|
Name |
Accession |
Description |
Interval |
E-value |
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
37-409 |
0e+00 |
|
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: 540.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 37 EEETLLKETVANFANEKVRPLVKVMDETSELNKGLLKDLFDMNLMGIDISDSYGGANMNFMGSIIAIEELAKVDPAISVI 116
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 117 VDVQNTLVNNCINRYGSIQQREKYLSMLAT-NTVGSFCLSESGSGSDAFALATRAVRQSDgTFVLNGTKQWITNAKEAGV 195
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGD-DYVLNGSKMWITNGGEADF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 196 FIVMANVDPSQGYKGITAFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDILGELGRGYKIAIEGLNEGRIG 275
Cdd:cd01158 160 YIVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 276 IAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLPFVFQASMAKLHCSR 355
Cdd:cd01158 240 IAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 74854817 356 VAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEIVK 409
Cdd:cd01158 320 VAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
34-409 |
1.54e-151 |
|
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: 433.88 E-value: 1.54e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 34 TLSEEETLLKETVANFANEKVRPLVKVMDETSELNKGLLKDLFDMNLMGIDISDSYGGANMNFMGSIIAIEELAKVDPAI 113
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 114 SVIVDVQNtLVNNCINRYGSIQQREKYLSMLATN-TVGSFCLSESGSGSDAFALATRAVRQSDGtFVLNGTKQWITNAKE 192
Cdd:COG1960 84 ALPVGVHN-GAAEALLRFGTEEQKERYLPRLASGeWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLNGQKTFITNAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 193 AGVFIVMANVDPSQGYKGITAFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDILGELGRGYKIAIEGLNEG 272
Cdd:COG1960 162 ADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 273 RIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLPFVFQASMAKLH 352
Cdd:COG1960 242 RLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLF 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 74854817 353 CSRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEIVK 409
Cdd:COG1960 322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
35-409 |
4.86e-111 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 330.53 E-value: 4.86e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 35 LSEEETLLKETVANFANEKVRPLVKVMDETSELNKGLLKDLFDMNLMGIDISDSYGGANMNFMGSIIAIEELAKVDPAIS 114
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 115 VIVDVQNTLVNNCINRYGSIQQREKYLSMLATNT-VGSFCLSESGSGSDAFALATRAVRQsDGTFVLNGTKQWITNAKEA 193
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEhIGALAMSEPNAGSDVVSMKLRAEKK-GDRYVLNGSKMWITNGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 194 GVFIVMANVDPSQGYKGITAFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDILGELGRGYKIAIEGLNEGR 273
Cdd:cd01156 161 DTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 274 IGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLPFVFQASMAKLHC 353
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 74854817 354 SRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEIVK 409
Cdd:cd01156 321 AEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
37-405 |
3.16e-105 |
|
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: 314.22 E-value: 3.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 37 EEETLLKETVANFANEKVRPLVKVMDETSELNKGLLKDlfdmnlmgidisdsygganmnfMGSIIAIEELAkvdpaisvi 116
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAE----------------------LGLLLGAALLL--------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 117 vdvqntlvnncinRYGSIQQREKYLSMLATNT-VGSFCLSESGSGSDAFALATRAVRqSDGTFVLNGTKQWITNAKEAGV 195
Cdd:cd00567 50 -------------AYGTEEQKERYLPPLASGEaIAAFALTEPGAGSDLAGIRTTARK-DGDGYVLNGRKIFISNGGDADL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 196 FIVMANVDPSQ-GYKGITAFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDILGELGRGYKIAIEGLNEGRI 274
Cdd:cd00567 116 FIVLARTDEEGpGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 275 GIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLPFV-FQASMAKLHC 353
Cdd:cd00567 196 LLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEArLEAAMAKLFA 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 74854817 354 SRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAK 405
Cdd:cd00567 276 TEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
35-407 |
1.51e-97 |
|
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: 296.28 E-value: 1.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 35 LSEEETLLKETVANFANEKVRPLVKVMDETSELNKGLLKDLFDMNLMGIDISDSYGGANMNFMGSIIAIEELAKVDPAIS 114
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 115 VIVDVQNtLVNNCINRYGSIQQREKYLSMLAT-NTVGSFCLSESGSGSDAFALATRAVRQSDgTFVLNGTKQWITNAKEA 193
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTmEKLASYCLTEPGSGSDAAALRTRAVREGD-HYVLNGSKAFISGAGDS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 194 GVFIVMANVDpSQGYKGITAFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDILGELGRGYKIAIEGLNEGR 273
Cdd:cd01162 159 DVYVVMARTG-GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 274 IGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLP-FVFQASMAKLH 352
Cdd:cd01162 238 LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPdAVKLCAMAKRF 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 74854817 353 ----CSRVAEKAasacISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEI 407
Cdd:cd01162 318 atdeCFDVANQA----LQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARAL 372
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
35-410 |
6.86e-86 |
|
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: 267.41 E-value: 6.86e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 35 LSEEETLLKETVANFANEKVRPlvKVMDETSELNKGLLKDLFDMNLMGIDISDSYGGANM-NFMGSIIAieELAKVDPAI 113
Cdd:cd01161 27 QTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLnNTQYARLA--EIVGMDLGF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 114 SVIVDVQNTLVNNCINRYGSIQQREKYLSMLATNT-VGSFCLSESGSGSDAFALATRAVRQSDGT-FVLNGTKQWITNAK 191
Cdd:cd01161 103 SVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEwIAAFALTEPSSGSDAASIRTTAVLSEDGKhYVLNGSKIWITNGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 192 EAGVFIVMAN---VDPSQGYK-GITAFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDILGELGRGYKIAIE 267
Cdd:cd01161 183 IADIFTVFAKtevKDATGSVKdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 268 GLNEGRIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLPFVFQ-- 345
Cdd:cd01161 263 ILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQie 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74854817 346 ASMAKLHCSRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEIVKN 410
Cdd:cd01161 343 AAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQH 407
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
35-407 |
1.08e-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: 266.15 E-value: 1.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 35 LSEEETLLKETVANFANEKVRPLVKVMDETSELNKGLLKDLFDMNLMGIDIsDSYGGANMNFMGSIIAIEELAKVDPAIS 114
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATI-KGYGCAGLSSVAYGLIAREVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 115 VIVDVQNTLVNNCINRYGSIQQREKYLSMLAT-NTVGSFCLSESGSGSDAFALATRAvRQSDGTFVLNGTKQWITNAKEA 193
Cdd:cd01151 92 SFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASgELIGCFGLTEPNHGSDPGGMETRA-RKDGGGYKLNGSKTWITNSPIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 194 GVFIVMANVDPSQGYKGitaFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDILGELgRGYKIAIEGLNEGR 273
Cdd:cd01151 171 DVFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNAR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 274 IGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLPFVFQASMAKLHC 353
Cdd:cd01151 247 YGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNN 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 74854817 354 SRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEI 407
Cdd:cd01151 327 CGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAI 380
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
20-409 |
1.41e-83 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 261.35 E-value: 1.41e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 20 RNYSKSKSFIQPITTLSEEETLL--KETVANFANEKVRPLVKVMDETSELNK--GLLKDLFDMNLMGIDISDSYGGANMN 95
Cdd:PLN02519 9 RRRGLARRFSSSSSSLLFDDTQLqfKESVQQFAQENIAPHAAAIDATNSFPKdvNLWKLMGDFNLHGITAPEEYGGLGLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 96 FMGSIIAIEELAKVDPAISVIVDVQNTLVNNCINRYGSIQQREKYLSMLATNT-VGSFCLSESGSGSDAFALATRAVRqS 174
Cdd:PLN02519 89 YLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEhVGALAMSEPNSGSDVVSMKCKAER-V 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 175 DGTFVLNGTKQWITNAKEAGVFIVMANVDPSQGYKGITAFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDI 254
Cdd:PLN02519 168 DGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 255 LGELGRGYKIAIEGLNEGRIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAAR 334
Cdd:PLN02519 248 LGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVAR 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74854817 335 IKEAGLPFVFQASMAKLHCSRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEIVK 409
Cdd:PLN02519 328 DCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
35-408 |
1.73e-83 |
|
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: 260.21 E-value: 1.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 35 LSEEETLLKETVANFANEKVRPLVKVMDETSELNKGLLKDLFDMNLMGIDISDSYGGANMNFMGSIIAIEELAKVDPAIS 114
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 115 VIVDVqNTLVNNCINRYGSIQQREKYL-SMLATNTVGSFCLSESGSGSDAFALATRAVRQSDgTFVLNGTKQWITNAKEA 193
Cdd:cd01157 81 TAIEA-NSLGQMPVIISGNDEQKKKYLgRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNGGKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 194 GVFIVMANVDP---SQGYKGITAFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDILGELGRGYKIAIEGLN 270
Cdd:cd01157 159 NWYFLLARSDPdpkCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 271 EGRIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLPFVFQASMAK 350
Cdd:cd01157 239 KTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 74854817 351 LHCSRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEIV 408
Cdd:cd01157 319 AFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
37-408 |
9.80e-83 |
|
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: 258.20 E-value: 9.80e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 37 EEETLLKETVANFANEKVRPLVKVMDETSELNKGLLKDLFDMNLMGIDISDSYGGANMNFMGSIIAIEELAKVDpAISVI 116
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAG-GSGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 117 VDVQNTLVNNCINRYGSIQQREKYL-SMLATNTVGSFCLSESGSGSDAFALATRAVRqsDGT-FVLNGTKQWITNAKEAG 194
Cdd:cd01160 80 LSLHTDIVSPYITRAGSPEQKERVLpQMVAGKKIGAIAMTEPGAGSDLQGIRTTARK--DGDhYVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 195 VFIVMANVD-PSQGYKGITAFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDILGELGRGYKIAIEGLNEGR 273
Cdd:cd01160 158 VVIVVARTGgEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 274 IGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLPFVFQASMAKLHC 353
Cdd:cd01160 238 LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 74854817 354 SRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEIV 408
Cdd:cd01160 318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
38-409 |
2.39e-78 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 247.93 E-value: 2.39e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 38 EETLLKETVANFANEKVRPLVKVMDETSELNKGLLKDLFDMNLMGIDISDSYGGANMNFMGSIIAIEELAKVDPAISVIV 117
Cdd:PTZ00461 40 EHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 118 DVQNTLVNNCINRYGSIQQREKYL-SMLATNTVGSFCLSESGSGSDAFALATRAVRQSDGTFVLNGTKQWITNAKEAGVF 196
Cdd:PTZ00461 120 LAHSMLFVNNFYYSASPAQRARWLpKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKIWITNGTVADVF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 197 IVMANVDPSqgykgITAFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDILGELGRGYKIAIEGLNEGRIGI 276
Cdd:PTZ00461 200 LIYAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 277 AAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLPFVFQASMAKLHCSRV 356
Cdd:PTZ00461 275 AAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPI 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 74854817 357 AEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEIVK 409
Cdd:PTZ00461 355 AKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLK 407
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
35-411 |
1.05e-64 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 211.90 E-value: 1.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 35 LSEEETLLKETVANF-ANEKVRPLVKVMDETSELNKGLLKDLFD--MNLMGIDisDSYGGANMNFMGSIIAIEELAKVDP 111
Cdd:PRK12341 5 LTEEQELLLASIRELiTRNFPEEYFRTCDENGTYPREFMRALADngISMLGVP--EEFGGTPADYVTQMLVLEEVSKCGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 112 AISVIVDVQNtlVNNcINRYGSIQQREKylSMLATNTVGS--FCL--SESGSGSDAFALATRAVRQsDGTFVLNGTKQWI 187
Cdd:PRK12341 83 PAFLITNGQC--IHS-MRRFGSAEQLRK--TAESTLETGDpaYALalTEPGAGSDNNSATTTYTRK-NGKVYLNGQKTFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 188 TNAKEAGVFIVMA-NVDPSQGYKGITAFIVESNNPGLRIGKKEdKLGIRASSTCEVILDNCVVKPTDILGELGRGYKIAI 266
Cdd:PRK12341 157 TGAKEYPYMLVLArDPQPKDPKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 267 EGLNEGRIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLPFVFQA 346
Cdd:PRK12341 236 YNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74854817 347 SMAKLHCSRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEIVKNF 411
Cdd:PRK12341 316 ALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDY 380
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
35-407 |
6.24e-56 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 189.68 E-value: 6.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 35 LSEEETLLKETVANFANEKVRPLVKVMDETSELNKGLLKDLFDMNLMGIDISdSYGGANMNFMGSIIAIEELAKVDPAIS 114
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDASCS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 115 VIVDVQNTLVNNCINRYGSIQQREKYLSMLAT-NTVGSFCLSESGSGSDAFALATRAvRQSDGTFVLNGTKQWITNAKEA 193
Cdd:PLN02526 108 TFILVHSSLAMLTIALCGSEAQKQKYLPSLAQlDTVACWALTEPDYGSDASSLNTTA-TKVEGGWILNGQKRWIGNSTFA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 194 GVFIVMA-NVDPSQgykgITAFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDILGELGrGYKIAIEGLNEG 272
Cdd:PLN02526 187 DVLVIFArNTTTNQ----INGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVN-SFQDTNKVLAVS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 273 RIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLPFVFQASMAKLH 352
Cdd:PLN02526 262 RVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAW 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 74854817 353 CSRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEI 407
Cdd:PLN02526 342 ITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
44-408 |
1.33e-53 |
|
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: 183.36 E-value: 1.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 44 ETVANFANEKVRPLVKVMD--------ETSELNKGLLKDLFDMN---LMGIDISDSYGGANMNFMGSIIAIEELAKVDPA 112
Cdd:cd01153 3 EEVARLAENVLAPLNADGDregpvfddGRVVVPPPFKEALDAFAeagWMALGVPEEYGGQGLPITVYSALAEIFSRGDAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 113 ISVIVDVQNTLvnNCINRYGSIQQREKYLS-MLATNTVGSFCLSESGSGSDAFALATRAVRQSDGTFVLNGTKQWITNAK 191
Cdd:cd01153 83 LMYASGTQGAA--ATLLAHGTEAQREKWIPrLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 192 EAG----VFIVMANV-DPSQGYKGITAFIVES-----NNPGLRIGKKEDKLGIRASSTCEVILDNcvvKPTDILGELGRG 261
Cdd:cd01153 161 HDMseniVHLVLARSeGAPPGVKGLSLFLVPKflddgERNGVTVARIEEKMGLHGSPTCELVFDN---AKGELIGEEGMG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 262 YKIAIEGLNEGRIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATF----------------------QGMQFTYADLA 319
Cdd:cd01153 238 LAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAApavtiihhpdvrrslmtqkayaEGSRALDLYTA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 320 VDIEAGRLLTYNAARIKEAGLPFVFQASMAKLHCSRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQ 399
Cdd:cd01153 318 TVQDLAERKATEGEDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQ 397
|
....*....
gi 74854817 400 LQTIAKEIV 408
Cdd:cd01153 398 ALDLIGRKI 406
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
259-407 |
1.76e-52 |
|
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: 172.44 E-value: 1.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 259 GRGYKIAIEGLNEGRIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEA 338
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74854817 339 GLPFVFQASMAKLHCSRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEI 407
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
34-411 |
2.92e-48 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 168.47 E-value: 2.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 34 TLSEEETLLKETVANF-ANEKVRPLVKVMDETSELNKGLLKDLFDMNLMGIDISDSYGGANMNFMGSIIAIEELAKVDPA 112
Cdd:PRK03354 4 NLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 113 ISVIVDVQNTLvnNCINRYGSIQQREKYLSMLAT-NTVGSFCLSESGSGSDAFALATRAVRQsDGTFVLNGTKQWITNAK 191
Cdd:PRK03354 84 TYVLYQLPGGF--NTFLREGTQEQIDKIMAFRGTgKQMWNSAITEPGAGSDVGSLKTTYTRR-NGKVYLNGSKCFITSSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 192 EAGVFIVMANVDPSQGYKGITAFIVESNNPGLRIGKKEdKLGIRASSTCEVILDNCVVKPTDILGELGRGYKIAIEGLNE 271
Cdd:PRK03354 161 YTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 272 GRIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLPFVFQASMAKL 351
Cdd:PRK03354 240 ERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKY 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 352 HCSRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEIVKNF 411
Cdd:PRK03354 320 FCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQY 379
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
154-399 |
5.05e-41 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 150.21 E-value: 5.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 154 LSESGSGSDAFALATRAVRQSDGTFVLNGTKqWITNAKEAGVFIVMAN-VDPSQGYKGITAFIVESNNP-----GLRIGK 227
Cdd:cd01154 153 MTEKQGGSDLGANETTAERSGGGVYRLNGHK-WFASAPLADAALVLARpEGAPAGARGLSLFLVPRLLEdgtrnGYRIRR 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 228 KEDKLGIRASSTCEVILDNCVvkpTDILGELGRGYKIAIEGLNEGRIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIAT 307
Cdd:cd01154 232 LKDKLGTRSVATGEVEFDDAE---AYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLID 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 308 FQGMQFTYADLAVDIEAGRLLTYNAARI---KEAGLPFvfQASMA-------KLHCSRVAEKAASACISMLGGVGFTKEF 377
Cdd:cd01154 309 HPLMRRDLAEMEVDVEAATALTFRAARAfdrAAADKPV--EAHMArlatpvaKLIACKRAAPVTSEAMEVFGGNGYLEEW 386
|
250 260
....*....|....*....|..
gi 74854817 378 PAEKFFRDSKVGQIYEGTSNIQ 399
Cdd:cd01154 387 PVARLHREAQVTPIWEGTGNIQ 408
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
89-407 |
2.05e-32 |
|
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: 125.92 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 89 YGGANMNFMGSIIAIEELAKVDPAISVIVDVQNTLVNNcINRYGSIQQREKYLSMLATntvGS--FCL--SESGSGSDAF 164
Cdd:cd01152 58 YGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPT-ILAYGTDEQKRRFLPPILS---GEeiWCQgfSEPGAGSDLA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 165 ALATRAVRQSDGtFVLNGTKQWITNAKEAGVFIVMANVDPS-QGYKGITAFIVESNNPGLRIGKKEDKLGirASSTCEVI 243
Cdd:cd01152 134 GLRTRAVRDGDD-WVVNGQKIWTSGAHYADWAWLLVRTDPEaPKHRGISILLVDMDSPGVTVRPIRSING--GEFFNEVF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 244 LDNCVVKPTDILGELGRGYKIAIEGLNEGRigiaAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIE 323
Cdd:cd01152 211 LDDVRVPDANRVGEVNDGWKVAMTTLNFER----VSIGGSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 324 AGRLLTYNAARIKEAGLPFVFQASMAKLHCSRVAEKAASACISMLG-----GVGFTKEFPAEKFFRD---SKVGQIYEGT 395
Cdd:cd01152 287 ALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGtaallRDPAPGAELAGRWEADylrSRATTIYGGT 366
|
330
....*....|..
gi 74854817 396 SNIQLQTIAKEI 407
Cdd:cd01152 367 SEIQRNIIAERL 378
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
36-146 |
1.26e-31 |
|
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: 116.41 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 36 SEEETLLKETVANFANEKVRPLVKVMDETSELNKGLLKDLFDMNLMGIDISDSYGGANMNFMGSIIAIEELAKVDPAISV 115
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|.
gi 74854817 116 IVDVQNTLVNNCINRYGSIQQREKYLSMLAT 146
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
151-245 |
2.87e-31 |
|
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: 114.68 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 151 SFCLSESGSGSDAFALATRAVRQSDGTFVLNGTKQWITNAKEAGVFIVMANVDPSQGYKGITAFIVESNNPGLRIGKKED 230
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 74854817 231 KLGIRASSTCEVILD 245
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
82-409 |
1.30e-30 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 123.82 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 82 GIDISDSYGGANMNFMGSIIAIEELAKVDPAISVI----VDVQNTLVNncinrYGSIQQREKYLSMLATNT-VGSFCLSE 156
Cdd:PTZ00456 115 GISEPEEYGGQALPLSVGFITRELMATANWGFSMYpglsIGAANTLMA-----WGSEEQKEQYLTKLVSGEwSGTMCLTE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 157 SGSGSDAFALATRAVRQSDGTFVLNGTKQWIT----NAKEAGVFIVMANVDPSQ-GYKGITAFIVESN----------NP 221
Cdd:PTZ00456 190 PQCGTDLGQVKTKAEPSADGSYKITGTKIFISagdhDLTENIVHIVLARLPNSLpTTKGLSLFLVPRHvvkpdgsletAK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 222 GLRIGKKEDKLGIRASSTCEVILDNCVvkpTDILGELGRGYKIAIEGLNEGRIGIAAQMLGLAQGVFDSTIPYLMERKQF 301
Cdd:PTZ00456 270 NVKCIGLEKKMGIKGSSTCQLSFENSV---GYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSM 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 302 ------------GKPIATFQGMQ--------FTYADLAVDIEAGRLLTY-----NAARIKEAGLPFVFQASMAKLHCSRV 356
Cdd:PTZ00456 347 ralsgtkepekpADRIICHANVRqnilfakaVAEGGRALLLDVGRLLDIhaaakDAATREALDHEIGFYTPIAKGCLTEW 426
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 74854817 357 AEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQ-LQTIAKEIVK 409
Cdd:PTZ00456 427 GVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQaLDFIGRKVLS 480
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
128-405 |
2.07e-30 |
|
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: 120.57 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 128 INRYGSIQQREKYLSMLATNTVGS-FCLSESG-SGSDAFALATRAVRQSDgTFVLNGTKQWITNAKE--AGVFIVMANVD 203
Cdd:cd01155 104 LHRYGSEEQKKQWLEPLLDGKIRSaFAMTEPDvASSDATNIECSIERDGD-DYVINGRKWWSSGAGDprCKIAIVMGRTD 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 204 PSQG--YKGITAFIVESNNPGLRIgkkedklgIRASST----------CEVILDNCVVKPTDILGELGRGYKIAIEGLNE 271
Cdd:cd01155 183 PDGAprHRQQSMILVPMDTPGVTI--------IRPLSVfgyddaphghAEITFDNVRVPASNLILGEGRGFEIAQGRLGP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 272 GRIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARI------KEAglpfVFQ 345
Cdd:cd01155 255 GRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMidtvgnKAA----RKE 330
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 346 ASMAKLHCSRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAK 405
Cdd:cd01155 331 IAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
275-396 |
4.97e-21 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 88.17 E-value: 4.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 275 GIAAQMLGLAQGVFDSTIPYLMERKQ--FGKPIATFQGMQFTYADLAVDIEAGRLLTYNAA----RIKEAGLPFVF---- 344
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVTPalra 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 74854817 345 QASMAKLHCSRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTS 396
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
130-405 |
9.32e-20 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 91.78 E-value: 9.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 130 RYGSIQQREKYLSMLATNTVGS-FCLSESG-SGSDAFALATRAVRQSDgTFVLNGTKQWITNAKE--AGVFIVMANVDPS 205
Cdd:PLN02876 531 RYGNKEQQLEWLIPLLEGKIRSgFAMTEPQvASSDATNIECSIRRQGD-SYVINGTKWWTSGAMDprCRVLIVMGKTDFN 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 206 QG-YKGITAFIVESNNPGLRIGKKEDKLGIRAS--STCEVILDNCVVKPTDIL-GElGRGYKIAIEGLNEGRIGIAAQML 281
Cdd:PLN02876 610 APkHKQQSMILVDIQTPGVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNILlGE-GRGFEIAQGRLGPGRLHHCMRLI 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 282 GLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAA-------RIKEAGLpfvfqASMAKLHCS 354
Cdd:PLN02876 689 GAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAAdqldrlgNKKARGI-----IAMAKVAAP 763
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 74854817 355 RVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAK 405
Cdd:PLN02876 764 NMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAK 814
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
31-352 |
1.73e-15 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 78.46 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 31 PITTLSEEETllketvaNFANEKVRPLVKVMD--ETSELNKGLLKDLFDM----NLMGIDISDSYGGANMN-FMGSIIaI 103
Cdd:PRK13026 74 PKPTLTAEEQ-------AFIDNEVETLLTMLDdwDIVQNRKDLPPEVWDYlkkeGFFALIIPKEYGGKGFSaYANSTI-V 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 104 EELAKVDPAISVIVDVQNTL-VNNCINRYGSIQQREKYLSMLATNT-VGSFCLSESGSGSDAFALATRAV---RQSDGTF 178
Cdd:PRK13026 146 SKIATRSVSAAVTVMVPNSLgPGELLTHYGTQEQKDYWLPRLADGTeIPCFALTGPEAGSDAGAIPDTGIvcrGEFEGEE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 179 VL----NGTKQWITNAKEAGVFIVMANV-DPSQ--GYK---GITAFIVESNNPGLRIGKKEDKLGIR-ASSTcevILDNC 247
Cdd:PRK13026 226 VLglrlTWDKRYITLAPVATVLGLAFKLrDPDGllGDKkelGITCALIPTDHPGVEIGRRHNPLGMAfMNGT---TRGKD 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 248 VVKPTD-ILG---ELGRGYKIAIEGLNEGRiGIAAQMLGLAQGV--FDSTIPYLMERKQFGKPIATFQGMQFTYADLAVD 321
Cdd:PRK13026 303 VFIPLDwIIGgpdYAGRGWRMLVECLSAGR-GISLPALGTASGHmaTRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGN 381
|
330 340 350
....*....|....*....|....*....|....
gi 74854817 322 ---IEAGRLLTYNAARIKEAglPFVFQAsMAKLH 352
Cdd:PRK13026 382 tylLEAARRLTTTGLDLGVK--PSVVTA-IAKYH 412
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
103-411 |
3.85e-13 |
|
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: 71.21 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 103 IEELAKVDPAISVIVDVQNTLVNNCINRYGSIQQREKYLS-MLATNTVGSFCLSESGSGSDAFALATRAV-RQSDGTFVL 180
Cdd:cd01150 88 TNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQgANNLEIIGCFAQTELGHGSNLQGLETTATyDPLTQEFVI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 181 N-----GTKQWITN-AKEAGVFIVMAN-VDPSQGYkGITAFIVESNN-------PGLRIGKKEDKLG------------- 233
Cdd:cd01150 168 NtpdftATKWWPGNlGKTATHAVVFAQlITPGKNH-GLHAFIVPIRDpkthqplPGVTVGDIGPKMGlngvdngflqfrn 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 234 IRA------SSTCEVILDNCVVKPTDilgELGRGYKIAIEGLNEGRIGI---AAQMLGLAqgvfdSTIP--YLMERKQFG 302
Cdd:cd01150 247 VRIprenllNRFGDVSPDGTYVSPFK---DPNKRYGAMLGTRSGGRVGLiydAAMSLKKA-----ATIAirYSAVRRQFG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 303 K-------PIATFQGMQ---FTYadLAVDIE---AGRLLTYNAARIKEAGLPFVFQASmAKLH---------CSRVAEKA 360
Cdd:cd01150 319 PkpsdpevQILDYQLQQyrlFPQ--LAAAYAfhfAAKSLVEMYHEIIKELLQGNSELL-AELHalsaglkavATWTAAQG 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 74854817 361 ASACISMLGGVGFTKE--FPaeKFFRDSKVGQIYEGTSNIQLQTIAKEIVKNF 411
Cdd:cd01150 396 IQECREACGGHGYLAMnrLP--TLRDDNDPFCTYEGDNTVLLQQTANYLLKKY 446
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
154-398 |
1.88e-12 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 68.62 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 154 LSESGSGSDAFALATRAVRQSDGTFVLNGTKqWITNAKEAGVFIVMAnvdpsQGYKGITAFIVESNNP-----GLRIGKK 228
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLADGSYRLVGHK-WFFSVPQSDAHLVLA-----QAKGGLSCFFVPRFLPdgqrnAIRLERL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 229 EDKLGIRASSTCEVILDNCVVKptdILGELGRGYKIAIEGLNEGRIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATF 308
Cdd:PRK11561 258 KDKLGNRSNASSEVEFQDAIGW---LLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQ 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 309 QGMQFTYADLAVDIEAGRLLTYNAAR-------IKEAGLPFVFQASMAKLHCSRVAEKAASAcISMLGGVGFTKEFPAEK 381
Cdd:PRK11561 335 PLMRQVLSRMALQLEGQTALLFRLARawdrradAKEALWARLFTPAAKFVICKRGIPFVAEA-MEVLGGIGYCEESELPR 413
|
250
....*....|....*..
gi 74854817 382 FFRDSKVGQIYEGTSNI 398
Cdd:PRK11561 414 LYREMPVNSIWEGSGNI 430
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
130-353 |
1.01e-09 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 60.60 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 130 RYGSIQQREKYLSMLATNT-VGSFCLSESGSGSDAFAL-----ATRAVRQSDGT--FVLNGTKQWITNAKEAGV----FI 197
Cdd:PRK09463 174 HYGTDEQKDHYLPRLARGEeIPCFALTSPEAGSDAGSIpdtgvVCKGEWQGEEVlgMRLTWNKRYITLAPIATVlglaFK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 198 VmanVDPSQ--GYK---GITAFIVESNNPGLRIGKKEDKLGIRasstceviLDNC------VVKPTD-ILGE---LGRGY 262
Cdd:PRK09463 254 L---YDPDGllGDKedlGITCALIPTDTPGVEIGRRHFPLNVP--------FQNGptrgkdVFIPLDyIIGGpkmAGQGW 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 263 KIAIEGLNEGR-IGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVD---IEAGRLLTYNAarIKEA 338
Cdd:PRK09463 323 RMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTLTTAA--VDLG 400
|
250
....*....|....*
gi 74854817 339 GLPFVFQAsMAKLHC 353
Cdd:PRK09463 401 EKPSVLSA-IAKYHL 414
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
103-413 |
7.50e-08 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 54.48 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 103 IEELAKVDPAISVIVDVQNTLVNNCINRYGSIQQREKYLSMLAT-NTVGSFCLSESGSGSDAFALATRAV--RQSDgTFV 179
Cdd:PLN02636 127 TEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNlDYPGCFAMTELHHGSNVQGLQTTATfdPLTD-EFV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 180 LN-----GTKQWITNAKEAGVFI-VMANVD-PSQGYKGIT-----AFIV-------ESNNPGLRIGKKEDKLGIRASSTC 240
Cdd:PLN02636 206 INtpndgAIKWWIGNAAVHGKFAtVFARLKlPTHDSKGVSdmgvhAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 241 EVILDNcVVKPTDIL----GELGR--GYKIAIEGLNE-----------GRIGIAAQMLGLAQGVFDSTIPYLMERKQFGK 303
Cdd:PLN02636 286 ALRFRS-VRIPRDNLlnrfGDVSRdgKYTSSLPTINKrfaatlgelvgGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGP 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 304 P------IATFQGMQF--------TYA-----DLAVDIEAGRLLTYNAARIKE-----AGLpfvfqasmaKLHCSRVAEK 359
Cdd:PLN02636 365 PkqpeisILDYQSQQHklmpmlasTYAfhfatEYLVERYSEMKKTHDDQLVADvhalsAGL---------KAYITSYTAK 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 74854817 360 AASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEIVKNFNK 413
Cdd:PLN02636 436 ALSTCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQYKE 489
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
79-287 |
7.58e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 51.04 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 79 NLMGIDISDSYGGANMNFMGSIIAIEELAKVDPAISVIVDVQNTLVNNCINRYGSIQQREKYLSMLATNTVGSFCLSESG 158
Cdd:PTZ00457 64 NLYGARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWATEEG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 159 SGSDAFALATRAVRQSDGTFVLNGTKQWItNAKEAGVFIVMAN-VDPSQGYKGITA------FIVESNNPGLRIGKKedk 231
Cdd:PTZ00457 144 CGSDISMNTTKASLTDDGSYVLTGQKRCE-FAASATHFLVLAKtLTQTAAEEGATEvsrnsfFICAKDAKGVSVNGD--- 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 74854817 232 lgirasstcEVILDNCVVKptDILGELGRGYKIAIEGLNEGRIGIAAQMLGLAQGV 287
Cdd:PTZ00457 220 ---------SVVFENTPAA--DVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRV 264
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
55-334 |
1.67e-06 |
|
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: 49.63 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 55 RPLVKVMDETS---ELNKGL----LKDLFDMNLMGIDISDSYGGANMNFMGSIIAIEELAKVDPAISVIVDVQNTLVNNc 127
Cdd:cd01163 4 RPLAARIAEGAaerDRQRGLpyeeVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVEA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 128 INRYGSIQQREKYLSMLATNTVGSFCLSESGSGSDAFAlaTRAVRQSDGTFVLNGTKQWITNAKEAGvFIVMANVDPSQg 207
Cdd:cd01163 83 LLLAGPEQFRKRWFGRVLNGWIFGNAVSERGSVRPGTF--LTATVRDGGGYVLNGKKFYSTGALFSD-WVTVSALDEEG- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74854817 208 ykGITAFIVESNNPGLRIGKKEDKLGIR--ASSTceVILDNCVVKPTDILG----ELGRGYKIAIEGLNegrigIAAQML 281
Cdd:cd01163 159 --KLVFAAVPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLPrpnaPDRGTLLTAIYQLV-----LAAVLA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 74854817 282 GLAQGVFDSTIPYLMERKQ-FGKPIAT-----FQGMQfTYADLAVDIEAGRLLTYNAAR 334
Cdd:cd01163 230 GIARAALDDAVAYVRSRTRpWIHSGAEsarddPYVQQ-VVGDLAARLHAAEALVLQAAR 287
|
|
| |
