|
Name |
Accession |
Description |
Interval |
E-value |
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
7-390 |
2.33e-168 |
|
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: 475.60 E-value: 2.33e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 7 EEQAMIRDMVRDFAESVLAPTCLDRDREQKAPLEEWRVFCEQtGLQGITISEEYGGSPVDDVSEAIIVEELARVDPSFSV 86
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAEL-GLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 87 MFCVHVGLCSKTIALHGNDEQKQKYLTRLAQSE-IGAYSLSEAGAGTDAAALGCKAKlsDDGAHYILNGEKMWVTNGASA 165
Cdd:cd01158 80 IVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEkIGAFALSEPGAGSDAAALKTTAK--KDGDDYVLNGSKMWITNGGEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 166 DIYVLFAKdVDHPefgvKKHGGTTAFIVEKSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVLKVPGDGFPIAMNA 245
Cdd:cd01158 158 DFYIVFAV-TDPS----KGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 246 LDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAKQRhyeddAPRHT 325
Cdd:cd01158 233 LDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDN-----GEPFI 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511215 326 MEASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRIVINRSIA 390
Cdd:cd01158 308 KEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLL 372
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-389 |
1.48e-157 |
|
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: 448.13 E-value: 1.48e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 1 MDFAEAEEQAMIRDMVRDFAESVLAPTCLDRDREQKAPLEEWRVFCEQtGLQGITISEEYGGSPVDDVSEAIIVEELARV 80
Cdd:COG1960 1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAEL-GLLGLTIPEEYGGLGLSLVELALVLEELARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 81 DPSFSVMFCVHVGlCSKTIALHGNDEQKQKYLTRLAQSE-IGAYSLSEAGAGTDAAALGCKAKlsDDGAHYILNGEKMWV 159
Cdd:COG1960 80 DASLALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEwIGAFALTEPGAGSDAAALRTTAV--RDGDGYVLNGQKTFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 160 TNGASADIYVLFAKDVDHPefgvkKHGGTTAFIVEKSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVLKVPGDGF 239
Cdd:COG1960 157 TNAPVADVILVLARTDPAA-----GHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 240 PIAMNALDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAKqrhyeD 319
Cdd:COG1960 232 KIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLL-----D 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 320 DAPRHTMEASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRIVINRSI 389
Cdd:COG1960 307 AGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRL 376
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
7-389 |
9.53e-123 |
|
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: 359.80 E-value: 9.53e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 7 EEQAMIRDMVRDFAESVLAPTCLDRDREQKAPLEEWRVFCEQtGLQGITISEEYGGSPVDDVSEAIIVEELARVDPSFSV 86
Cdd:cd01156 4 DEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKL-GLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 87 MFCVHVGLCSKTIALHGNDEQKQKYLTRLAQSE-IGAYSLSEAGAGTDAAALGCKAKLSDDgaHYILNGEKMWVTNGASA 165
Cdd:cd01156 83 SYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEhIGALAMSEPNAGSDVVSMKLRAEKKGD--RYVLNGSKMWITNGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 166 DIYVLFAKDvdHPEFGVKkhgGTTAFIVEKSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVLKVPGDGFPIAMNA 245
Cdd:cd01156 161 DTLVVYAKT--DPSAGAH---GITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 246 LDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAKQRHYEDdaprhT 325
Cdd:cd01156 236 LDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMD-----P 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511215 326 MEASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRIVINRSI 389
Cdd:cd01156 311 KDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGREL 374
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
7-387 |
5.53e-112 |
|
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: 330.40 E-value: 5.53e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 7 EEQAMIRDMVRDFAESVLAPTCLDRDREQKAPLEEWRvfceQTGLQgitiseeyggspvddvseaiiveelarvdpsfsv 86
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLA----ELGLL---------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 87 mfcvhvgLCSKTIALHGNDEQKQKYLTRLAQSE-IGAYSLSEAGAGTDAAALGCKAKLSDDGahYILNGEKMWVTNGASA 165
Cdd:cd00567 43 -------LGAALLLAYGTEEQKERYLPPLASGEaIAAFALTEPGAGSDLAGIRTTARKDGDG--YVLNGRKIFISNGGDA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 166 DIYVLFAKDVDHPefgvKKHGGTTAFIVEKSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVLKVPGDGFPIAMNA 245
Cdd:cd00567 114 DLFIVLARTDEEG----PGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 246 LDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAkqrhYEDDAPRHT 325
Cdd:cd00567 190 LNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWL----LDQGPDEAR 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511215 326 MEASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRIVINR 387
Cdd:cd00567 266 LEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
1-390 |
1.54e-109 |
|
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: 327.12 E-value: 1.54e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 1 MDFAEAEEQAMIRDMVRDFAESVLAPTCLDR-DREQKAPLEEWRvfceQTGLQGITISEEYGGSPVDDVSEAIIVEELAR 79
Cdd:cd01161 23 LTEEQTEELNMLVGPVEKFFEEVNDPAKNDQlEKIPRKTLTQLK----ELGLFGLQVPEEYGGLGLNNTQYARLAEIVGM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 80 vDPSFSVMFCVHVGLCSKTIALHGNDEQKQKYLTRLAQSE-IGAYSLSEAGAGTDAAALGCKAKLSDDGAHYILNGEKMW 158
Cdd:cd01161 99 -DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEwIAAFALTEPSSGSDAASIRTTAVLSEDGKHYVLNGSKIW 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 159 VTNGASADIYVLFAK-DVDHPEFGVKKHggTTAFIVEKSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVLKVPGD 237
Cdd:cd01161 178 ITNGGIADIFTVFAKtEVKDATGSVKDK--ITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 238 GFPIAMNALDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAKQRHY 317
Cdd:cd01161 256 GFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGL 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511215 318 eddAPRHTMEASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRIVINRSIA 390
Cdd:cd01161 336 ---KAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGL 405
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
7-392 |
1.43e-108 |
|
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: 323.63 E-value: 1.43e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 7 EEQAMIRDMVRDFAESVLAPTCLDRDREQKAPLEEWRVFCEQtGLQGITISEEYGGSPVDDVSEAIIVEELARVDPSFSV 86
Cdd:cd01162 3 EEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAEL-GFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 87 MFCVHvGLCSKTIALHGNDEQKQKYLTRLAQSE-IGAYSLSEAGAGTDAAALGCKAKLsdDGAHYILNGEKMWVTNGASA 165
Cdd:cd01162 82 YISIH-NMCAWMIDSFGNDEQRERFLPDLCTMEkLASYCLTEPGSGSDAAALRTRAVR--EGDHYVLNGSKAFISGAGDS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 166 DIYVLFAKDvdhpefGVKKHGGTTAFIVEKSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVLKVPGDGFPIAMNA 245
Cdd:cd01162 159 DVYVVMART------GGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 246 LDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAKQRhyedDAPRHT 325
Cdd:cd01162 233 LNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDR----GDPDAV 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663511215 326 MEASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRIVINRSIAPE 392
Cdd:cd01162 309 KLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
7-387 |
7.35e-99 |
|
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: 298.73 E-value: 7.35e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 7 EEQAMIRDMVRDFAESVLAPTCLDRDREQKAPLEEWRVFCEqTGLQGITISEEYGGSPVDDVSEAIIVEELARvdPSFSV 86
Cdd:cd01157 3 EQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWE-LGLMNTHIPEDCGGLGLGTFDTCLITEELAY--GCTGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 87 MFCVHV-GLCSKTIALHGNDEQKQKYLTRLAQSE-IGAYSLSEAGAGTDAAalGCKAKLSDDGAHYILNGEKMWVTNGAS 164
Cdd:cd01157 80 QTAIEAnSLGQMPVIISGNDEQKKKYLGRMTEEPlMCAYCVTEPGAGSDVA--GIKTKAEKKGDEYIINGQKMWITNGGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 165 ADIYVLFAKDVDHPEFGVKKhgGTTAFIVEKSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVLKVPGDGFPIAMN 244
Cdd:cd01157 158 ANWYFLLARSDPDPKCPASK--AFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 245 ALDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAKqrhyeDDAPRH 324
Cdd:cd01157 236 AFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEV-----DSGRRN 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511215 325 TMEASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRIVINR 387
Cdd:cd01157 311 TYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISR 373
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
7-389 |
1.15e-98 |
|
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: 298.26 E-value: 1.15e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 7 EEQAMIRDMVRDFAESVLAPTCLDRDREQKAPLEEWRVFCEQtGLQGITISEEYGGSPVDDVSEAIIVEELARVDpSFSV 86
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQ-GLLGVGFPEEYGGIGGDLLSAAVLWEELARAG-GSGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 87 MFCVHVGLCSKTIALHGNDEQKQKYLTRLAQSE-IGAYSLSEAGAGTDAAALGCKAKlsDDGAHYILNGEKMWVTNGASA 165
Cdd:cd01160 79 GLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKkIGAIAMTEPGAGSDLQGIRTTAR--KDGDHYVLNGSKTFITNGMLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 166 DIYVLFAKdVDHPEFGvkkHGGTTAFIVEKSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVLKVPGDGFPIAMNA 245
Cdd:cd01160 157 DVVIVVAR-TGGEARG---AGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 246 LDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWakqRHYEDDAPrhT 325
Cdd:cd01160 233 LPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAW---RHEQGRLD--V 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511215 326 MEASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRIVINRSI 389
Cdd:cd01160 308 AEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
2-392 |
7.19e-90 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 276.76 E-value: 7.19e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 2 DFAEAEEQAMIRDMVRDFAESVLAPTCLDRDREQKAPLEE--WRVFCEqTGLQGITISEEYGGSPVDDVSEAIIVEELAR 79
Cdd:PLN02519 23 SLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGD-FNLHGITAPEEYGGLGLGYLYHCIAMEEISR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 80 VDPSFSVMFCVHVGLCSKTIALHGNDEQKQKYLTRLAQSE-IGAYSLSEAGAGTDAAALGCKAKLSDDGahYILNGEKMW 158
Cdd:PLN02519 102 ASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEhVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 159 VTNGASADIYVLFAKDvdHPEFGVKkhgGTTAFIVEKSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVLKVPGDG 238
Cdd:PLN02519 180 CTNGPVAQTLVVYAKT--DVAAGSK---GITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 239 FPIAMNALDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAKQRHYE 318
Cdd:PLN02519 255 VYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKV 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511215 319 DDAprhtmEASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRIVINRSIAPE 392
Cdd:PLN02519 335 DRK-----DCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
7-389 |
2.04e-85 |
|
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: 264.61 E-value: 2.04e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 7 EEQAMIRDMVRDFAESVLAPTCLDRDREQKAPLEEWRVFCEqTGLQGITIsEEYGGSPVDDVSEAIIVEELARVDPSFSV 86
Cdd:cd01151 15 EEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGE-LGLLGATI-KGYGCAGLSSVAYGLIAREVERVDSGYRS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 87 MFCVHVGLCSKTIALHGNDEQKQKYLTRLAQSE-IGAYSLSEAGAGTDAAALGCKAKlsDDGAHYILNGEKMWVTNGASA 165
Cdd:cd01151 93 FMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGElIGCFGLTEPNHGSDPGGMETRAR--KDGGGYKLNGSKTWITNSPIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 166 DIYVLFAKDVDHpefgvkkhGGTTAFIVEKSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVLkvPG-DGFPIAMN 244
Cdd:cd01151 171 DVFVVWARNDET--------GKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL--PGaEGLRGPFK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 245 ALDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMvykaAWAKQRHYedDAPRH 324
Cdd:cd01151 241 CLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLA----CLRVGRLK--DQGKA 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511215 325 TME-ASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRIVINRSI 389
Cdd:cd01151 315 TPEqISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAI 380
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
8-379 |
2.55e-77 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 244.85 E-value: 2.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 8 EQAMIRDMVRDFAESVLAPTCLDRDREQKAPLEEWRVFCEqTGLQGITISEEYGGSPVDDVSEAIIVEELARVDPSFSVM 87
Cdd:PTZ00461 40 EHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGD-LGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 88 FCVHVGLCSKTIALHGNDEQKQKYLTRLAQSE-IGAYSLSEAGAGTDAAALGCKAKLSDDGaHYILNGEKMWVTNGASAD 166
Cdd:PTZ00461 119 YLAHSMLFVNNFYYSASPAQRARWLPKVLTGEhVGAMGMSEPGAGTDVLGMRTTAKKDSNG-NYVLNGSKIWITNGTVAD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 167 IYVLFAKdVDhpefgvkkhGGTTAFIVEKSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVLKVPGDGFPIAMNAL 246
Cdd:PTZ00461 198 VFLIYAK-VD---------GKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 247 DNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAwakqrHYEDDAPRHTM 326
Cdd:PTZ00461 268 ELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVS-----HNVHPGNKNRL 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 663511215 327 EASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQE 379
Cdd:PTZ00461 343 GSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-389 |
4.79e-66 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 214.59 E-value: 4.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 1 MDFAEAEEQ----AMIRD-MVRDFAESVLApTCldrDREQKAPLEEWRVFCEqTGLQGITISEEYGGSPVDDVSEAIIVE 75
Cdd:PRK12341 1 MDFSLTEEQelllASIRElITRNFPEEYFR-TC---DENGTYPREFMRALAD-NGISMLGVPEEFGGTPADYVTQMLVLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 76 ELARVDPSFsvmFCVHVGLCSKTIALHGNDEQKQKYLTRLAQSEIGAYSL--SEAGAGTDAAALGCKAKlSDDGAHYiLN 153
Cdd:PRK12341 76 EVSKCGAPA---FLITNGQCIHSMRRFGSAEQLRKTAESTLETGDPAYALalTEPGAGSDNNSATTTYT-RKNGKVY-LN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 154 GEKMWVTNGASADIYVLFAKDVDHPEfgvkKHGGTTAFIVEKSFEGFSVGKKEdKLGIRSSDTCSLLLDSCKVPVENVLK 233
Cdd:PRK12341 151 GQKTFITGAKEYPYMLVLARDPQPKD----PKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 234 VPGDGFPIAMNALDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAK 313
Cdd:PRK12341 226 EEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQA 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511215 314 qrhyeDDAPRHTMEASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRIVINRSI 389
Cdd:PRK12341 306 -----DNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQI 376
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
236-389 |
3.25e-59 |
|
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: 189.00 E-value: 3.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 236 GDGFPIAMNALDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAKqr 315
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEAL-- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511215 316 hyeDDAPRHTMEASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRIVINRSI 389
Cdd:pfam00441 79 ---DAGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
14-381 |
1.55e-57 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 192.99 E-value: 1.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 14 DMVRDFAESVLAPTCLDRDREQ--------KAP---LEEWRVFCEqTGLQGITISEEYGGSPVDDVSEAIIVEELARVDP 82
Cdd:cd01153 3 EEVARLAENVLAPLNADGDREGpvfddgrvVVPppfKEALDAFAE-AGWMALGVPEEYGGQGLPITVYSALAEIFSRGDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 83 SFSVMFCVHVGLCskTIALHGNDEQKQKYLTRLAQSE-IGAYSLSEAGAGTDAAALGCKAKLSDDGAHYIlNGEKMWVTN 161
Cdd:cd01153 82 PLMYASGTQGAAA--TLLAHGTEAQREKWIPRLAEGEwTGTMCLTEPDAGSDLGALRTKAVYQADGSWRI-NGVKRFISA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 162 GASAD----IYVLFAKDVDHPEfGVKkhgGTTAFIVEK-----SFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVenvL 232
Cdd:cd01153 159 GEHDMseniVHLVLARSEGAPP-GVK---GLSLFLVPKflddgERNGVTVARIEEKMGLHGSPTCELVFDNAKGEL---I 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 233 KVPGDGFPIAMNALDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKP--------IAYHQSIGNILADMATRTEAARL 304
Cdd:cd01153 232 GEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLikaapavtIIHHPDVRRSLMTQKAYAEGSRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 305 MV-YKAAW---AKQRHYEDDAPRHTMEAS-----MAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYE 375
Cdd:cd01153 312 LDlYTATVqdlAERKATEGEDRKALSALAdlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYE 391
|
....*.
gi 663511215 376 GTQEVQ 381
Cdd:cd01153 392 GTTGIQ 397
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
2-389 |
4.31e-53 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 181.59 E-value: 4.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 2 DFAEAEEQAmIRDMVRDFAESVLAPTCLDRDREQKAPLEEWRVFcEQTGLQGITIsEEYGGSPVDDVSEAIIVEELARVD 81
Cdd:PLN02526 27 DLLTPEEQA-LRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKL-GSLGIAGGTI-KGYGCPGLSITASAIATAEVARVD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 82 PSFSVMFCVHVGLCSKTIALHGNDEQKQKYLTRLAQ-SEIGAYSLSEAGAGTDAAALGCKAKLSDDGahYILNGEKMWVT 160
Cdd:PLN02526 104 ASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQlDTVACWALTEPDYGSDASSLNTTATKVEGG--WILNGQKRWIG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 161 NGASADIYVLFAKDVDHPEFgvkkhggtTAFIVEKSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENvlKVPG-DGF 239
Cdd:PLN02526 182 NSTFADVLVIFARNTTTNQI--------NGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDED--RLPGvNSF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 240 PIAMNALDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMvykaAWAKQRHYED 319
Cdd:PLN02526 252 QDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLV----GWRLCKLYES 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511215 320 D--APRHtmeASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRIVINRSI 389
Cdd:PLN02526 328 GkmTPGH---ASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
1-389 |
1.17e-51 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 176.95 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 1 MDFAEAEEQAMIRDMVRDFAESVLAPTCLDR-DREQKAPLEEWRVFCEqTGLQGITISEEYGGSPVDDVSEAIIVEELAR 79
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELMASENWEAYFAEcDRDSVYPERFVKALAD-MGIDSLLIPEEHGGLDAGFVTLAAVWMELGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 80 VDPSFSVMFCVHVGLcsKTIALHGNDEQKQKYLTRLAQSE-IGAYSLSEAGAGTDAAALGCKAKlSDDGAHYiLNGEKMW 158
Cdd:PRK03354 80 LGAPTYVLYQLPGGF--NTFLREGTQEQIDKIMAFRGTGKqMWNSAITEPGAGSDVGSLKTTYT-RRNGKVY-LNGSKCF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 159 VTNGASADIYVLFAKDVDHPEFGVkkhggTTAFIVEKSFEGFSVGKKEdKLGIRSSDTCSLLLDSCKVPVENVLKVPGDG 238
Cdd:PRK03354 156 ITSSAYTPYIVVMARDGASPDKPV-----YTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 239 FPIAMNALDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAkqrhyE 318
Cdd:PRK03354 230 FNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWK-----A 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663511215 319 DDAPRHTMEASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRIVINRSI 389
Cdd:PRK03354 305 DNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAV 375
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
7-389 |
2.33e-47 |
|
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: 165.60 E-value: 2.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 7 EEQAMIRDMVRDFAESVLAPTCL----DRDREQKAPLEEWRVFCEQTGLQGITISEEYGGSPVDDVSEAIIVEELARVD- 81
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPELReesaLGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 82 PSfsVMFCVHVGLCSKTIALHGNDEQKQKYLTRLAQSE-IGAYSLSEAGAGTDAAALGCKAklSDDGAHYILNGEKMWVT 160
Cdd:cd01152 81 PV--PFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEeIWCQGFSEPGAGSDLAGLRTRA--VRDGDDWVVNGQKIWTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 161 NGASAD-IYVLFAKDVDhpefgVKKHGGTTAFIVEKSFEGFSVGKKEDKLGirSSDTCSLLLDSCKVPVENVLKVPGDGF 239
Cdd:cd01152 157 GAHYADwAWLLVRTDPE-----APKHRGISILLVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGW 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 240 PIAMNALDNSRIGIAaqalGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAKQRHYED 319
Cdd:cd01152 230 KVAMTTLNFERVSIG----GSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPP 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511215 320 DAprhtmEASMAKLFAGDTAMWVAERAVQVLG-----GYGYTTDF---PVERFFRDAKITQIYEGTQEVQRIVINRSI 389
Cdd:cd01152 306 GA-----EASIAKLFGSELAQELAELALELLGtaallRDPAPGAElagRWEADYLRSRATTIYGGTSEIQRNIIAERL 378
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
105-381 |
9.29e-43 |
|
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: 154.45 E-value: 9.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 105 DEQKQKYLTRLAQSE-----IGAYSLSEAGAGTDAAALGCKAKLSDDGAhYILNGEKmWVTNGASADIYVLFAKDVDHPE 179
Cdd:cd01154 128 PEELKQYLPGLLSDRyktglLGGTWMTEKQGGSDLGANETTAERSGGGV-YRLNGHK-WFASAPLADAALVLARPEGAPA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 180 fgvkKHGGTTAFIVEKSFE-----GFSVGKKEDKLGIRSSDTCSLLLDSCkvpVENVLKVPGDGFPIAMNALDNSRIGIA 254
Cdd:cd01154 206 ----GARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 255 AQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAKQRHyEDDAPRHTMEA----SM 330
Cdd:cd01154 279 VAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRA-AADKPVEAHMArlatPV 357
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 663511215 331 AKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQ 381
Cdd:cd01154 358 AKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
7-116 |
1.00e-38 |
|
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: 134.51 E-value: 1.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 7 EEQAMIRDMVRDFAESVLAPTCLDRDREQKAPLEEWRVFCEQtGLQGITISEEYGGSPVDDVSEAIIVEELARVDPSFSV 86
Cdd:pfam02771 2 EEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGEL-GLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|
gi 663511215 87 MFCVHVGLCSKTIALHGNDEQKQKYLTRLA 116
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLA 110
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
30-390 |
1.37e-37 |
|
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: 139.83 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 30 DRDREQKAPLEEWRVFCEQTGLQGITISEEYGGSPVDDVSEAIIVEELARvdpSFsvmFCVHVGLCS-------KTIALH 102
Cdd:cd01155 34 DRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGR---SF---FAPEVFNCQapdtgnmEVLHRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 103 GNDEQKQKYLTRLAQSEI-GAYSLSEAG-AGTDAAALGCKakLSDDGAHYILNGEKMWvTNGAS---ADIYVLFAKdVDH 177
Cdd:cd01155 108 GSEEQKKQWLEPLLDGKIrSAFAMTEPDvASSDATNIECS--IERDGDDYVINGRKWW-SSGAGdprCKIAIVMGR-TDP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 178 PefGVKKHGGTTAFIVEKSFEGFsvgKKEDKLGIRSSDT-----CSLLLDSCKVPVENVLKVPGDGFPIAMNALDNSRIG 252
Cdd:cd01155 184 D--GAPRHRQQSMILVPMDTPGV---TIIRPLSVFGYDDaphghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIH 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 253 IAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAKQRHYEDDApRHtmEASMAK 332
Cdd:cd01155 259 HCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAA-RK--EIAMIK 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 663511215 333 LFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRivinRSIA 390
Cdd:cd01155 336 VAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHL----RSIA 389
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
40-391 |
1.15e-30 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 123.44 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 40 EEWRVFCEQtGLQGITISEEYGGSPVDDVSEAIIVEELARVDPSFSVMFCVHVGLCsKTIALHGNDEQKQKYLTRLAQSE 119
Cdd:PTZ00456 103 EAYQALKAG-GWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAA-NTLMAWGSEEQKEQYLTKLVSGE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 120 -IGAYSLSEAGAGTDAAALGCKAKLSDDGAhYILNGEKMWVTNG----ASADIYVLFAKDVDHPEFGVkkhgGTTAFIVE 194
Cdd:PTZ00456 181 wSGTMCLTEPQCGTDLGQVKTKAEPSADGS-YKITGTKIFISAGdhdlTENIVHIVLARLPNSLPTTK----GLSLFLVP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 195 K-------SFE---GFSVGKKEDKLGIRSSDTCSLLLDSckvPVENVLKVPGDGFPIAMNALDNSRIGIAAQALGIAQGA 264
Cdd:PTZ00456 256 RhvvkpdgSLEtakNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 265 YESALGYAHER------------EAFGKPIAYHQSIG-NILADMATrTEAARLMVYKAAWAKQRHYE--DDAPRHTMEAS 329
Cdd:PTZ00456 333 FQNALRYARERrsmralsgtkepEKPADRIICHANVRqNILFAKAV-AEGGRALLLDVGRLLDIHAAakDAATREALDHE 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663511215 330 M------AKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEVQRI-VINRSIAP 391
Cdd:PTZ00456 412 IgfytpiAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVLS 480
|
|
| sulfur_SfnB |
TIGR04022 |
sulfur acquisition oxidoreductase, SfnB family; Members of this protein family belong to the ... |
4-370 |
3.77e-28 |
|
sulfur acquisition oxidoreductase, SfnB family; Members of this protein family belong to the greater family of acyl-CoA dehydrogenases. This family includes the sulfate starvation induced protein SfnB of Pseudomonas putida strain DS1, which is both encoded nearby to and phylogenetically closely correlated with the dimethyl sulphone monooxygenase SfnG. This family shows considerable sequence similarity to the Rhodococcus dibenzothiophene desulfurization enzyme DszC, although that enzyme falls outside of the scope of this family. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 274924 [Multi-domain] Cd Length: 391 Bit Score: 113.90 E-value: 3.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 4 AEAEEQAmirdmvRDFAESvLAPTCLDRDREQKAPLEEWRVFcEQTGLQGITISEEYGGSPVDDVSEAIIVEELARVDPS 83
Cdd:TIGR04022 8 AEALEIA------RRLAAE-FAPGAAERDRERRLPWAELDAF-SQSGLWGITVPRAYGGAGVSYATLAEVIAIISAADPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 84 FSVMFCVHVGLCSkTIALHGNDEQKQKYLTRLAQSEIGAYSLSEAGAGTdaaALGCKAKLSDDGAHYILNGEKMWVTnGA 163
Cdd:TIGR04022 80 LGQIPQNHFYALE-VLRLTGSEEQKRFFFGEVLAGERFGNAFSERGTRN---VLDFQTRLRRDGDGYRLNGRKFYST-GA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 164 sadiyvLFAKDVdhPEFGVKKHGGTTAFIVEKSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVlkVPG-DGF--P 240
Cdd:TIGR04022 155 ------LFAHWI--PVLALDDEGRAVLAFVPRDAPGLTVIDDWSGFGQRTTASGTVLLDDVRVPAEHV--VPIqRAFdrP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 241 IAMNALdnSRIGIAAQALGIAQGAYESALGYAHER----------EAFGKPIAYHQsigniLADMATRTEAARLMVYKAA 310
Cdd:TIGR04022 225 TAAGPV--AQIIHAAIDAGIARAALADTLAFVRERarpwidsgveRASDDPLTIAE-----VGDLAIRLHAAEALLERAG 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511215 311 WAKQRHYEDDAPRHTMEASM----AKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKI 370
Cdd:TIGR04022 298 RAVDAARAEPTEESVAAASIavaeAKVLTTEIALLAASKLFELAGTRSTLAEHNLDRHWRNART 361
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
252-379 |
2.75e-27 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 105.12 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 252 GIAAQALGIAQGAYESALGYAHERE--AFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAKQRHYEDDAP---RHTM 326
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKPvtpALRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 663511215 327 EASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQE 379
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
122-222 |
4.44e-24 |
|
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: 95.04 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 122 AYSLSEAGAGTDAAALGCKAKLSDDGaHYILNGEKMWVTNGASADIYVLFAKDVdhpefGVKKHGGTTAFIVEKSFEGFS 201
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGG-GWVLNGTKWWITNAGIADLFLVLARTG-----GDDRHGGISLFLVPKDAPGVS 74
|
90 100
....*....|....*....|.
gi 663511215 202 VGKKEDKLGIRSSDTCSLLLD 222
Cdd:pfam02770 75 VRRIETKLGVRGLPTGELVFD 95
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
102-380 |
1.03e-20 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 94.09 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 102 HGNDEQKQKYLTRLAQSEI-GAYSLSEAG-AGTDAAALGCKakLSDDGAHYILNGEKMWvTNGA---SADIYVLFAKDvd 176
Cdd:PLN02876 532 YGNKEQQLEWLIPLLEGKIrSGFAMTEPQvASSDATNIECS--IRRQGDSYVINGTKWW-TSGAmdpRCRVLIVMGKT-- 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 177 hpEFGVKKHGGTTAFIVEKSFEGFSVGKKEDKLGIRSS--DTCSLLLDSCKVPVENVLKVPGDGFPIAMNALDNSRIGIA 254
Cdd:PLN02876 607 --DFNAPKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHC 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 255 AQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMATRTEAARLMVYKAAWAKQRHYEDDApRHTMeaSMAKLF 334
Cdd:PLN02876 685 MRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLGNKKA-RGII--AMAKVA 761
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 663511215 335 AGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAKITQIYEGTQEV 380
Cdd:PLN02876 762 APNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
17-369 |
8.62e-19 |
|
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: 86.99 E-value: 8.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 17 RDFAE--SVLAPTCLDRDREQKAPLEEWRVFcEQTGLQGITISEEYGGSPVDDVSEAIIVEELARVDPSFSVMFCVHVGL 94
Cdd:cd01163 1 ARARPlaARIAEGAAERDRQRGLPYEEVALL-RQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 95 cSKTIALHGNDEQKQKYLTRLAQSEIGAYSLSEAGAGTDAAALgckAKLSDDGAHYILNGEKMWVTNGASADIYVLFAKD 174
Cdd:cd01163 80 -VEALLLAGPEQFRKRWFGRVLNGWIFGNAVSERGSVRPGTFL---TATVRDGGGYVLNGKKFYSTGALFSDWVTVSALD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 175 VDhpefgvkkhGGTTAFIVEKSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVLKVPGDGFPIAMNALdNSRIGIA 254
Cdd:cd01163 156 EE---------GKLVFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 255 AQALGIAQGAYESALGYAHEReafGKPIAY------------HQSIGnilaDMATRTEAARLMVYKAAWAKQRHYEDDA- 321
Cdd:cd01163 226 AVLAGIARAALDDAVAYVRSR---TRPWIHsgaesarddpyvQQVVG----DLAARLHAAEALVLQAARALDAAAAAGTa 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 663511215 322 --PRHTMEASM----AKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDAK 369
Cdd:cd01163 299 ltAEARGEAALavaaAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
49-260 |
4.83e-15 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 76.46 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 49 TGLQGITISEEYGGSPVDDVSEAIIVEELARVDPSFSVMFCVHVGLCSKTIALHGNDEQKQKYLTRLAQSEIGAYSLSEA 128
Cdd:PTZ00457 63 GNLYGARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWATEE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 129 GAGTDAAALGCKAKLSDDGAhYILNGEKMWVtNGASADIYVLFAKDVDH--PEFGVKKHGGTTAFIVEKSFEGFSVgkke 206
Cdd:PTZ00457 143 GCGSDISMNTTKASLTDDGS-YVLTGQKRCE-FAASATHFLVLAKTLTQtaAEEGATEVSRNSFFICAKDAKGVSV---- 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 663511215 207 dklgirSSDTCSLLldscKVPVENVLKVPGDGFPIAMNALDNSRIGIAAQALGI 260
Cdd:PTZ00457 217 ------NGDSVVFE----NTPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGI 260
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
6-306 |
4.23e-11 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 64.59 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 6 AEEQAMIR-------DMVRDFaESVLAptclDRDreqkAPLEEWRVFCEQtGLQGITISEEYGGSPVDDVSEAIIVEELA 78
Cdd:PRK13026 80 AEEQAFIDnevetllTMLDDW-DIVQN----RKD----LPPEVWDYLKKE-GFFALIIPKEYGGKGFSAYANSTIVSKIA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 79 --RVDPSFSVMfcVHVGLCSKTIALH-GNDEQKQKYLTRLAQ-SEIGAYSLSEAGAGTDAAALG-----CKAKLsdDGAH 149
Cdd:PRK13026 150 trSVSAAVTVM--VPNSLGPGELLTHyGTQEQKDYWLPRLADgTEIPCFALTGPEAGSDAGAIPdtgivCRGEF--EGEE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 150 YI---LNGEKMWVTNGASADIYVLFAKDVDhPE--FGVKKHGGTTAFIVEKSFEGFSVGKKEDKLG-------IRSSDTC 217
Cdd:PRK13026 226 VLglrLTWDKRYITLAPVATVLGLAFKLRD-PDglLGDKKELGITCALIPTDHPGVEIGRRHNPLGmafmngtTRGKDVF 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 218 sllldsckVPVENVLKVP---GDGFPIAMNALDNSRiGIAAQALGIAQG--AYESALGYAHEREAFGKPIAYHQSIGNIL 292
Cdd:PRK13026 305 --------IPLDWIIGGPdyaGRGWRMLVECLSAGR-GISLPALGTASGhmATRTTGAYAYVRRQFGMPIGQFEGVQEAL 375
|
330
....*....|....*..
gi 663511215 293 ADMATRT---EAARLMV 306
Cdd:PRK13026 376 ARIAGNTyllEAARRLT 392
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
125-377 |
5.41e-11 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 64.00 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 125 LSEAGAGTDAAALGCKAKLSDDGAhYILNGEKmWVTNGASADIYVLFAKdvdhpefgvkKHGGTTAFIVEK-----SFEG 199
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLADGS-YRLVGHK-WFFSVPQSDAHLVLAQ----------AKGGLSCFFVPRflpdgQRNA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 200 FSVGKKEDKLGIRSSDtcsllldSCKVPVEN----VLKVPGDGFPIAMNALDNSRIGIAAQALGIAQGAYESALGYAHER 275
Cdd:PRK11561 252 IRLERLKDKLGNRSNA-------SSEVEFQDaigwLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQR 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 276 EAFGKPIAYHQSIGNILADMATRTEA--ARLMVYKAAWakqrhyedDAPRHTMEASMAKLFA--------GDTAMWVAEr 345
Cdd:PRK11561 325 QVFGKPLIEQPLMRQVLSRMALQLEGqtALLFRLARAW--------DRRADAKEALWARLFTpaakfvicKRGIPFVAE- 395
|
250 260 270
....*....|....*....|....*....|..
gi 663511215 346 AVQVLGGYGYTTDFPVERFFRDAKITQIYEGT 377
Cdd:PRK11561 396 AMEVLGGIGYCEESELPRLYREMPVNSIWEGS 427
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
6-305 |
6.29e-10 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 60.99 E-value: 6.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 6 AEEQAMIR-------DMVRDFAESVlaptcldrdREQKAPLEEWRvFCEQTGLQGITISEEYGGSPVDDVSEAIIVEELA 78
Cdd:PRK09463 81 AEEQAFLDgpveelcRMVNDWQITH---------ELADLPPEVWQ-FIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 79 RVDPSFSVMFCVHVGLCSKTIALH-GNDEQKQKYLTRLAQ-SEIGAYSLSEAGAGTDAAAL---G--CKAKLSDDGAHYI 151
Cdd:PRK09463 151 SRSGTLAVTVMVPNSLGPGELLLHyGTDEQKDHYLPRLARgEEIPCFALTSPEAGSDAGSIpdtGvvCKGEWQGEEVLGM 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 152 -LNGEKMWVTNGASADIYVLFAKDVDhPE--FGVKKHGGTTAFIVEKSFEGFSVGKKEDKLG-------IRSSDTCslll 221
Cdd:PRK09463 231 rLTWNKRYITLAPIATVLGLAFKLYD-PDglLGDKEDLGITCALIPTDTPGVEIGRRHFPLNvpfqngpTRGKDVF---- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 222 dsckVPVENVL---KVPGDGFPIAMNALDNSR-IGIAAQALGIAQGAYESALGYAHEREAFGKPIAYHQSIGNILADMAT 297
Cdd:PRK09463 306 ----IPLDYIIggpKMAGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAG 381
|
330
....*....|.
gi 663511215 298 RT---EAARLM 305
Cdd:PRK09463 382 NAylmDAARTL 392
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
73-376 |
1.01e-07 |
|
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: 53.87 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 73 IVEELARVDPSFSVMFCVHVGLCSKTIALHGNDEQKQKYL-TRLAQSEIGAYSLSEAGAGTDAAALGCKAKLSDDGAHYI 151
Cdd:cd01150 87 LTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLqGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 152 LN-----GEKMWVTN-GASADIYVLFAK----DVDHpefgvkkhgGTTAFIVE-------KSFEGFSVGKKEDKLGIRSS 214
Cdd:cd01150 167 INtpdftATKWWPGNlGKTATHAVVFAQlitpGKNH---------GLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 215 DTCSLLLDSCKVPVENVL----------------KVPGDGFPIAMNALDNSRIGIAAQALGIAQGAYESALGYAHEREAF 278
Cdd:cd01150 238 DNGFLQFRNVRIPRENLLnrfgdvspdgtyvspfKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQF 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 279 GKPiaYHQSIGNILadmATRTEAARLMVYKAAWAKQRHYEDDAPRHTMEASM----------AKLFAGDTAM-----WVA 343
Cdd:cd01150 318 GPK--PSDPEVQIL---DYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKellqgnsellAELHALSAGLkavatWTA 392
|
330 340 350
....*....|....*....|....*....|....*....
gi 663511215 344 ERAVQVL----GGYGYT--TDFPVERffRDAKITQIYEG 376
Cdd:cd01150 393 AQGIQECreacGGHGYLamNRLPTLR--DDNDPFCTYEG 429
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
24-368 |
1.23e-07 |
|
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: 53.12 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 24 LAPTCLDR----DREQKAPLEEWRVFCEqTGLQGITISEEYGGSPVDDVSEAIIVEELARVDPSFSVM---FCVHvglcS 96
Cdd:cd01159 6 LAPLIRERapeaERARRLPDEVVRALRE-IGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVasiVATH----S 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 97 KTIALHGNDEQKQKY----LTRLAqseiGAYslseagagtdaaALGCKAKLSDDGahYILNGEKMWVTNGASADIYVL-- 170
Cdd:cd01159 81 RMLAAFPPEAQEEVWgdgpDTLLA----GSY------------APGGRAERVDGG--YRVSGTWPFASGCDHADWILVga 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 171 -FAKDVDHPEFGvkkhggttAFIVEKsfEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVLKVPGD---GFPIAMNAL 246
Cdd:cd01159 143 iVEDDDGGPLPR--------AFVVPR--AEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMmagDGPGGSTPV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 247 DNSRI------GIAAQALGIAQGAYESALGYAHEREAFGK--------PIAYHQsigniLADMATRTEAARLMVYKA--- 309
Cdd:cd01159 213 YRMPLrqvfplSFAAVSLGAAEGALAEFLELAGKRVRQYGaavkmaeaPITQLR-----LAEAAAELDAARAFLERAtrd 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 663511215 310 AWAKQRHYEDDAPRHTMEASMAKLFAGDTAMWVAERAVQVLGGYGYTTDFPVERFFRDA 368
Cdd:cd01159 288 LWAHALAGGPIDVEERARIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDI 346
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
73-380 |
3.01e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 52.55 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 73 IVEELARVDPSFSVMFCVHVGLCSKTIALHGNDEQKQKYLTRLAQSEI-GAYSLSEAGAGTDAAALGCKAKLSDDGAHYI 151
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYpGCFAMTELHHGSNVQGLQTTATFDPLTDEFV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 152 LN-----GEKMWVTNGA-SADIYVLFAK-DVDHPEFGVKKHGGTTAFIV-------EKSFEGFSVGKKEDKLGIRSSDTC 217
Cdd:PLN02636 206 INtpndgAIKWWIGNAAvHGKFATVFARlKLPTHDSKGVSDMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 218 SLLLDSCKVPVENVLK----VPGDG------------FPIAMNALDNSRIGIAAQALGIAQGAYESALGYAHEREAFGKP 281
Cdd:PLN02636 286 ALRFRSVRIPRDNLLNrfgdVSRDGkytsslptinkrFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPP 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 282 ------IAYHQSIGNILADMATRTE----AARLMVYKAAWAKQRHYED-DAPRHTMEASMAKLFAGDTAMWVAErAVQVL 350
Cdd:PLN02636 366 kqpeisILDYQSQQHKLMPMLASTYafhfATEYLVERYSEMKKTHDDQlVADVHALSAGLKAYITSYTAKALST-CREAC 444
|
330 340 350
....*....|....*....|....*....|...
gi 663511215 351 GGYGYTTdfpVERF--FR-DAKITQIYEGTQEV 380
Cdd:PLN02636 445 GGHGYAA---VNRFgsLRnDHDIFQTFEGDNTV 474
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
90-238 |
1.28e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 44.07 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 90 VHVGLCSKTIALHGNDEQKQKYLTRLAQSEI-GAYSLSEAGAGTDAAALGCKAKLSDDGAHYILN-----GEKMWVTN-G 162
Cdd:PTZ00460 97 VHFAMVIPAFQVLGTDEQINLWMPSLLNFEIvGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFWPGElG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511215 163 ASADIYVLFAKDVdhpeFGVKKHGgTTAFIVE-------KSFEGFSVGKKEDKLGIRSSDTCSLLLDSCKVPVENVL--- 232
Cdd:PTZ00460 177 FLCNFALVYAKLI----VNGKNKG-VHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLary 251
|
....*..
gi 663511215 233 -KVPGDG 238
Cdd:PTZ00460 252 iKVSEDG 258
|
|
| |
