|
Name |
Accession |
Description |
Interval |
E-value |
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
5-382 |
0e+00 |
|
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: 791.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 5 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ 84
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 85 TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 164
Cdd:cd01157 81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 165 YFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKT 244
Cdd:cd01157 161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 245 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF 324
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 554506554 325 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDK 382
Cdd:cd01157 321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-378 |
2.46e-160 |
|
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: 455.07 E-value: 2.46e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 1 MLQEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGC 80
Cdd:COG1960 1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 81 TGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGG 160
Cdd:COG1960 81 ASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 161 KANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGA 240
Cdd:COG1960 161 VADVILVLARTDPAAGH---RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMST 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 241 FDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASI 320
Cdd:COG1960 238 LNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAM 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 554506554 321 AKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 378
Cdd:COG1960 318 AKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARR 375
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
7-382 |
1.12e-150 |
|
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: 430.15 E-value: 1.12e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 7 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTA 86
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 87 IEG-NSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 165
Cdd:cd01158 81 VSVhNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 166 FLLARSDPDPKapaNKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTR 245
Cdd:cd01158 161 IVFAVTDPSKG---YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 246 PVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFA 325
Cdd:cd01158 238 IGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 554506554 326 GDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAReHIDK 382
Cdd:cd01158 318 SEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAK-HLLK 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
7-377 |
5.71e-134 |
|
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: 386.25 E-value: 5.71e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 7 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGlmnthipencgglglgtfdacliseelaygctgvqta 86
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLL------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 87 iegnslGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYF 166
Cdd:cd00567 44 ------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 167 LLARSDPDPkaPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRP 246
Cdd:cd00567 118 VLARTDEEG--PGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 247 VVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRN-TYYASIAKAFA 325
Cdd:cd00567 196 LLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEaRLEAAMAKLFA 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 554506554 326 GDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 377
Cdd:cd00567 276 TEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
6-378 |
1.55e-112 |
|
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: 333.26 E-value: 1.55e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 6 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQT 85
Cdd:cd01162 2 NEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 86 AIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 165
Cdd:cd01162 82 YISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 166 FLLARSDpdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTR 245
Cdd:cd01162 162 VVMARTG----GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 246 PVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRN-TYYASIAKAF 324
Cdd:cd01162 238 LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDaVKLCAMAKRF 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 554506554 325 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 378
Cdd:cd01162 318 ATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARA 371
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
5-378 |
6.05e-111 |
|
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: 329.37 E-value: 6.05e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 5 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ 84
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 85 TAIEGNS---LGQmpIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGK 161
Cdd:cd01156 82 LSYGAHSnlcINQ--IYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 162 ANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAF 241
Cdd:cd01156 160 ADTLVVYAKTDPSAGA---HGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 242 DKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIA 321
Cdd:cd01156 237 DYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGV 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 554506554 322 KAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 378
Cdd:cd01156 317 ILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRE 373
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
7-378 |
1.49e-102 |
|
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: 307.89 E-value: 1.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 7 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY-GCTGVQT 85
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARaGGSGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 86 AIEgNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 165
Cdd:cd01160 81 SLH-TDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 166 FLLARSDPDPKAPANKAFtgFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTR 245
Cdd:cd01160 160 IVVARTGGEARGAGGISL--FLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 246 PVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFA 325
Cdd:cd01160 238 LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 554506554 326 GDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 378
Cdd:cd01160 318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
1-376 |
1.01e-91 |
|
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: 281.28 E-value: 1.01e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 1 MLQEFTEQQKEFQATARKFAREEIIPvaAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY-G 79
Cdd:cd01161 23 LTEEQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMdL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 80 CTGVQTAIEgNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWIT 157
Cdd:cd01161 101 GFSVTLGAH-QSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWIT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 158 NGGKANWYFLLARSD-PDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKV 236
Cdd:cd01161 180 NGGIADIFTVFAKTEvKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 237 AMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTY 316
Cdd:cd01161 260 AMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEY 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 554506554 317 Y--ASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVA 376
Cdd:cd01161 340 QieAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIA 401
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
5-378 |
1.85e-84 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 262.51 E-value: 1.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 5 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP--VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEEL--AYGC 80
Cdd:PLN02519 26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEIsrASGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 81 TGVQTAIEGNsLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGG 160
Cdd:PLN02519 106 VGLSYGAHSN-LCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 161 KANWYFLLARSDPdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGA 240
Cdd:PLN02519 185 VAQTLVVYAKTDV---AAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 241 FDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASI 320
Cdd:PLN02519 262 LDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAG 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 554506554 321 AKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 378
Cdd:PLN02519 342 VILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRE 399
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
6-378 |
3.34e-72 |
|
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: 230.32 E-value: 3.34e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 6 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNThIPENCGGLGLGTFDACLISEELAYGCTGVQT 85
Cdd:cd01151 14 TEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVERVDSGYRS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 86 AIE-GNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 164
Cdd:cd01151 93 FMSvQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 165 YFLLARSDPDPKapankaFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGdGAGFKVAMGAFDKT 244
Cdd:cd01151 173 FVVWARNDETGK------IRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPG-AEGLRGPFKCLNNA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 245 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELArmsyQRAAWEV----DSGRRNTYYASI 320
Cdd:cd01151 246 RYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALG----LLACLRVgrlkDQGKATPEQISL 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 554506554 321 AKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 378
Cdd:cd01151 322 LKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRA 379
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
7-377 |
3.93e-62 |
|
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: 204.12 E-value: 3.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 7 EQQKEFQATARKFAREEIIP-----VAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCT 81
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPelreeSALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 82 GVQtaieGNSLGQM---PIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWIT 157
Cdd:cd01152 81 PVP----FNQIGIDlagPTILAyGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 158 NGGKANWYFLLARSDPDpkAPANKAFTGFIVEADTPGIQIgR--KELNMGqrcSDTRGIVFEDVKVPKENVLIGDGAGFK 235
Cdd:cd01152 157 GAHYADWAWLLVRTDPE--APKHRGISILLVDMDSPGVTV-RpiRSINGG---EFFNEVFLDDVRVPDANRVGEVNDGWK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 236 VAMGAFDKTRPVVAAGAVGLAQRALDeatkYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNT 315
Cdd:cd01152 231 VAMTTLNFERVSIGGSAATFFELLLA----RLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 316 YYASIAKAFAGDIANQLATDAVQILG--------GNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 377
Cdd:cd01152 307 AEASIAKLFGSELAQELAELALELLGtaallrdpAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAE 376
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
14-371 |
2.66e-61 |
|
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: 202.62 E-value: 2.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 14 ATARKFAREEIIPVAAEYDKTG--------EYPVP---LIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTG 82
Cdd:cd01153 3 EEVARLAENVLAPLNADGDREGpvfddgrvVVPPPfkeALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 83 VqtAIEGNSLGQMPIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNGG 160
Cdd:cd01153 83 L--MYASGTQGAAATLLAhGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 161 KANW----YFLLARSDPDPkaPANKAFTGFIV-----EADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPkenvLIGD- 230
Cdd:cd01153 161 HDMSenivHLVLARSEGAP--PGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE----LIGEe 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 231 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVE--------HQAISFMLAEMAMKVELARMSYQ 302
Cdd:cd01153 235 GMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAapavtiihHPDVRRSLMTQKAYAEGSRALDL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 303 RAAWEVDSGRR--------------NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTS 368
Cdd:cd01153 315 YTATVQDLAERkategedrkalsalADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTT 394
|
...
gi 554506554 369 QIQ 371
Cdd:cd01153 395 GIQ 397
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
6-367 |
3.00e-61 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 202.86 E-value: 3.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 6 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQT 85
Cdd:PTZ00461 38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 86 AIEGNS-LGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDE-YIINGQKMWITNGGKAN 163
Cdd:PTZ00461 118 AYLAHSmLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGnYVLNGSKIWITNGTVAD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 164 WYFLLARSDpdpkapanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDK 243
Cdd:PTZ00461 198 VFLIYAKVD--------GKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLEL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 244 TRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKA 323
Cdd:PTZ00461 270 ERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKL 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 554506554 324 FAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGT 367
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
6-384 |
3.42e-59 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 196.49 E-value: 3.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 6 TEQQKEFQATARKF-AREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYgcTGVQ 84
Cdd:PRK12341 6 TEEQELLLASIRELiTRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSK--CGAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 85 TAIEGNSLGQMPIIIAGNDQQKKKYLgRMTEEPLMCAYC--VTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKA 162
Cdd:PRK12341 84 AFLITNGQCIHSMRRFGSAEQLRKTA-ESTLETGDPAYAlaLTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 163 NWYFLLARsDPDPKAPaNKAFTGFIVEADTPGIQIGRKElNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFD 242
Cdd:PRK12341 163 PYMLVLAR-DPQPKDP-KKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 243 KTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAK 322
Cdd:PRK12341 240 MERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAK 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 554506554 323 AFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK 384
Cdd:PRK12341 320 LYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDYQ 381
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
231-377 |
1.11e-53 |
|
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: 174.75 E-value: 1.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 231 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDS 310
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 554506554 311 GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 377
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
7-377 |
2.79e-53 |
|
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: 181.43 E-value: 2.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 7 EQQKEFQATARKFAREEIIPVAAEYDktgEYPVPLIRRAW--------------ELGLMNTHIPENCGGLGLGTFDACLI 72
Cdd:cd01155 1 RKAQELRARVKAFMEEHVYPAEQEFL---EYYAEGGDRWWtpppiieklkakakAEGLWNLFLPEVSGLSGLTNLEYAYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 73 SEEL--------AYGCTGVQTaiegnslGQMPIIIA-GNDQQKKKYLgrmteEPLM-----CAYCVTEPG-AGSDVAGIK 137
Cdd:cd01155 78 AEETgrsffapeVFNCQAPDT-------GNMEVLHRyGSEEQKKQWL-----EPLLdgkirSAFAMTEPDvASSDATNIE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 138 TKAEKKGDEYIINGQKMWITNGG--KANWYFLLARSDPDpKAPANKAFTGFIVEADTPGIQIGRKELNMGQrcSDTRG-- 213
Cdd:cd01155 146 CSIERDGDDYVINGRKWWSSGAGdpRCKIAIVMGRTDPD-GAPRHRQQSMILVPMDTPGVTIIRPLSVFGY--DDAPHgh 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 214 --IVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMA 291
Cdd:cd01155 223 aeITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 292 MKVELARMSYQRAAWEVDSGRRNTYYASIA--KAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQ 369
Cdd:cd01155 303 IEIEQARLLVLKAAHMIDTVGNKAARKEIAmiKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDE 382
|
....*...
gi 554506554 370 IQRLIVAR 377
Cdd:cd01155 383 VHLRSIAR 390
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
5-384 |
5.23e-48 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 167.32 E-value: 5.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 5 FTEQQKEFQATARKF-AREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELayGCTGV 83
Cdd:PRK03354 5 LNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--GRLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 84 QTAIegnsLGQMP-----IIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN 158
Cdd:PRK03354 83 PTYV----LYQLPggfntFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 159 GGKANWYFLLARSDPDPKAPAnkaFTGFIVEADTPGIQIGRKElNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM 238
Cdd:PRK03354 159 SAYTPYIVVMARDGASPDKPV---YTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 239 GAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA 318
Cdd:PRK03354 235 EEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDA 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 554506554 319 SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK 384
Cdd:PRK03354 315 AMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
6-378 |
3.42e-45 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 160.40 E-value: 3.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 6 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIP-ENCGGLGLgTFDACLISEELAYGCTGVQ 84
Cdd:PLN02526 30 TPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIKgYGCPGLSI-TASAIATAEVARVDASCST 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 85 TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 164
Cdd:PLN02526 109 FILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 165 YFLLARSdpdpkaPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAgFKVAMGAFDKT 244
Cdd:PLN02526 189 LVIFARN------TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNS-FQDTNKVLAVS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 245 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF 324
Cdd:PLN02526 262 RVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAW 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 554506554 325 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVARE 378
Cdd:PLN02526 342 ITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGRE 395
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
6-113 |
6.00e-39 |
|
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: 134.90 E-value: 6.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 6 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQT 85
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100
....*....|....*....|....*....
gi 554506554 86 AIE-GNSLGQMPIIIAGNDQQKKKYLGRM 113
Cdd:pfam02771 81 ALSvHSSLGAPPILRFGTEEQKERYLPKL 109
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
109-377 |
2.99e-35 |
|
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: 133.65 E-value: 2.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 109 YLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEK-KGDEYIINGQKmWITNGGKANWYFLLARsdPDPKAPANKAFTGFI 187
Cdd:cd01154 138 LLSDRYKTGLLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLAR--PEGAPAGARGLSLFL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 188 VEADTP-----GIQIGRKELNMGQRCSDTRGIVFEDVkvpkENVLIGD-GAGFKVAMGAFDKTRPVVAAGAVGLAQRALD 261
Cdd:cd01154 215 VPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA----EAYLIGDeGKGIYYILEMLNISRLDNAVAALGIMRRALS 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 262 EATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAA--WEVDSGRRNTYYA------SIAKAFAGDIANQLA 333
Cdd:cd01154 291 EAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAAraFDRAAADKPVEAHmarlatPVAKLIACKRAAPVT 370
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 554506554 334 TDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 377
Cdd:cd01154 371 SEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLR 414
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
93-370 |
1.56e-32 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 129.53 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 93 GQMPIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPG-AGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLAR 170
Cdd:PLN02876 524 GNMEVLLRyGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVM 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 171 SDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGqrCSDT----RGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRP 246
Cdd:PLN02876 604 GKTDFNAPKHKQQSMILVDIQTPGVQIKRPLLVFG--FDDAphghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRL 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 247 VVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVD--SGRRNTYYASIAKAF 324
Cdd:PLN02876 682 HHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDrlGNKKARGIIAMAKVA 761
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 554506554 325 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQI 370
Cdd:PLN02876 762 APNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
121-217 |
6.03e-30 |
|
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: 110.83 E-value: 6.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 121 AYCVTEPGAGSDVAGIKTKA-EKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGR 199
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRH---GGISLFLVPKDAPGVSVRR 77
|
90
....*....|....*...
gi 554506554 200 KELNMGQRCSDTRGIVFE 217
Cdd:pfam02770 78 IETKLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
5-373 |
3.26e-22 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 98.40 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 5 FTEQQKEFQ----ATARKFAREEIIPVAAEYD-------KTGEYPVPL-IRRAWEL----GLMNTHIPENCGGLGLgTFD 68
Cdd:PTZ00456 52 KTDVTKELMdsllEEASKLATQTLLPLYESSDsegcvllKDGNVTTPKgFKEAYQAlkagGWTGISEPEEYGGQAL-PLS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 69 ACLISEELAYGCTGVQTAIEGNSLGQMPIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-E 146
Cdd:PTZ00456 131 VGFITRELMATANWGFSMYPGLSIGAANTLMAwGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgS 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 147 YIINGQKMWITNGG---KAN-WYFLLARSDPDPkaPANKAFTGFIVEADTP----------GIQIGRKELNMGQRCSDTR 212
Cdd:PTZ00456 211 YKITGTKIFISAGDhdlTENiVHIVLARLPNSL--PTTKGLSLFLVPRHVVkpdgsletakNVKCIGLEKKMGIKGSSTC 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 213 GIVFEDVKvpkeNVLIGD-GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTF------------GKLLVE 279
Cdd:PTZ00456 289 QLSFENSV----GYLIGEpNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIIC 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 280 HQAISFML------AE--MAMKVELAR-MSYQRAAWEVDS----GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFN 346
Cdd:PTZ00456 365 HANVRQNIlfakavAEggRALLLDVGRlLDIHAAAKDAATrealDHEIGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYI 444
|
410 420
....*....|....*....|....*..
gi 554506554 347 TEYPVEKLMRDAKIYQIYEGTSQIQRL 373
Cdd:PTZ00456 445 KGNGMEQILRDARIGTLYEGTTGIQAL 471
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
247-369 |
2.77e-19 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 83.16 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 247 VVAAGAVGLAQRALDEATKYALERKT--FGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWE----VDSGRRNTYY--- 317
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARieaaAAAGKPVTPAlra 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 554506554 318 -ASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQ 369
Cdd:pfam08028 81 eARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
95-384 |
2.24e-14 |
|
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: 74.67 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 95 MPIIIA-GNDQQKKKYL-GRMTEEPLMCaYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGK-ANW 164
Cdd:cd01150 110 GNAIKNlGTDEHQDYWLqGANNLEIIGC-FAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWWPGNLGKtATH 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 165 YFLLARSDPDPKapaNKAFTGFIV---EADT----PGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------IGDG 231
Cdd:cd01150 189 AVVFAQLITPGK---NHGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLnrfgdvSPDG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 232 A----------GFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFG--------KLLvEHQ------------ 281
Cdd:cd01150 266 TyvspfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGpkpsdpevQIL-DYQlqqyrlfpqlaa 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 282 --AISFMLAEMAMKVelarMSYQRAAWEVDSGRRNTYYASIA--KAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRD 357
Cdd:cd01150 345 ayAFHFAAKSLVEMY----HEIIKELLQGNSELLAELHALSAglKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDD 420
|
330 340
....*....|....*....|....*..
gi 554506554 358 AKIYQIYEGTSQIQRLIVAREHIDKYK 384
Cdd:cd01150 421 NDPFCTYEGDNTVLLQQTANYLLKKYA 447
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
12-359 |
8.28e-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: 71.97 E-value: 8.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 12 FQATARKFAREeiipvAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAygctgvqtAIEGNs 91
Cdd:cd01163 3 ARPLAARIAEG-----AAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELA--------AADSN- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 92 LGQMP---------IIIAGNDQQKKKYLGRMTEEPLM-CAycVTEPGaGSDVAGIKTKAEKKGDEYIINGQKmWITNGGK 161
Cdd:cd01163 69 IAQALrahfgfveaLLLAGPEQFRKRWFGRVLNGWIFgNA--VSERG-SVRPGTFLTATVRDGGGYVLNGKK-FYSTGAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 162 ANWYFLLARSDPDPKApankafTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM-GA 240
Cdd:cd01163 145 FSDWVTVSALDEEGKL------VFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLlTA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 241 FDKTrpVVAAGAVGLAQRALDEATKYALER-KTFGKLLVEH--------QAIsfmlAEMAMKVELARMSYQRAAWEVD-- 309
Cdd:cd01163 219 IYQL--VLAAVLAGIARAALDDAVAYVRSRtRPWIHSGAESarddpyvqQVV----GDLAARLHAAEALVLQAARALDaa 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 310 --SGRRNTYYASI--------AKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAK 359
Cdd:cd01163 293 aaAGTALTAEARGeaalavaaAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
125-377 |
2.25e-13 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 71.32 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 125 TEPGAGSDVAGIKTKAEKKGDE-YIINGQKmwitnggkanWYFLLARSDPD-PKAPANKAFTGFIVEADTP-----GIQI 197
Cdd:PRK11561 185 TEKQGGSDVLSNTTRAERLADGsYRLVGHK----------WFFSVPQSDAHlVLAQAKGGLSCFFVPRFLPdgqrnAIRL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 198 GRKELNMGQRCSDTRGIVFEDVK---VPKEnvliGDGAGFKVAMGAFdkTRPVVAAGAVGLAQRALDEATKYALERKTFG 274
Cdd:PRK11561 255 ERLKDKLGNRSNASSEVEFQDAIgwlLGEE----GEGIRLILKMGGM--TRFDCALGSHGLMRRAFSVAIYHAHQRQVFG 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 275 KLLVEHQAISFMLAEMAMKVE--------LARMSYQRA-AWEVDSGRRNTYYA--SIAKAFAGDIAnqlatDAVQILGGN 343
Cdd:PRK11561 329 KPLIEQPLMRQVLSRMALQLEgqtallfrLARAWDRRAdAKEALWARLFTPAAkfVICKRGIPFVA-----EAMEVLGGI 403
|
250 260 270
....*....|....*....|....*....|....
gi 554506554 344 GFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 377
Cdd:PRK11561 404 GYCEESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
139-358 |
2.34e-10 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 61.60 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 139 KAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFtgFIVEADtpgIQIGRKELNMGQRCSDTRGIVFED 218
Cdd:cd01159 112 RAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAF--VVPRAE---YEIVDTWHVVGLRGTGSNTVVVDD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 219 VKVPKENVLIGDGA-----------GFKVAMGAFDKtrPVVAAGAVGLAQRALDEATKYALER---KTFGKLLVEHQAIS 284
Cdd:cd01159 187 VFVPEHRTLTAGDMmagdgpggstpVYRMPLRQVFP--LSFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 285 FMLAEMAMKVELARMSYQRAAWEVDS---------------GRRNTYYASIAKAFAGDIANQLAtdavqilGGNGFNTEY 349
Cdd:cd01159 265 LRLAEAAAELDAARAFLERATRDLWAhalaggpidveerarIRRDAAYAAKLSAEAVDRLFHAA-------GGSALYTAS 337
|
....*....
gi 554506554 350 PVEKLMRDA 358
Cdd:cd01159 338 PLQRIWRDI 346
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
82-274 |
6.21e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 57.56 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 82 GVQTAIEGNSlgqmpIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKM 154
Cdd:PLN02636 142 GVQYSLWGGS-----VINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFVINtpndgAIKW 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 155 WITNG---GK-ANWYFLLARSDPDPKAPANKAFTGFIV-------EADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPK 223
Cdd:PLN02636 217 WIGNAavhGKfATVFARLKLPTHDSKGVSDMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPR 296
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 554506554 224 ENVL--IGD--------------GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFG 274
Cdd:PLN02636 297 DNLLnrFGDvsrdgkytsslptiNKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFG 363
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
50-262 |
6.60e-09 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 57.58 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 50 LMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSlGQMPIIIA--GNDQQKKKYLGRMTEEPLMCAYCVTEp 127
Cdd:PTZ00457 65 LYGARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHS-GFCTYLLStvGSKELKGKYLTAMSDGTIMMGWATEE- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 128 GAGSDVAGIKTKAEKKGD-EYIINGQKMWItNGGKANWYFLLAR------SDPDPKAPANKAFtgFIVEADTPGIQIgrk 200
Cdd:PTZ00457 143 GCGSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKtltqtaAEEGATEVSRNSF--FICAKDAKGVSV--- 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 554506554 201 elnmgqrcsDTRGIVFEDvkVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDE 262
Cdd:PTZ00457 217 ---------NGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQE 267
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
101-274 |
2.44e-08 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 56.00 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 101 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGKANWYFLL-ARSD 172
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTAtfDPKTDEFVIHsptltSSKWWPGGLGKVSTHAVVyARLI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 173 PDPKapaNKAFTGFIVEADT-------PGI---QIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------------IGD 230
Cdd:PLN02443 194 TNGK---DHGIHGFIVQLRSlddhsplPGVtvgDIGMKFGNGAYNTMDNGFLRFDHVRIPRDQMLmrlskvtregkyVQS 270
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 554506554 231 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFG 274
Cdd:PLN02443 271 DVPRQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFG 314
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
55-344 |
4.04e-08 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 55.35 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 55 IPENCGGLGlgtFDA----CLISEELAYGCTGVQTAIEGNSLGQMPIIIA-GNDQQKKKYLGRM---TEEPlmCaYCVTE 126
Cdd:PRK13026 127 IPKEYGGKG---FSAyansTIVSKIATRSVSAAVTVMVPNSLGPGELLTHyGTQEQKDYWLPRLadgTEIP--C-FALTG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 127 PGAGSDVA-----GIKTKAEKKGDEYI---INGQKMWITNGGKANWYFLLAR-SDPDP--KAPANKAFTGFIVEADTPGI 195
Cdd:PRK13026 201 PEAGSDAGaipdtGIVCRGEFEGEEVLglrLTWDKRYITLAPVATVLGLAFKlRDPDGllGDKKELGITCALIPTDHPGV 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 196 QIGRKELNMGQRCSD--TRGivfEDVKVPKEnVLIGD----GAGFKVAMGAFDKTRPV-VAAGAVGLAQRALDEATKYAL 268
Cdd:PRK13026 281 EIGRRHNPLGMAFMNgtTRG---KDVFIPLD-WIIGGpdyaGRGWRMLVECLSAGRGIsLPALGTASGHMATRTTGAYAY 356
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 554506554 269 ERKTFGKLLVEHQAISFMLAEMAMK---VELARMSYQRAaweVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNG 344
Cdd:PRK13026 357 VRRQFGMPIGQFEGVQEALARIAGNtylLEAARRLTTTG---LDLGVKPSVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
101-273 |
9.45e-08 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 54.01 E-value: 9.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 101 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWItnGGKAN---WYFLLAR 170
Cdd:PLN02312 168 GTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTtyDPKTEEFVINtpcesAQKYWI--GGAANhatHTIVFSQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 171 SDPDPKAPANKAFTGFIVEAD---TPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------IGDG---------- 231
Cdd:PLN02312 246 LHINGKNEGVHAFIAQIRDQDgniCPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLnsvadvSPDGkyvsaikdpd 325
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 554506554 232 AGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTF 273
Cdd:PLN02312 326 QRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
101-344 |
1.21e-07 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 53.67 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 101 GNDQQKKKYLGRM---TEEPlmCaYCVTEPGAGSDVA-----GIKTKAEKKGDEYI---INGQKMWITNG------GKAn 163
Cdd:PRK09463 176 GTDEQKDHYLPRLargEEIP--C-FALTSPEAGSDAGsipdtGVVCKGEWQGEEVLgmrLTWNKRYITLApiatvlGLA- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 164 wyFLLarSDPDpkapankaftGFI------------VEADTPGIQIGRKELNMGQRCSD--TRGivfEDVKVPKENVlIG 229
Cdd:PRK09463 252 --FKL--YDPD----------GLLgdkedlgitcalIPTDTPGVEIGRRHFPLNVPFQNgpTRG---KDVFIPLDYI-IG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 230 D----GAGFKVAMGAFDKTR----PVVAAGAVGLAQRAldeATKYALERKTFGKLLVEHQAISFMLAEMAMKvelarmsy 301
Cdd:PRK09463 314 GpkmaGQGWRMLMECLSVGRgislPSNSTGGAKLAALA---TGAYARIRRQFKLPIGKFEGIEEPLARIAGN-------- 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 554506554 302 qraAWEVDSGRRNTYYA-----------SIAKAFAGDIANQLATDAVQILGGNG 344
Cdd:PRK09463 383 ---AYLMDAARTLTTAAvdlgekpsvlsAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
101-273 |
8.48e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 47.92 E-value: 8.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 101 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITN-GGKANWYFLLARSD 172
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506554 173 PDPKAPANKAFTGFIVEADT----PGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL-----IGDGAGF------KVA 237
Cdd:PTZ00460 190 VNGKNKGVHPFMVRIRDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikVSEDGQVerqgnpKVS 269
|
170 180 190
....*....|....*....|....*....|....*.
gi 554506554 238 MGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTF 273
Cdd:PTZ00460 270 YASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQF 305
|
|
| |
