEIFSRGDAP--LMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 125 CQGFSEPQAGSDLASATTRAEDKGD-YFLVNGQKIWSSYAHIANYM----ILLARTGEDK--YKGLTMFI-----LNMKQ 192
Cdd:cd01153 120 TMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGEHDMSEnivhLVLARSEGAPpgVKGLSLFLvpkflDDGER 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2205656470 193 EGIRVSPINQLTGKSDFNT--VYFNNAKVPkenIIGNVGDGWKVAMTVLNHERFMLGVTMLFTSKIAL 258
Cdd:cd01153 200 NGVTVARIEEKMGLHGSPTceLVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAY 264
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
45-243 |
2.64e-26 |
|
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: 107.91 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 45 RKLADAGYLGITWPKEYGGQGLDPIYEVIAYEEfIRAGLPYGRSLGSIGLMVvAPAILKHGNEEQKRKYLPRILRAEDIW 124
Cdd:cd01162 39 RKAAELGFGGIYIRDDVGGSGLSRLDASIIFEA-LSTGCVSTAAYISIHNMC-AWMIDSFGNDEQRERFLPDLCTMEKLA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 125 CQGFSEPQAGSDLASATTRAEDKGDYFLVNGQKIWSSYAHIANYMILLARTGEDKYKGLTMFILNMKQEGIRVSPINQLT 204
Cdd:cd01162 117 SYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKM 196
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2205656470 205 GKSDFNT--VYFNNAKVPKENIIGNVGDGWKVAMTVLNHER 243
Cdd:cd01162 197 GWNAQPTraVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGR 237
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
43-259 |
5.59e-24 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 101.45 E-value: 5.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 43 WQRKLADAGYLGITWPKEYGGQGLDPIYEVIAYEEFIRAGLP----YGRSLGSIGlmvvapaILKHGNEEQKRKYLPRIL 118
Cdd:PRK03354 42 FVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPtyvlYQLPGGFNT-------FLREGTQEQIDKIMAFRG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 119 RAEDIWCQGFSEPQAGSDLASATTRAEDKGDYFLVNGQKIWSSYAHIANYMILLARTGEDKYKGL-TMFILNMKQEGIRV 197
Cdd:PRK03354 115 TGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVyTEWFVDMSKPGIKV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2205656470 198 SPINQLTGKSD-FNTVYFNNAKVPKENIIGNVGDGWKVAMTVLNHERFMLGVTMLFTSKIALE 259
Cdd:PRK03354 195 TKLEKLGLRMDsCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFE 257
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
125-200 |
4.09e-21 |
|
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: 86.57 E-value: 4.09e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2205656470 125 CQGFSEPQAGSDLAS-ATTRAEDKGDYFLVNGQKIWSSYAHIANYMILLARTG-EDKYKGLTMFILNMKQEGIRVSPI 200
Cdd:pfam02770 1 AFALTEPGAGSDVASlKTTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGgDDRHGGISLFLVPKDAPGVSVRRI 78
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
45-246 |
1.09e-18 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 86.53 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 45 RKLADAGYLGITWPKEYGGQGLDPIYEVIAYEE-------FIRAGLPYGrslgsiglMVVAPAILKHGNEEQKRKYLPRI 117
Cdd:PTZ00461 75 KQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHElskydpgFCLAYLAHS--------MLFVNNFYYSASPAQRARWLPKV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 118 LRAEDIWCQGFSEPQAGSD-LASATTRAEDKGDYFLVNGQKIWSSYAHIANYMILLArtgedKYKG-LTMFILNMKQEGI 195
Cdd:PTZ00461 147 LTGEHVGAMGMSEPGAGTDvLGMRTTAKKDSNGNYVLNGSKIWITNGTVADVFLIYA-----KVDGkITAFVVERGTKGF 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2205656470 196 RVSPINQLTG--KSDFNTVYFNNAKVPKENIIGNVGDGWKVAMTVLNHERFML 246
Cdd:PTZ00461 222 TQGPKIDKCGmrASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTL 274
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
101-235 |
9.19e-16 |
|
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: 77.82 E-value: 9.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 101 ILKHGNEEQKRKYLPRILRAEDIWCQGFSEPQ-AGSDLASATTRAEDKGDYFLVNGQKIWSSYA-----HIAnymILLAR 174
Cdd:cd01155 104 LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAgdprcKIA---IVMGR 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2205656470 175 T---GEDKYKGLTMFILNMKQEGIRVSPINQLTGKSDFN----TVYFNNAKVPKENIIGNVGDGWKVA 235
Cdd:cd01155 181 TdpdGAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDAPhghaEITFDNVRVPASNLILGEGRGFEIA 248
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
47-226 |
2.63e-14 |
|
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: 73.13 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 47 LADAGYLGITWPKEYGGQGLDP--IYEVIAyeEFIRAGLPYGRSLGSIGLMVVapAILKHGNEEQKRKYLPRILrAEDIW 124
Cdd:cd01163 31 LRQSGLGTLRVPKEYGGLGASLpdLYEVVR--ELAAADSNIAQALRAHFGFVE--ALLLAGPEQFRKRWFGRVL-NGWIF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 125 CQGFSEpQAGSDLASATTRAEDKGDYFLVNGQKIWSSYAHIANYMILLARTGEDKykgLTMFILNMKQEGIRV----SPI 200
Cdd:cd01163 106 GNAVSE-RGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK---LVFAAVPTDRPGITVvddwDGF 181
|
170 180
....*....|....*....|....*..
gi 2205656470 201 NQ-LTGKSdfnTVYFNNAKVPKENIIG 226
Cdd:cd01163 182 GQrLTASG---TVTFDNVRVEPDEVLP 205
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
47-188 |
1.34e-12 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 68.74 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 47 LADAGYLGITWPKEYGGQGLDPIYEVIAYEEFIRAGLPYGRSLG-SIGlmvVAPAILKHGNEEQKRKYLPRILRAEDIWC 125
Cdd:PTZ00456 108 LKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGlSIG---AANTLMAWGSEEQKEQYLTKLVSGEWSGT 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 126 QGFSEPQAGSDLASATTRAEDKGD-YFLVNGQKIWSS---YAHIANYM-ILLART--GEDKYKGLTMFIL 188
Cdd:PTZ00456 185 MCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISagdHDLTENIVhIVLARLpnSLPTTKGLSLFLV 254
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
229-358 |
1.00e-11 |
|
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: 62.27 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 229 GDGWKVAMTVLNHERFMLGVTMLFTSKIALE-----------------SLRGVKER-EELEDEVEGLEAFYRRILVKLRR 290
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDealayarrrkafgrpliDFQLVRHKlAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2205656470 291 GEDIDVEGSMLKLLASELLQRIYEIAVT-----NYDLETVMkEKWYLGMLASRgrtIAGGTSEILRNVVGERA 358
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQlhggyGYLREYPV-ERLYRDARVLR---IGEGTSEIQRNIIARRL 149
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
46-223 |
5.20e-11 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 63.33 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 46 KLADAGYLGITwPKEYGGQGLDPIYEVIAYEEFIRAGLPYGRSL---GSIGLMVVAPAilkhGNEEQKRKYLPRILRAED 122
Cdd:PLN02526 68 KLGSLGIAGGT-IKGYGCPGLSITASAIATAEVARVDASCSTFIlvhSSLAMLTIALC----GSEAQKQKYLPSLAQLDT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 123 IWCQGFSEPQAGSDLASATTRAEDKGDYFLVNGQKIWSSYAHIANYMILLAR-TGEDKYKGltmFILNMKQEGIRVSPIN 201
Cdd:PLN02526 143 VACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFARnTTTNQING---FIVKKGAPGLKATKIE 219
|
170 180
....*....|....*....|....
gi 2205656470 202 QLTGKSDFNT--VYFNNAKVPKEN 223
Cdd:PLN02526 220 NKIGLRMVQNgdIVLKDVFVPDED 243
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
98-244 |
3.65e-09 |
|
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: 57.77 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 98 APAILKHGNEEQKrKYLPRIL--RAEDIW--CQGFSEPQAGSDLASATTRAE-DKGDYFLVNGQKiWSSYAHIANYMILL 172
Cdd:cd01154 120 VYALRKYGPEELK-QYLPGLLsdRYKTGLlgGTWMTEKQGGSDLGANETTAErSGGGVYRLNGHK-WFASAPLADAALVL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 173 ART--GEDKYKGLTMFILNMKQE-----GIRVSPINQLTGKSDFNT--VYFNNAKVpkeNIIGNVGDGWKVAMTVLNHER 243
Cdd:cd01154 198 ARPegAPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATgeVEFDDAEA---YLIGDEGKGIYYILEMLNISR 274
|
.
gi 2205656470 244 F 244
Cdd:cd01154 275 L 275
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
60-264 |
9.19e-09 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 56.81 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 60 EYGGQGLDPIYEVIAYEEFIRAGLpyGRSLGSIGLMVVAPAILKH-GNEEQKRKYLPRIlrAEDIWCQGFS-EPQAGSDL 137
Cdd:PTZ00457 73 EYGGLGLGHTAHALIYEEVGTNCD--SKLLSTIQHSGFCTYLLSTvGSKELKGKYLTAM--SDGTIMMGWAtEEGCGSDI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 138 ASATTRA--EDKGDYFLVnGQKiWSSYAHIANYMILLART--------GEDKYKGLTMFILNMKQEGIRVSPinqltgks 207
Cdd:PTZ00457 149 SMNTTKAslTDDGSYVLT-GQK-RCEFAASATHFLVLAKTltqtaaeeGATEVSRNSFFICAKDAKGVSVNG-------- 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2205656470 208 dfNTVYFNNAkvPKENIIGNVGDGWKVAMTVLNHERFMLGVTMLFTSKIALESLRGV 264
Cdd:PTZ00457 219 --DSVVFENT--PAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQELRGS 271
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
43-139 |
9.94e-09 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 56.75 E-value: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 43 WQRkLADAGYLGITWPKEYGGQGLDPiyevIAYEEFIR--AglpyGRSL-GSIGLMV---VAPA--ILKHGNEEQKRKYL 114
Cdd:PRK09463 115 WQF-IKEHGFFGMIIPKEYGGLEFSA----YAHSRVLQklA----SRSGtLAVTVMVpnsLGPGelLLHYGTDEQKDHYL 185
|
90 100
....*....|....*....|....*
gi 2205656470 115 PRILRAEDIWCQGFSEPQAGSDLAS 139
Cdd:PRK09463 186 PRLARGEEIPCFALTSPEAGSDAGS 210
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
43-139 |
2.62e-07 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 52.27 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 43 WQRkLADAGYLGITWPKEYGGQGLDP-----IYEVIAyeefiraglpyGRSlGSIGLMVVAP-------AILKHGNEEQK 110
Cdd:PRK13026 114 WDY-LKKEGFFALIIPKEYGGKGFSAyanstIVSKIA-----------TRS-VSAAVTVMVPnslgpgeLLTHYGTQEQK 180
|
90 100
....*....|....*....|....*....
gi 2205656470 111 RKYLPRILRAEDIWCQGFSEPQAGSDLAS 139
Cdd:PRK13026 181 DYWLPRLADGTEIPCFALTGPEAGSDAGA 209
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
101-235 |
7.76e-07 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 50.95 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 101 ILKHGNEEQKRKYLPRILRAEdiWCQGFS--EPQ-AGSDLASATTRAEDKGDYFLVNGQKIWSSYAH--IANYMILLART 175
Cdd:PLN02876 529 LLRYGNKEQQLEWLIPLLEGK--IRSGFAmtEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMdpRCRVLIVMGKT 606
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2205656470 176 --GEDKYKGLTMFILNMKQEGIRVSPINQLTGKSD----FNTVYFNNAKVPKENIIGNVGDGWKVA 235
Cdd:PLN02876 607 dfNAPKHKQQSMILVDIQTPGVQIKRPLLVFGFDDaphgHAEISFENVRVPAKNILLGEGRGFEIA 672
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
19-253 |
9.12e-04 |
|
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: 41.16 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 19 PESLKGRKILFETVEFD-------DYNEL---RSWQRKLADAGYLGItWPKEYGGQGLDPIYEVIAYEEFIRAGL--PYG 86
Cdd:cd01150 25 EENLRRKREVERELESDplfqrelPSKHLsreELYEELKRKAKTDVE-RMGELMADDPEKMLALTNSLGGYDLSLgaKLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 87 RSLGSIGlmvvaPAILKHGNEEQKRKYLPRILRAEDIWCQGFSEPQAGSDLASATTRA--EDKGDYFLVN-----GQKIW 159
Cdd:cd01150 104 LHLGLFG-----NAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWW 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 160 -SSYAHIANYMILLAR-TGEDKYKGLTMFILNMKQ-------EGIRVSPINQLTGKS--DFNTVYFNNAKVPKENIIGNV 228
Cdd:cd01150 179 pGNLGKTATHAVVFAQlITPGKNHGLHAFIVPIRDpkthqplPGVTVGDIGPKMGLNgvDNGFLQFRNVRIPRENLLNRF 258
|
250 260
....*....|....*....|....*....
gi 2205656470 229 G----DGWKVAMTVLNHERFMlgvTMLFT 253
Cdd:cd01150 259 GdvspDGTYVSPFKDPNKRYG---AMLGT 284
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
99-225 |
4.05e-03 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 39.05 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656470 99 PAILKHGNEEQKRKYLPRILRAEDIWCQGFSEPQAGSDLASATTRA--EDKGDYFLVNGQKIWSS------YAHIANYMI 170
Cdd:PLN02443 108 PAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTAtfDPKTDEFVIHSPTLTSSkwwpggLGKVSTHAV 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2205656470 171 LLAR-TGEDKYKGLTMFILNMKQ-------EGIRVSPINQLTGKSDFNT-----VYFNNAKVPKENII 225
Cdd:PLN02443 188 VYARlITNGKDHGIHGFIVQLRSlddhsplPGVTVGDIGMKFGNGAYNTmdngfLRFDHVRIPRDQML 255
|
|
| |
