|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-340 |
1.37e-40 |
|
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: 146.52 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 1 MDFVFDEDQEALADSVKRLLMTEMTPElIRELWATPtGRSDELWALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGY 80
Cdd:COG1960 1 MDFELTEEQRALRDEVREFAEEEIAPE-AREWDREG-EFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 81 FGSPEPL-LDTALVSAGVLARLPASDWRDALLRDIAEGRARVALV--------HPVNP------------------YAAD 133
Cdd:COG1960 79 ADASLALpVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFAltepgagsDAAALrttavrdgdgyvlngqktFITN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 134 VHVADTLLCehrgeLHRVDPAQCAWRT----VDSVDP----SRRLFTLDWEPS-------------AATRIASADEAAPL 192
Cdd:COG1960 159 APVADVILV-----LARTDPAAGHRGIslflVPKDTPgvtvGRIEDKMGLRGSdtgelffddvrvpAENLLGEEGKGFKI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 193 LNRALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIaDDHPQRA 272
Cdd:COG1960 234 AMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLL-DAGEDAA 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 273 VFVSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMK--RIWALSGswGDSAFHKARVADAILGDA 340
Cdd:COG1960 313 LEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRdaRILTIYE--GTNEIQRLIIARRLLGRP 380
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
187-333 |
2.67e-24 |
|
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: 101.21 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 187 DEAAPLLNRALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIAD 266
Cdd:cd00567 180 GGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ 259
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1144346276 267 DHPQRAVFVSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMKRIWALSGSWGDSAFHKARVA 333
Cdd:cd00567 260 GPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
196-336 |
2.40e-22 |
|
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: 91.55 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 196 ALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIADDHPQRAvFV 275
Cdd:pfam00441 10 TLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGA-EA 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1144346276 276 SHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMKRIWALSGSWGDSAFHKARVADAI 336
Cdd:pfam00441 89 SMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-316 |
2.53e-16 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 79.39 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 1 MDFVFDEDQEALADSVKRLLMTEMTPELIRElWATPTGRSDELWALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGY 80
Cdd:PRK12341 1 MDFSLTEEQELLLASIRELITRNFPEEYFRT-CDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 81 FGSPEPLLDTALVSAGVLARlpASDWRDALLRDIAEGRARVALVHPVN-PYA-ADVHVADTLLCEHRGELH--------- 149
Cdd:PRK12341 80 CGAPAFLITNGQCIHSMRRF--GSAEQLRKTAESTLETGDPAYALALTePGAgSDNNSATTTYTRKNGKVYlngqktfit 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 150 ---RVDPAQCAWRTVDSVDPsRRLFTLDWEPSAATRIASAD-----------------------------EAAPLLN--R 195
Cdd:PRK12341 158 gakEYPYMLVLARDPQPKDP-KKAFTLWWVDSSKPGIKINPlhkigwhmlstcevyldnveveesdlvgeEGMGFLNvmY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 196 ALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAiADDHPQRAVFV 275
Cdd:PRK12341 237 NFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQ-ADNGQSLRTSA 315
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1144346276 276 SHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQifmkRIW 316
Cdd:PRK12341 316 ALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVS----RFW 352
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-340 |
1.37e-40 |
|
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: 146.52 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 1 MDFVFDEDQEALADSVKRLLMTEMTPElIRELWATPtGRSDELWALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGY 80
Cdd:COG1960 1 MDFELTEEQRALRDEVREFAEEEIAPE-AREWDREG-EFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 81 FGSPEPL-LDTALVSAGVLARLPASDWRDALLRDIAEGRARVALV--------HPVNP------------------YAAD 133
Cdd:COG1960 79 ADASLALpVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFAltepgagsDAAALrttavrdgdgyvlngqktFITN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 134 VHVADTLLCehrgeLHRVDPAQCAWRT----VDSVDP----SRRLFTLDWEPS-------------AATRIASADEAAPL 192
Cdd:COG1960 159 APVADVILV-----LARTDPAAGHRGIslflVPKDTPgvtvGRIEDKMGLRGSdtgelffddvrvpAENLLGEEGKGFKI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 193 LNRALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIaDDHPQRA 272
Cdd:COG1960 234 AMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLL-DAGEDAA 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 273 VFVSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMK--RIWALSGswGDSAFHKARVADAILGDA 340
Cdd:COG1960 313 LEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRdaRILTIYE--GTNEIQRLIIARRLLGRP 380
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
187-333 |
2.67e-24 |
|
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: 101.21 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 187 DEAAPLLNRALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIAD 266
Cdd:cd00567 180 GGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ 259
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1144346276 267 DHPQRAVFVSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMKRIWALSGSWGDSAFHKARVA 333
Cdd:cd00567 260 GPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
196-336 |
2.40e-22 |
|
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: 91.55 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 196 ALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIADDHPQRAvFV 275
Cdd:pfam00441 10 TLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGA-EA 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1144346276 276 SHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMKRIWALSGSWGDSAFHKARVADAI 336
Cdd:pfam00441 89 SMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
196-313 |
2.09e-19 |
|
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: 88.09 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 196 ALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQaIADDHPQRAVFV 275
Cdd:cd01158 232 TLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAAR-LKDNGEPFIKEA 310
|
90 100 110
....*....|....*....|....*....|....*...
gi 1144346276 276 SHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMK 313
Cdd:cd01158 311 AMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYR 348
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
166-315 |
1.37e-17 |
|
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: 82.88 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 166 PSRRLFTLDWEPSAATRIASADEAAPLLNRALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLAD 245
Cdd:cd01162 202 PTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLAD 281
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 246 VAIRYEFARPVVARAAQAIADDHPQRAVFVSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQIFMKRI 315
Cdd:cd01162 282 MATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDL 351
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-316 |
2.53e-16 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 79.39 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 1 MDFVFDEDQEALADSVKRLLMTEMTPELIRElWATPTGRSDELWALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGY 80
Cdd:PRK12341 1 MDFSLTEEQELLLASIRELITRNFPEEYFRT-CDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 81 FGSPEPLLDTALVSAGVLARlpASDWRDALLRDIAEGRARVALVHPVN-PYA-ADVHVADTLLCEHRGELH--------- 149
Cdd:PRK12341 80 CGAPAFLITNGQCIHSMRRF--GSAEQLRKTAESTLETGDPAYALALTePGAgSDNNSATTTYTRKNGKVYlngqktfit 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 150 ---RVDPAQCAWRTVDSVDPsRRLFTLDWEPSAATRIASAD-----------------------------EAAPLLN--R 195
Cdd:PRK12341 158 gakEYPYMLVLARDPQPKDP-KKAFTLWWVDSSKPGIKINPlhkigwhmlstcevyldnveveesdlvgeEGMGFLNvmY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 196 ALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAiADDHPQRAVFV 275
Cdd:PRK12341 237 NFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQ-ADNGQSLRTSA 315
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1144346276 276 SHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQifmkRIW 316
Cdd:PRK12341 316 ALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVS----RFW 352
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
7-305 |
2.51e-14 |
|
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: 73.30 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 7 EDQEALADSVKRLLMTEMTPELIRelWATPTGRSDELWALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGYFG--SP 84
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHE--WEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGgsGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 85 EPLLDTALVSAgVLARLPASDWRDALLRDIAEGR--ARVALVHP-----------------------------VNPYAAD 133
Cdd:cd01160 79 GLSLHTDIVSP-YITRAGSPEQKERVLPQMVAGKkiGAIAMTEPgagsdlqgirttarkdgdhyvlngsktfiTNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 134 VH--VADT-----------LLCEHRGE--LHRVDP-AQCAWRTVDSVDpsrrLFTLDWEPSAATRIASADEAAPLLNRAL 197
Cdd:cd01160 158 VVivVARTggeargaggisLFLVERGTpgFSRGRKlKKMGWKAQDTAE----LFFDDCRVPAENLLGEENKGFYYLMQNL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 198 DHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQaiadDHPQRAVFVSH 277
Cdd:cd01160 234 PQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAW----RHEQGRLDVAE 309
|
330 340 350
....*....|....*....|....*....|.
gi 1144346276 278 AKLAAMSAAQLAAR---HAMQVHGAIGYTWE 305
Cdd:cd01160 310 ASMAKYWATELQNRvayECVQLHGGWGYMRE 340
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
204-313 |
1.22e-12 |
|
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: 68.38 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 204 VAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIaDDHPQRAVFVSHAKLAAM 283
Cdd:cd01157 244 VAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEV-DSGRRNTYYASIAKAFAA 322
|
90 100 110
....*....|....*....|....*....|
gi 1144346276 284 SAAQLAARHAMQVHGAIGYTWELDLQIFMK 313
Cdd:cd01157 323 DIANQLATDAVQIFGGNGFNSEYPVEKLMR 352
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
197-302 |
2.07e-11 |
|
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: 64.35 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 197 LDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIADDHPQRAVFVS 276
Cdd:cd01156 236 LDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAG 315
|
90 100
....*....|....*....|....*.
gi 1144346276 277 hAKLAAMSAAQLAARHAMQVHGAIGY 302
Cdd:cd01156 316 -VILYAAEKATQVALDAIQILGGNGY 340
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
6-84 |
1.91e-08 |
|
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: 51.70 E-value: 1.91e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1144346276 6 DEDQEALADSVKRLLMTEMTPeLIRELWATPTGrSDELWALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGYFGSP 84
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAP-HAAEWDEEGEF-PRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADAS 77
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
7-118 |
2.50e-08 |
|
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: 55.05 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 7 EDQEALADSVKRLLMTEMTPELIRELWAT--PTGRSDELW-ALFASQGLTAVSVPEAHGGLGLTEAEWALLAQAYGYFGS 83
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPELREESALGyrEGREDRRRWqRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1144346276 84 PEPLLDTALVSAG-VLARLPASDWRDALLRDIAEGR 118
Cdd:cd01152 81 PVPFNQIGIDLAGpTILAYGTDEQKRRFLPPILSGE 116
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
197-271 |
8.76e-08 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 53.34 E-value: 8.76e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1144346276 197 LDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIADDHPQR 271
Cdd:PLN02519 262 LDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDR 336
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
7-316 |
3.05e-07 |
|
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: 51.70 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 7 EDQEALADSVKRLLMTEMTPELIRELWATPTGRSDELWALfasqGLTAVSVPEAHGGLGLTEAEWALLAQAYGYFGSPEP 86
Cdd:cd01161 29 EELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKEL----GLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFSV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 87 LLDtALVSAGVLARLPAS--DWRDALLRDIAEGR--ARVALVHP-------------------------------VNPYA 131
Cdd:cd01161 105 TLG-AHQSIGFKGILLFGteAQKEKYLPKLASGEwiAAFALTEPssgsdaasirttavlsedgkhyvlngskiwiTNGGI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 132 ADVHV--ADTLLCEHRGELHRVDPAQCAWRTVDSVDPSRRLFTLDWEPSAATRIASADEAAPLLN-------------RA 196
Cdd:cd01161 184 ADIFTvfAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENvlgevgdgfkvamNI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 197 LDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAA-----QAIADDHPQR 271
Cdd:cd01161 264 LNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSgnmdrGLKAEYQIEA 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1144346276 272 AVfvshAKLAAMSAAQLAARHAMQVHGAIGYTWEL-------DLQIFmkRIW 316
Cdd:cd01161 344 AI----SKVFASEAAWLVVDEAIQIHGGMGFMREYgvervlrDLRIF--RIF 389
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
195-316 |
1.58e-06 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 49.55 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 195 RALDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIADDHPQRaVF 274
Cdd:PTZ00461 265 RNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNR-LG 343
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1144346276 275 VSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQifmkRIW 316
Cdd:PTZ00461 344 SDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVE----RLW 381
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
197-302 |
6.29e-06 |
|
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: 47.75 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 197 LDHGAFAvaaqlLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAA----QAIADD----H 268
Cdd:cd01154 275 LDNAVAA-----LGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAArafdRAAADKpveaH 349
|
90 100 110
....*....|....*....|....*....|....
gi 1144346276 269 PQRAvFVSHAKLAAMSAAQLAARHAMQVHGAIGY 302
Cdd:cd01154 350 MARL-ATPVAKLIACKRAAPVTSEAMEVFGGNGY 382
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
208-301 |
6.60e-05 |
|
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: 44.30 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 208 LLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIaDDHPQRAV--FVSHAKLAAMSA 285
Cdd:cd01155 263 LIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMI-DTVGNKAArkEIAMIKVAAPRM 341
|
90
....*....|....*.
gi 1144346276 286 AQLAARHAMQVHGAIG 301
Cdd:cd01155 342 ALKIIDRAIQVHGAAG 357
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
1-316 |
2.01e-04 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 42.90 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 1 MDFVFDEDQEALADSVKRLLMTEMTPELIRElwATPTGRSDELW-ALFASQGLTAVSVPEAHGGLGlteAEWALLAQAY- 78
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELMASENWEAYFAE--CDRDSVYPERFvKALADMGIDSLLIPEEHGGLD---AGFVTLAAVWm 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 79 --GYFGSPEPLLDTALVSAGVLARLPASDWRDALLRDIAEGRA--RVALVHPvnPYAADVHVADTLLCEHRGELH----- 149
Cdd:PRK03354 76 elGRLGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQmwNSAITEP--GAGSDVGSLKTTYTRRNGKVYlngsk 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 150 --RVDPAQCAWRTV---DSVDPSRRLFTlDW-------------EPSAATRIASADE----------------AAPLLNR 195
Cdd:PRK03354 154 cfITSSAYTPYIVVmarDGASPDKPVYT-EWfvdmskpgikvtkLEKLGLRMDSCCEitfddveldekdmfgrEGNGFNR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 196 A---LDHGAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAiADDHPQRA 272
Cdd:PRK03354 233 VkeeFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWK-ADNGTITS 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1144346276 273 VFVSHAKLAAMSAAQLAARHAMQVHGAIGYTWELDLQifmkRIW 316
Cdd:PRK03354 312 GDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRIS----RFW 351
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
210-320 |
1.96e-03 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 40.12 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 210 GLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPV---VARAAQAIADDHPQ--RAVFVSHAKLAAMS 284
Cdd:PRK11561 308 GLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALlfrLARAWDRRADAKEAlwARLFTPAAKFVICK 387
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1144346276 285 AAQLAARHAMQVHGAIGYTWELDL-----QIFMKRIWALSG 320
Cdd:PRK11561 388 RGIPFVAEAMEVLGGIGYCEESELprlyrEMPVNSIWEGSG 428
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
207-301 |
2.67e-03 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 39.78 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1144346276 207 QLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAIRYEFARPVVARAAQAIaDDHPQRAV--FVSHAKLAAMS 284
Cdd:PLN02876 686 RLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQL-DRLGNKKArgIIAMAKVAAPN 764
|
90
....*....|....*..
gi 1144346276 285 AAQLAARHAMQVHGAIG 301
Cdd:PLN02876 765 MALKVLDMAMQVHGAAG 781
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
193-248 |
6.09e-03 |
|
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: 38.11 E-value: 6.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1144346276 193 LNRAldhgAFAVAAQLLGLTQRVLDVAIDYSAQRKQFGKAIGSYQALKHLLADVAI 248
Cdd:cd01151 242 LNNA----RYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLT 293
|
|
| |
