|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
10-371 |
1.21e-144 |
|
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: 414.62 E-value: 1.21e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 10 EVCKELIEPIERDIEDKGLYIPETLSKLGELGFFSVSFPREFGGVGLTFEEAVKSSIILSSYTSTLSMIIGAHQLASFSI 89
Cdd:COG1960 18 EFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLALPVGVHNGAAEAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 90 FLFGSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSDYYILNGTKAFVTNAGLANLYVIFAKTNPESGA 169
Cdd:COG1960 98 LRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADVILVLARTDPAAGH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 170 RGITAFVVEGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVPKENVIGRANLGFIVAMKTLELGRILTAAGSVGLMERAL 249
Cdd:COG1960 178 RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAAL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 250 RESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKDlNASDLGLYSSIAKYYATKSAVDVTRLATQI 329
Cdd:COG1960 258 ELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLD-AGEDAALEAAMAKLFATEAALEVADEALQI 336
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 504266920 330 FGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIANQILK 371
Cdd:COG1960 337 HGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
2-371 |
2.51e-131 |
|
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: 380.46 E-value: 2.51e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 2 EKIEEITKEVCKELIEPIERDIEDKGLYIPETLSKLGELGFFSVSFPREFGGVGLTFEEAVKSSIILSSYTSTLSMIIGA 81
Cdd:cd01158 4 QMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 82 H-QLASFSIFLFGSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSDYYILNGTKAFVTNAGLANLYVIF 160
Cdd:cd01158 84 HnSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFYIVF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 161 AKTNPESGARGITAFVVEGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVPKENVIGRANLGFIVAMKTLELGRILTAAG 240
Cdd:cd01158 164 AVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 241 SVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKDlNASDLGLYSSIAKYYATKSAV 320
Cdd:cd01158 244 ALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKD-NGEPFIKEAAMAKLFASEVAM 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 504266920 321 DVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIANQILK 371
Cdd:cd01158 323 RVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
10-366 |
9.05e-113 |
|
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: 331.56 E-value: 9.05e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 10 EVCKELIEPIERDIEDKGLYIPETLSKLGELGffsvsfprefggvgltfeeavkssiilssytstlsmiiGAHQLAsfsi 89
Cdd:cd00567 12 EFAAEELEPYARERRETPEEPWELLAELGLLL--------------------------------------GAALLL---- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 90 fLFGSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSDYYILNGTKAFVTNAGLANLYVIFAKTNPE-SG 168
Cdd:cd00567 50 -AYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEEgPG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 169 ARGITAFVVEGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVPKENVIGRANLGFIVAMKTLELGRILTAAGSVGLMERA 248
Cdd:cd00567 129 HRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVALGAARAA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 249 LRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKDLNASDLGLYSSIAKYYATKSAVDVTRLATQ 328
Cdd:cd00567 209 LDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEAAREVADLAMQ 288
|
330 340 350
....*....|....*....|....*....|....*...
gi 504266920 329 IFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIA 366
Cdd:cd00567 289 IHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
2-370 |
3.66e-96 |
|
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: 291.27 E-value: 3.66e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 2 EKIEEITKEVCKELIEPIERDIEDKGLYIPETLSKLGELGFFSVSFPREFGGVGLTfeeAVKSSII---LSSYTSTLSMI 78
Cdd:cd01162 6 RAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLS---RLDASIIfeaLSTGCVSTAAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 79 IGAHQLASFSIFLFGSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSDYYILNGTKAFVTNAGLANLYV 158
Cdd:cd01162 83 ISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVYV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 159 IFAKTNpESGARGITAFVVEGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVPKENVIGRANLGFIVAMKTLELGRILTA 238
Cdd:cd01162 163 VMARTG-GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 239 AGSVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKDLNASDLGLYSSIAKYYATKS 318
Cdd:cd01162 242 SCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 504266920 319 AVDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIANQIL 370
Cdd:cd01162 322 CFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALL 373
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
2-371 |
1.90e-95 |
|
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: 289.31 E-value: 1.90e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 2 EKIEEITKEVCKELIEPIERDIEDKGLYIPETLSKLGELGFFSVSFPREFGGVGLTFEEAVKSSIILSSYTSTLSMIIGA 81
Cdd:cd01156 7 EMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 82 H-QLASFSIFLFGSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSDYYILNGTKAFVTNAGLANLYVIF 160
Cdd:cd01156 87 HsNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDADTLVVY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 161 AKTNPESGARGITAFVVEGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVPKENVIGRANLGFIVAMKTLELGRILTAAG 240
Cdd:cd01156 167 AKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 241 SVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKD-LNASDLGLYSSIakYYATKSA 319
Cdd:cd01156 247 PIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDrGNMDPKDAAGVI--LYAAEKA 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 504266920 320 VDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIANQILK 371
Cdd:cd01156 325 TQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
4-371 |
5.80e-93 |
|
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: 283.98 E-value: 5.80e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 4 IEEITKEVCKELIEPIERDIEDKGL--------YIPE-TLSKLGELGFFSVSFPREFGGVGLTfeeAVKSSIILS--SYT 72
Cdd:cd01161 23 LTEEQTEELNMLVGPVEKFFEEVNDpakndqleKIPRkTLTQLKELGLFGLQVPEEYGGLGLN---NTQYARLAEivGMD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 73 STLSMIIGAHQ-LASFSIFLFGSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSD--YYILNGTKAFVT 149
Cdd:cd01161 100 LGFSVTLGAHQsIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDgkHYVLNGSKIWIT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 150 NAGLANLYVIFAKTNPE----SGARGITAFVVEGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVPKENVIGRANLGFIV 225
Cdd:cd01161 180 NGGIADIFTVFAKTEVKdatgSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 226 AMKTLELGRILTAAGSVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIV-LTASRKKDLNASDL 304
Cdd:cd01161 260 AMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAyMTSGNMDRGLKAEY 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504266920 305 GLYSSIAKYYATKSAVDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIANQILK 371
Cdd:cd01161 340 QIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQ 406
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
3-370 |
1.16e-84 |
|
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: 261.75 E-value: 1.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 3 KIEEITKEVCKELIEPIERDIEDKGLYIPETLSKLGELGFFSVSFPREFGGVGLTFEEAVKSSIILSSYTSTLSMIIGAH 82
Cdd:cd01157 7 EFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQTAIEAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 83 QLASFSIFLFGSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSDYYILNGTKAFVTNAGLANLYVIFAK 162
Cdd:cd01157 87 SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 163 TNPESGA---RGITAFVVEGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVPKENVIGRANLGFIVAMKTLELGRILTAA 239
Cdd:cd01157 167 SDPDPKCpasKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 240 GSVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKDlNASDLGLYSSIAKYYATKSA 319
Cdd:cd01157 247 GAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVD-SGRRNTYYASIAKAFAADIA 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 504266920 320 VDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIANQIL 370
Cdd:cd01157 326 NQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
11-370 |
4.53e-81 |
|
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: 252.42 E-value: 4.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 11 VCKELIePIERDIEDKGLYIPETLSKLGELGFFSVSFPREFGGVGLTFeeavKSSIILS---SYTSTLSMIIGAH-QLAS 86
Cdd:cd01160 14 FAKEVA-PFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDL----LSAAVLWeelARAGGSGPGLSLHtDIVS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 87 FSIFLFGSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSDYYILNGTKAFVTNAGLANLYVIFAKTNPE 166
Cdd:cd01160 89 PYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGGE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 167 -SGARGITAFVVEGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVPKENVIGRANLGFIVAMKTLELGRILTAAGSVGLM 245
Cdd:cd01160 169 aRGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 246 ERALRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIV---LTASRKKDLNASDlglySSIAKYYATKSAVDV 322
Cdd:cd01160 249 EFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLdncAWRHEQGRLDVAE----ASMAKYWATELQNRV 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 504266920 323 TRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIANQIL 370
Cdd:cd01160 325 AYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
2-371 |
9.10e-68 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 218.98 E-value: 9.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 2 EKIEEITKEVCKELIEPIERDIeDKGLYIPETLS---KLGELGFFSVSFPREFGGVGLTFEEAVKSSIILSSYTSTLSMI 78
Cdd:PLN02519 31 LQFKESVQQFAQENIAPHAAAI-DATNSFPKDVNlwkLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 79 IGAH-QLASFSIFLFGSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSDYYILNGTKAFVTNAGLANLY 157
Cdd:PLN02519 110 YGAHsNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 158 VIFAKTNPESGARGITAFVVEGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVPKENVIGRANLGFIVAMKTLELGRILT 237
Cdd:PLN02519 190 VVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 238 AAGSVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKDLNASDLGLYSSIAkYYATK 317
Cdd:PLN02519 270 AAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVI-LCAAE 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 504266920 318 SAVDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIANQILK 371
Cdd:PLN02519 349 RATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
4-369 |
1.22e-62 |
|
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: 205.28 E-value: 1.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 4 IEEITKEVCKELIEPIERDIEDKGLYIPETLSKLGELGFFSVSfPREFGGVGLTfeeAVKSSIIL-------SSYTSTLS 76
Cdd:cd01151 20 IRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGAT-IKGYGCAGLS---SVAYGLIArevervdSGYRSFMS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 77 MIIGahqLASFSIFLFGSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSDYYILNGTKAFVTNAGLANL 156
Cdd:cd01151 96 VQSS---LVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 157 YVIFAKTNPESGARGitaFVVEGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVPKENVIGRANlGFIVAMKTLELGRIL 236
Cdd:cd01151 173 FVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAE-GLRGPFKCLNNARYG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 237 TAAGSVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKD--LNASDLglySSIAKYY 314
Cdd:cd01151 249 IAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDqgKATPEQ---ISLLKRN 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 504266920 315 ATKSAVDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIANQI 369
Cdd:cd01151 326 NCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAI 380
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
4-372 |
5.00e-62 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 204.40 E-value: 5.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 4 IEEITKEVCKELIEPIERDIEDKGLYIPETLSKLGELGFFSVSFPREFGGVGLtfeEAVKSSII---LSSYTSTLSMIIG 80
Cdd:PTZ00461 44 LRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGM---DAVAAVIIhheLSKYDPGFCLAYL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 81 AHQLASFSIFLF-GSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSD-YYILNGTKAFVTNAGLANLYV 158
Cdd:PTZ00461 121 AHSMLFVNNFYYsASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVFL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 159 IFAKTNPEsgargITAFVVEGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVPKENVIGRANLGFIVAMKTLELGRILTA 238
Cdd:PTZ00461 201 IYAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 239 AGSVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRK-KDLNASDLGlySSIAKYYATK 317
Cdd:PTZ00461 276 AMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNvHPGNKNRLG--SDAAKLFATP 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 504266920 318 SAVDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIANQILKG 372
Cdd:PTZ00461 354 IAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKG 408
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-371 |
6.30e-60 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 198.03 E-value: 6.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 1 MEKIEEITKEVCKEliePIERDIEDKGLYIPETLSKLGELGFFSVSFPREFGGVG-------LTFEEAVKSSIILSSYTS 73
Cdd:PRK12341 13 LASIRELITRNFPE---EYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPadyvtqmLVLEEVSKCGAPAFLITN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 74 TLSMiigahqlasFSIFLFGSDMLKEKYLLE-LNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSDYYILNGTKAFVTNAG 152
Cdd:PRK12341 90 GQCI---------HSMRRFGSAEQLRKTAEStLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 153 LANLYVIFAK-TNPESGARGITAFVVEGNTPGLAVgHKEEKMALPYLPNATVTLKDVKVPKENVIGRANLGFIVAMKTLE 231
Cdd:PRK12341 161 EYPYMLVLARdPQPKDPKKAFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 232 LGRILTAAGSVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKDlNASDLGLYSSIA 311
Cdd:PRK12341 240 MERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQAD-NGQSLRTSAALA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 312 KYYATKSAVDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIANQILK 371
Cdd:PRK12341 319 KLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILK 378
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
6-361 |
1.81e-57 |
|
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: 192.22 E-value: 1.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 6 EITKEVCKELIEPIERDIEDKGL--------YIP---ETLSKLGELGFFSVSFPREFGGVGLTFeeAVKSSI--ILSSYT 72
Cdd:cd01153 3 EEVARLAENVLAPLNADGDREGPvfddgrvvVPPpfkEALDAFAEAGWMALGVPEEYGGQGLPI--TVYSALaeIFSRGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 73 STLSMIIGAHQLASfSIFLFGSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSD-YYILNGTKAFVTNA 151
Cdd:cd01153 81 APLMYASGTQGAAA-TLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 152 ----GLANLYVIFAKT-NPESGARGITAFVV-----EGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVPkenVIGRANL 221
Cdd:cd01153 160 ehdmSENIVHLVLARSeGAPPGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 222 GFIVAMKTLELGRILTAAGSVGLMERALRESIKYAKERTQGGQP--------IANYQMIQSYLAEMKTLLETSREIVLTA 293
Cdd:cd01153 237 GLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLikaapavtIIHHPDVRRSLMTQKAYAEGSRALDLYT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 294 SRKKDL------------NASDL-GLYSSIAKYYATKSAVDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEI 360
Cdd:cd01153 317 ATVQDLaerkategedrkALSALaDLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
|
.
gi 504266920 361 Q 361
Cdd:cd01153 397 Q 397
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
222-366 |
6.56e-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: 167.05 E-value: 6.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 222 GFIVAMKTLELGRILTAAGSVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKDlNA 301
Cdd:pfam00441 3 GFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALD-AG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504266920 302 SDLGLYSSIAKYYATKSAVDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIA 366
Cdd:pfam00441 82 GPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
85-363 |
6.34e-41 |
|
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: 148.67 E-value: 6.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 85 ASFSIFLFGSDMLKEKYLLELNKGK---LIGAFSLTEPHAGSDPSAIKTTAVLD-SDYYILNGTKAFVTNAgLANLYVIF 160
Cdd:cd01154 119 AVYALRKYGPEELKQYLPGLLSDRYktgLLGGTWMTEKQGGSDLGANETTAERSgGGVYRLNGHKWFASAP-LADAALVL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 161 AKT-NPESGARGITAFVV-----EGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVpkeNVIGRANLGFIVAMKTLELGR 234
Cdd:cd01154 198 ARPeGAPAGARGLSLFLVprlleDGTRNGYRIRRLKDKLGTRSVATGEVEFDDAEA---YLIGDEGKGIYYILEMLNISR 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 235 ILTAAGSVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKDLNASDLG-------LY 307
Cdd:cd01154 275 LDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPveahmarLA 354
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 504266920 308 SSIAKYYATKSAVDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKL 363
Cdd:cd01154 355 TPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
31-371 |
5.62e-40 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 145.36 E-value: 5.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 31 PETLSK-LGELGFFSVSFPREFGGVGLTFEEAVKSSIILSSYTSTLSMIigaHQL-ASFSIFL-FGSDMLKEKYLLELNK 107
Cdd:PRK03354 39 PERFVKaLADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVL---YQLpGGFNTFLrEGTQEQIDKIMAFRGT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 108 GKLIGAFSLTEPHAGSDPSAIKTTAVLDSDYYILNGTKAFVTNAGLANLYVIFAKTNPESGARGITAFVVEGNTPGLAVG 187
Cdd:PRK03354 116 GKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 188 hKEEKMALPYLPNATVTLKDVKVPKENVIGRANLGFIVAMKTLELGRILTAAGSVGLMERALRESIKYAKERTQGGQPIA 267
Cdd:PRK03354 196 -KLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 268 NYQMIQSYLAEMKTLLETSREIVLTASRKKDLNASDLGlYSSIAKYYATKSAVDVTRLATQIFGGYGYVRGYTVERLYRE 347
Cdd:PRK03354 275 RFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSG-DAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRD 353
|
330 340
....*....|....*....|....
gi 504266920 348 AKMYEIVEGTNEIQKLIIANQILK 371
Cdd:PRK03354 354 LRVDRVSGGSDEMQILTLGRAVLK 377
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
36-370 |
1.12e-38 |
|
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: 142.10 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 36 KLGELGFFSVSFPREFGGVGLTFEEAVkssIILSSYTS----TLSMIIGAHqLASFSIFLFGSDMLKEKYLLELNKGKLI 111
Cdd:cd01152 43 ALAAAGWAAPGWPKEYGGRGASLMEQL---IFREEMAAagapVPFNQIGID-LAGPTILAYGTDEQKRRFLPPILSGEEI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 112 GAFSLTEPHAGSDPSAIKTTAVLDSDYYILNGTKAFVTNAGLANLYVIFAKTNPESGA-RGITAFVVEGNTPGLAVGHKE 190
Cdd:cd01152 119 WCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEAPKhRGISILLVDMDSPGVTVRPIR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 191 EKMALPYLpnATVTLKDVKVPKENVIGRANLGFIVAMKTLELGRILTAAGSVGLMERALResikYAKERTQGGQPIANYQ 270
Cdd:cd01152 199 SINGGEFF--NEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLLA----RLLLLTRDGRPLIDDP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 271 MIQSYLAEMKTLLETSREIVLTASRKKdLNASDLGLYSSIAKYYATKSAVDVTRLATQIFGGYGYVRGYT--------VE 342
Cdd:cd01152 273 LVRQRLARLEAEAEALRLLVFRLASAL-AAGKPPGAEASIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWE 351
|
330 340
....*....|....*....|....*...
gi 504266920 343 RLYREAKMYEIVEGTNEIQKLIIANQIL 370
Cdd:cd01152 352 ADYLRSRATTIYGGTSEIQRNIIAERLL 379
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
9-369 |
1.21e-37 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 139.99 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 9 KEVCKELIEPIERDIEDKGLYIPETLSKLGELGFFSVSFpREFGGVGLTF-EEAVKSSIILSSYTSTLSMIIGAHQLASF 87
Cdd:PLN02526 41 RECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSItASAIATAEVARVDASCSTFILVHSSLAML 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 88 SIFLFGSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSDYYILNGTKAFVTNAGLANLYVIFAKTnpeS 167
Cdd:PLN02526 120 TIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFARN---T 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 168 GARGITAFVVEGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVPKENVIGRANlGFIVAMKTLELGRILTAAGSVGLMER 247
Cdd:PLN02526 197 TTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVN-SFQDTNKVLAVSRVMVAWQPIGISMG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 248 ALRESIKYAKERTQGGQPIANYQMIQSYLAEMktlLETSREIVLTASRKKDLNASDLGL--YSSIAKYYATKSAVDVTRL 325
Cdd:PLN02526 276 VYDMCHRYLKERKQFGAPLAAFQINQEKLVRM---LGNIQAMFLVGWRLCKLYESGKMTpgHASLGKAWITKKARETVAL 352
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 504266920 326 ATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIANQI 369
Cdd:PLN02526 353 GRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
32-371 |
1.68e-29 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 119.59 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 32 ETLSKLGELGFFSVSFPREFGGVGLTFEEAVKSSIILSSYTSTLSMIIGAHQLASFSIFLFGSDMLKEKYLLELNKGKLI 111
Cdd:PTZ00456 103 EAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 112 GAFSLTEPHAGSDPSAIKTTAVLDSD-YYILNGTKAFVTnAGLANL-----YVIFAKT-NPESGARGITAFVVEGNTP-- 182
Cdd:PTZ00456 183 GTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFIS-AGDHDLtenivHIVLARLpNSLPTTKGLSLFLVPRHVVkp 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 183 --------GLAVGHKEEKMALPYLPNATVTLKDvkvPKENVIGRANLGFIVAMKTLELGRILTAAGSVGLMERALRESIK 254
Cdd:PTZ00456 262 dgsletakNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 255 YAKERT------------QGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKDL--NASD----------LGLYSSI 310
Cdd:PTZ00456 339 YARERRsmralsgtkepeKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIhaAAKDaatrealdheIGFYTPI 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504266920 311 AKYYATKSAVDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKL-IIANQILK 371
Cdd:PTZ00456 419 AKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVLS 480
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
91-371 |
2.93e-29 |
|
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: 116.72 E-value: 2.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 91 LFGSDMLKEKYLLELNKGKLIGAFSLTEPH-AGSDPSAIKTTAVLDSDYYILNGTKAFVTNAG--LANLYVIFAKTNPES 167
Cdd:cd01155 106 RYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGdpRCKIAIVMGRTDPDG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 168 GARGI--TAFVVEGNTPGLAV--------------GHKEekmalpylpnatVTLKDVKVPKENVIGRANLGFIVAMKTLE 231
Cdd:cd01155 186 APRHRqqSMILVPMDTPGVTIirplsvfgyddaphGHAE------------ITFDNVRVPASNLILGEGRGFEIAQGRLG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 232 LGRILTAAGSVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKDL--NASDLGLYSS 309
Cdd:cd01155 254 PGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTvgNKAARKEIAM 333
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504266920 310 IaKYYATKSAVDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIANQILK 371
Cdd:cd01155 334 I-KVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
113-206 |
2.90e-27 |
|
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: 103.51 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 113 AFSLTEPHAGSDPSAIKTTAVL-DSDYYILNGTKAFVTNAGLANLYVIFAKTNPESGARGITAFVVEGNTPGLAVGHKEE 191
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADgDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 504266920 192 KMALPYLPNATVTLK 206
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
31-358 |
6.65e-21 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 94.25 E-value: 6.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 31 PETLSKLGELGFFSVSFPREFGGVGltFEEAVKSSII--LSSYTSTLS---MI---IGAHQLASFsiflFGSDMLKEKYL 102
Cdd:PRK13026 111 PEVWDYLKKEGFFALIIPKEYGGKG--FSAYANSTIVskIATRSVSAAvtvMVpnsLGPGELLTH----YGTQEQKDYWL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 103 LELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSDYY--------ILNGTKAFVTNA------GLAnlyviFAKTNPE-- 166
Cdd:PRK13026 185 PRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRGEFegeevlglRLTWDKRYITLApvatvlGLA-----FKLRDPDgl 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 167 ---SGARGITAFVVEGNTPGLAVGHKEEKMALPYLpNATVTLKDVKVPKENVIG---RANLGFIVAMKTLELGR-ILTAA 239
Cdd:PRK13026 260 lgdKKELGITCALIPTDHPGVEIGRRHNPLGMAFM-NGTTRGKDVFIPLDWIIGgpdYAGRGWRMLVECLSAGRgISLPA 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 240 GSVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEM--KT-LLETSReiVLTASrkkdlnASDLGL----YSSIAK 312
Cdd:PRK13026 339 LGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIagNTyLLEAAR--RLTTT------GLDLGVkpsvVTAIAK 410
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 504266920 313 YYATKSAVDVTRLATQIFGGYGYVRG--YTVERLYREAKMYEIVEGTN 358
Cdd:PRK13026 411 YHMTELARDVVNDAMDIHAGKGIQLGpkNYLGHAYMAVPIAITVEGAN 458
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
37-349 |
1.86e-20 |
|
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: 91.62 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 37 LGELGFFSVSFPREFGGVGLTFEEAVKSSIILSSYTSTLSMIIGAHQLASFSIFLFGSDMLKEKYLLELNKGKLIG-AFS 115
Cdd:cd01163 31 LRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVEALLLAGPEQFRKRWFGRVLNGWIFGnAVS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 116 ltePHAGSDPSAIKTTAVLDSDYYILNGTKAFVTNAGLANLYVIFAKTnpESGArgITAFVVEGNTPGLAVGHKEEKMAL 195
Cdd:cd01163 111 ---ERGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALD--EEGK--LVFAAVPTDRPGITVVDDWDGFGQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 196 PYLPNATVTLKDVKVPKENVIGRANLGFIVAMKTLeLGRILTAAGSVGLMERALRESIKYAKERTQ----GGQPIA--NY 269
Cdd:cd01163 184 RLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAGIARAALDDAVAYVRSRTRpwihSGAESArdDP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 270 QMIQSYlAEMKTLLETSREIVLTASR-------------KKDLNASDLGLYSsiAKYYATKSAVDVTRLATQIFGGYGYV 336
Cdd:cd01163 263 YVQQVV-GDLAARLHAAEALVLQAARaldaaaaagtaltAEARGEAALAVAA--AKVVVTRLALDATSRLFEVGGASATA 339
|
330
....*....|...
gi 504266920 337 RGYTVERLYREAK 349
Cdd:cd01163 340 REHNLDRHWRNAR 352
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
31-358 |
9.29e-20 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 91.03 E-value: 9.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 31 PETLSKLGELGFFSVSFPREFGGVGltFEEAVKSSII--LSSYTSTLS---MI---IGAHQLasfsIFLFGSDMLKEKYL 102
Cdd:PRK09463 112 PEVWQFIKEHGFFGMIIPKEYGGLE--FSAYAHSRVLqkLASRSGTLAvtvMVpnsLGPGEL----LLHYGTDEQKDHYL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 103 LELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSDYYI--------LNGTKAFVTNA------GLAnlyviFAKTNPE-- 166
Cdd:PRK09463 186 PRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQgeevlgmrLTWNKRYITLApiatvlGLA-----FKLYDPDgl 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 167 ---SGARGITAFVVEGNTPGLAVGHKEEKMALPYLpNATVTLKDVKVPKENVIG---RANLGFIVAMKTLELGR-ILTAA 239
Cdd:PRK09463 261 lgdKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQ-NGPTRGKDVFIPLDYIIGgpkMAGQGWRMLMECLSVGRgISLPS 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 240 GSVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEM--KT-LLETSReiVLTAsrkkdlNASDLGLY----SSIAK 312
Cdd:PRK09463 340 NSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIagNAyLMDAAR--TLTT------AAVDLGEKpsvlSAIAK 411
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 504266920 313 YYATKSAVDVTRLATQIFGGYGYVRG--YTVERLYREAKMYEIVEGTN 358
Cdd:PRK09463 412 YHLTERGRQVINDAMDIHGGKGICLGpnNFLARAYQAAPIAITVEGAN 459
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
93-371 |
6.46e-18 |
|
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: 85.07 E-value: 6.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 93 GSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLD--SDYYILN-----GTKAFVTNAGL-ANLYVIFAKTN 164
Cdd:cd01150 117 GTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDplTQEFVINtpdftATKWWPGNLGKtATHAVVFAQLI 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 165 PESGARGITAFVV---EGNT----PGLAVGHKEEKMALPYLPNATVTLKDVKVPKENVIGR----------------ANL 221
Cdd:cd01150 197 TPGKNHGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRfgdvspdgtyvspfkdPNK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 222 GFIVAMKTLELGRILTAAGSVGLMERALRESIKYAKERTQGGQ-------PIANYQMIQ----SYLAE-----------M 279
Cdd:cd01150 277 RYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPkpsdpevQILDYQLQQyrlfPQLAAayafhfaakslV 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 280 KTLLETSREIVLTASRK-KDLNAsdlglYSSIAKYYATKSAVDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTN 358
Cdd:cd01150 357 EMYHEIIKELLQGNSELlAELHA-----LSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDN 431
|
330
....*....|...
gi 504266920 359 EIQKLIIANQILK 371
Cdd:cd01150 432 TVLLQQTANYLLK 444
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
100-366 |
6.70e-18 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 85.23 E-value: 6.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 100 KYLLELNKGKLIGAFSLTEPH-AGSDPSAIKTTAVLDSDYYILNGTKAFVTNA--GLANLYVIFAKTNPESGA-RGITAF 175
Cdd:PLN02876 540 EWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTDFNAPKhKQQSMI 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 176 VVEGNTPGLAVGHKEEKMALPYLPN--ATVTLKDVKVPKENVIGRANLGFIVAMKTLELGRILTAAGSVGLMERALRESI 253
Cdd:PLN02876 620 LVDIQTPGVQIKRPLLVFGFDDAPHghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMV 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 254 KYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKDL--NASDLGLYsSIAKYYATKSAVDVTRLATQIFG 331
Cdd:PLN02876 700 QRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRlgNKKARGII-AMAKVAAPNMALKVLDMAMQVHG 778
|
250 260 270
....*....|....*....|....*....|....*
gi 504266920 332 GYGYVRGYTVERLYREAKMYEIVEGTNEIQKLIIA 366
Cdd:PLN02876 779 AAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIA 813
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
10-102 |
2.70e-14 |
|
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: 68.64 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 10 EVCKELIEPIERDIEDKGLYIPETLSKLGELGFFSVSFPREFGGVGLTFEEAVkssII---LSSYTSTLSMIIGAH-QLA 85
Cdd:pfam02771 13 EFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYA---LVaeeLARADASVALALSVHsSLG 89
|
90
....*....|....*..
gi 504266920 86 SFSIFLFGSDMLKEKYL 102
Cdd:pfam02771 90 APPILRFGTEEQKERYL 106
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
88-371 |
4.24e-14 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 73.74 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 88 SIFLFGSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLD--SDYYILN-----GTKAFVTNAGL-ANLYVI 159
Cdd:PLN02636 151 SVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVINtpndgAIKWWIGNAAVhGKFATV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 160 FAKTN-PESGARGIT-----AFVV-------EGNTPGLAVGHKEEKMALPYLPNATVTLKDVKVPKENVIGR-------- 218
Cdd:PLN02636 231 FARLKlPTHDSKGVSdmgvhAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRfgdvsrdg 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 219 --------ANLGFIVAMKTLELGRILTAAGSVGLMERALRESIKYAKERTQGGQP------IANYQMIQ----------- 273
Cdd:PLN02636 311 kytsslptINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQhklmpmlasty 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 274 ------SYLAEMKTLLETSREIVLTAsrkkDLNASDLGLYSSIAKYyaTKSAVDVTRLATqifGGYGYVRGYTVERLYRE 347
Cdd:PLN02636 391 afhfatEYLVERYSEMKKTHDDQLVA----DVHALSAGLKAYITSY--TAKALSTCREAC---GGHGYAAVNRFGSLRND 461
|
330 340
....*....|....*....|....
gi 504266920 348 AKMYEIVEGTNEIQKLIIANQILK 371
Cdd:PLN02636 462 HDIFQTFEGDNTVLLQQVAADLLK 485
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
238-359 |
1.95e-12 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 63.90 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 238 AAGSVGLMERALRESIKYAKERTQ--GGQPIANYQMIQSYLAEMKTLLETSREIVL-TASRKKDL------NASDLGLYS 308
Cdd:pfam08028 3 AAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLErAAARIEAAaaagkpVTPALRAEA 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 504266920 309 SIAKYYATKSAVDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNE 359
Cdd:pfam08028 83 RRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
50-251 |
1.74e-09 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 59.12 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 50 EFGGVGLTFE-EAVKSSIILSSYTSTLSMIIGAHQLASFSIFLFGSDMLKEKYLLELNKGKLIGAFSlTEPHAGSDPSAI 128
Cdd:PTZ00457 73 EYGGLGLGHTaHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISMN 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 129 KTTAVLDSD-YYILNGTKAFVtNAGLANLYVIFAKT----NPESGARGI---TAFVVEGNTPGLAVGhkeekmalpylpN 200
Cdd:PTZ00457 152 TTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKTltqtAAEEGATEVsrnSFFICAKDAKGVSVN------------G 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504266920 201 ATVTLKDVkvPKENVIGRANLGFIVAMKTLELGRILTAAGSVGLMERALRE 251
Cdd:PTZ00457 219 DSVVFENT--PAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQE 267
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
232-360 |
8.79e-08 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 53.99 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 232 LGRILTAAGSVGLMERALRESIKYAKERTQGGQPIANYQMIQSYLAEMKTLLETSREIVLTASRKKDLNASDLG-----L 306
Cdd:PRK11561 297 MTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEalwarL 376
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 504266920 307 YSSIAKYYATKSAVDVTRLATQIFGGYGYVRGYTVERLYREAKMYEIVEGTNEI 360
Cdd:PRK11561 377 FTPAAKFVICKRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNI 430
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
71-259 |
2.07e-06 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 49.77 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 71 YTSTLSMIIGAH-QLASFSIFLFGSDMLKEKYLLELNKGKLIGAFSLTEPHAGSDPSAIKTTAVLDSDyyilngTKAFVT 149
Cdd:PLN02312 145 YDHSLAIKLGVHfFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPK------TEEFVI 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504266920 150 N--------------AGLANLYVIFAKTNPESGARGITAFVVE-----GNT-PGLAVGHKEEKMALPYLPNATVTLKDVK 209
Cdd:PLN02312 219 NtpcesaqkywiggaANHATHTIVFSQLHINGKNEGVHAFIAQirdqdGNIcPNIRIADCGHKIGLNGVDNGRIWFDNLR 298
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504266920 210 VPKENV----------------IGRANLGFIVAMKTLELGRILTAAGSVGLMERALRESIKYAKER 259
Cdd:PLN02312 299 IPRENLlnsvadvspdgkyvsaIKDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSR 364
|
|
| |
