|
Name |
Accession |
Description |
Interval |
E-value |
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
5-379 |
0e+00 |
|
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: 614.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 5 LTEDQQAFRDAARAFAEKSMAPHAAQWDAEHIFPVDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELAAACPSTA 84
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 85 AFITIHNMATWMVASFASDDLRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVRDGESYVINGSKMFISGAGATDI 164
Cdd:cd01162 81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 165 LVLMARTGDAdsGSKGISTFVIPADADGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGDGFAIAMKGLDGGRL 244
Cdd:cd01162 161 YVVMARTGGE--GPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 245 NIATCSLGGAQAALLRARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDSGDPEATLHCAMAKRFA 324
Cdd:cd01162 239 NIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1952118256 325 TDACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRLL 379
Cdd:cd01162 319 TDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALL 373
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-382 |
4.60e-169 |
|
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: 477.41 E-value: 4.60e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 1 MDFNLTEDQQAFRDAARAFAEKSMAPHAAQWDAEHIFPVDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELAAAC 80
Cdd:COG1960 1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 81 PSTAAFITIHNMATWMVASFASDDLRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVRDGESYVINGSKMFISGAG 160
Cdd:COG1960 81 ASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 161 ATDILVLMARTGDADsGSKGISTFVIPADADGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGDGFAIAMKGLD 240
Cdd:COG1960 161 VADVILVLARTDPAA-GHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 241 GGRLNIATCSLGGAQAALLRARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDSGDPeATLHCAMA 320
Cdd:COG1960 240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGED-AALEAAMA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952118256 321 KRFATDACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRLLDDG 382
Cdd:COG1960 319 KLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRP 380
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
7-380 |
6.09e-150 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 428.61 E-value: 6.09e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 7 EDQQAFRDAARAFAEKSMAPHAAQWDAEHIFPVDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELAAACPSTAAF 86
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 87 ITIHN-MATWMVASFASDDLRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVRDGESYVINGSKMFISGAGATDIL 165
Cdd:cd01158 81 VSVHNsLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 166 VLMARTgDADSGSKGISTFVIPADADGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGDGFAIAMKGLDGGRLN 245
Cdd:cd01158 161 IVFAVT-DPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 246 IATCSLGGAQAALLRARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDSGDP---EAtlhcAMAKR 322
Cdd:cd01158 240 IAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPfikEA----AMAKL 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952118256 323 FATDACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRLLD 380
Cdd:cd01158 316 FASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
92-376 |
1.46e-123 |
|
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: 359.68 E-value: 1.46e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 92 MATWMVASFASDDLRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVRDGESYVINGSKMFISGAGATDILVLMART 171
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLART 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 172 GDADSGSKGISTFVIPADADGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGDGFAIAMKGLDGGRLNIATCSL 251
Cdd:cd00567 123 DEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVAL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 252 GGAQAALLRARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDSGDPEATLHCAMAKRFATDACFEV 331
Cdd:cd00567 203 GAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEAAREV 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1952118256 332 ANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIAR 376
Cdd:cd00567 283 ADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
21-379 |
7.11e-104 |
|
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: 311.36 E-value: 7.11e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 21 EKSMAPHAAQWDAEHIFPVDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELAAACPSTAAFITIHNMATWMVASF 100
Cdd:cd01160 15 AKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGLSLHTDIVSPYITRA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 101 ASDDLRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVRDGESYVINGSKMFISGAGATDILVLMARTGDADSGSKG 180
Cdd:cd01160 95 GSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGGEARGAGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 181 ISTFVIPADADGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGDGFAIAMKGLDGGRLNIATCSLGGAQAALLR 260
Cdd:cd01160 175 ISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 261 ARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDSGDPEATlHCAMAKRFATDACFEVANEALQLHG 340
Cdd:cd01160 255 TRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVA-EASMAKYWATELQNRVAYECVQLHG 333
|
330 340 350
....*....|....*....|....*....|....*....
gi 1952118256 341 GYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRLL 379
Cdd:cd01160 334 GWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
5-378 |
1.05e-100 |
|
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: 303.18 E-value: 1.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 5 LTEDQQAFRDAARAFAEKSMAPHAAQWDAEHIFPVDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELAAACPSTA 84
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 85 AFITIH-NMATWMVASFASDDLRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVRDGESYVINGSKMFISGAGATD 163
Cdd:cd01156 82 LSYGAHsNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 164 ILVLMARTgDADSGSKGISTFVIPADADGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGDGFAIAMKGLDGGR 243
Cdd:cd01156 162 TLVVYAKT-DPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 244 LNIATCSLGGAQAALLRARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDSGDPEAtLHCAMAKRF 323
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDP-KDAAGVILY 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1952118256 324 ATDACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRL 378
Cdd:cd01156 320 AAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGREL 374
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
32-375 |
2.61e-100 |
|
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: 303.62 E-value: 2.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 32 DAEHIFPVDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELAAACPSTAAFITIHNMATWMVASFASDDLRQEIVP 111
Cdd:cd01161 52 DQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 112 RLASGEWLASYCLTEPGAGSDAASLRTRAVR--DGESYVINGSKMFISGAGATDILVLMART--GDADSGSK-GISTFVI 186
Cdd:cd01161 132 KLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWITNGGIADIFTVFAKTevKDATGSVKdKITAFIV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 187 PADADGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGDGFAIAMKGLDGGRLNIATCSLGGAQAALLRARNYMH 266
Cdd:cd01161 212 ERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYAN 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 267 ERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDSG-DPEATLHCAMAKRFATDACFEVANEALQLHGGYGYI 345
Cdd:cd01161 292 NRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGlKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFM 371
|
330 340 350
....*....|....*....|....*....|
gi 1952118256 346 REYPLERYLRDLRVHQILEGTNEIMRLIIA 375
Cdd:cd01161 372 REYGVERVLRDLRIFRIFEGTNEILRLFIA 401
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
5-380 |
3.30e-96 |
|
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: 291.80 E-value: 3.30e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 5 LTEDQQAFRDAARAFAEKSMAPHAAQWDAEHIFPVDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELAAACPSTA 84
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 85 AFITIHNMATWMVASFASDDLRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVRDGESYVINGSKMFISGAGATDI 164
Cdd:cd01157 81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 165 LVLMARTgDAD---SGSKGISTFVIPADADGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGDGFAIAMKGLDG 241
Cdd:cd01157 161 YFLLARS-DPDpkcPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 242 GRLNIATCSLGGAQAALLRARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDSGDpEATLHCAMAK 321
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGR-RNTYYASIAK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952118256 322 RFATDACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRLLD 380
Cdd:cd01157 319 AFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
5-376 |
7.05e-79 |
|
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: 247.66 E-value: 7.05e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 5 LTEDQQAFRDAARAFAEKSMAPHAAQWDAEHIFPVDVMKEAGAMGFMGMyTPESLGGMGLSRLDTSVIVEELAAACPSTA 84
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 85 AFITIH-NMATWMVASFASDDLRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVRDGESYVINGSKMFISGAGATD 163
Cdd:cd01151 92 SFMSVQsSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 164 ILVLMARTGDADsgskGISTFVIPADADGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVgNEGDGFAIAMKGLDGGR 243
Cdd:cd01151 172 VFVVWARNDETG----KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNAR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 244 LNIATCSLGGAQAALLRARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQM-VRLGAFKlDSGD--PEATlhcAMA 320
Cdd:cd01151 247 YGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLAcLRVGRLK-DQGKatPEQI---SLL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952118256 321 KRFATDACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIAR 376
Cdd:cd01151 323 KRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
24-379 |
8.61e-74 |
|
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: 235.36 E-value: 8.61e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 24 MAPHAAQWDAE--------HIFPVDVMKEAGAM---GFMGMYTPESLGGMGLSRLDTSVIVEELAAAC-PSTAAFITIHN 91
Cdd:cd01153 13 LAPLNADGDREgpvfddgrVVVPPPFKEALDAFaeaGWMALGVPEEYGGQGLPITVYSALAEIFSRGDaPLMYASGTQGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 92 MATwmVASFASDDLRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVRDGE-SYVINGSKMFIS-GAGATD---ILV 166
Cdd:cd01153 93 AAT--LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISaGEHDMSeniVHL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 167 LMARTGDADSGSKGISTFVIP-----ADADGVSYGKNEEKMGWHSQPTRLVTLEDVRVPAsnrVGNEGDGFAIAMKGLDG 241
Cdd:cd01153 171 VLARSEGAPPGVKGLSLFLVPkflddGERNGVTVARIEEKMGLHGSPTCELVFDNAKGEL---IGEEGMGLAQMFAMMNG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 242 GRLNIATCSLGGAQAALLRARNYMHERQQFGKPLAAFQALQF--------KLADMVTNLVAARQMVRLGAFKLDSGDPEA 313
Cdd:cd01153 248 ARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIihhpdvrrSLMTQKAYAEGSRALDLYTATVQDLAERKA 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952118256 314 T-------------LHCAMAKRFATDACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRLL 379
Cdd:cd01153 328 TegedrkalsaladLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALDLIGRKI 406
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
21-382 |
1.84e-73 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 234.39 E-value: 1.84e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 21 EKSMAPHAAQWDAEHIFP--VDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELAAACPSTAAFITIH-NMATWMV 97
Cdd:PLN02519 42 QENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHsNLCINQL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 98 ASFASDDLRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVRDGESYVINGSKMFISGAGATDILVLMARTgDADSG 177
Cdd:PLN02519 122 VRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKT-DVAAG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 178 SKGISTFVIPADADGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGDGFAIAMKGLDGGRLNIATCSLGGAQAA 257
Cdd:PLN02519 201 SKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQAC 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 258 LLRARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDSG--DPEatlHCAMAKRFATDACFEVANEA 335
Cdd:PLN02519 281 LDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGkvDRK---DCAGVILCAAERATQVALQA 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1952118256 336 LQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRLLDDG 382
Cdd:PLN02519 358 IQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKEE 404
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-381 |
2.39e-71 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 228.07 E-value: 2.39e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 1 MDFNLTEDQQAFRDAARAFAEKSmAPHA--AQWDAEHIFPVDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELAA 78
Cdd:PRK12341 1 MDFSLTEEQELLLASIRELITRN-FPEEyfRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 79 ACpSTAAFIT----IHNMATwmvasFASDD-LRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVR-DGESYvINGS 152
Cdd:PRK12341 80 CG-APAFLITngqcIHSMRR-----FGSAEqLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRkNGKVY-LNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 153 KMFISGAGATDILVLMARTGDADSGSKGISTFVIPADADGVSYGKnEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGDGF 232
Cdd:PRK12341 153 KTFITGAKEYPYMLVLARDPQPKDPKKAFTLWWVDSSKPGIKINP-LHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 233 AIAMKGLDGGRLNIATCSLGGAQAALLRARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDSGDPe 312
Cdd:PRK12341 232 LNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQS- 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952118256 313 ATLHCAMAKRFATDACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRLLDD 381
Cdd:PRK12341 311 LRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKD 379
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
49-380 |
2.97e-56 |
|
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: 188.71 E-value: 2.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 49 GFMGMYTPESLGGMGLSRLDTSVIVEELAAACPSTAAFITIHNMATWMVASFASDDLRQEIVPRLASGE--WLASYclTE 126
Cdd:cd01152 48 GWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEeiWCQGF--SE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 127 PGAGSDAASLRTRAVRDGESYVINGSKMFISGAGATDILVLMARTGDADSGSKGISTFVIPADADGVSYGKNEEKMGWHS 206
Cdd:cd01152 126 PGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEAPKHRGISILLVDMDSPGVTVRPIRSINGGEF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 207 qpTRLVTLEDVRVPASNRVGNEGDGFAIAMKGLDGGRLNIAtcslGGAQAALLRARNYMHERQQFGKPLAAFQALQFKLA 286
Cdd:cd01152 206 --FNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIG----GSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 287 DMVTNLVAARQMVRLGAFKLDSG---DPEAtlhcAMAKRFATDACFEVANEALQLHGGYGYIREYPL--------ERYLR 355
Cdd:cd01152 280 RLEAEAEALRLLVFRLASALAAGkppGAEA----SIAKLFGSELAQELAELALELLGTAALLRDPAPgaelagrwEADYL 355
|
330 340
....*....|....*....|....*
gi 1952118256 356 DLRVHQILEGTNEIMRLIIARRLLD 380
Cdd:cd01152 356 RSRATTIYGGTSEIQRNIIAERLLG 380
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
1-381 |
1.10e-55 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 187.35 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 1 MDFNLTEDQQAFRDAARAFAEK-SMAPHAAQWDAEHIFPVDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELAAA 79
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELMASeNWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 80 CPSTAAFITIHNMATWMVASfASDDLRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVRDGESYVINGSKMFISGA 159
Cdd:PRK03354 81 GAPTYVLYQLPGGFNTFLRE-GTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 160 GATDILVLMARtgDADSGSKGIST-FVIPADADGVSYGKnEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGDGFAIAMKG 238
Cdd:PRK03354 160 AYTPYIVVMAR--DGASPDKPVYTeWFVDMSKPGIKVTK-LEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 239 LDGGRLNIATCSLGGAQAALLRARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDSGDPEATlHCA 318
Cdd:PRK03354 237 FDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSG-DAA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952118256 319 MAKRFATDACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRLLDD 381
Cdd:PRK03354 316 MCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
229-378 |
1.96e-50 |
|
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: 166.28 E-value: 1.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 229 GDGFAIAMKGLDGGRLNIATCSLGGAQAALLRARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDS 308
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 309 GDPEATLhCAMAKRFATDACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRL 378
Cdd:pfam00441 81 GGPDGAE-ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
26-379 |
1.05e-47 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 167.42 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 26 PHAAQWDAEHIFPVDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELAAACPSTAAFITIHNMAtwMVASF---AS 102
Cdd:PTZ00461 58 KHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSML--FVNNFyysAS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 103 DDLRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVRDG-ESYVINGSKMFISGAGATDILVLMARTgdadsgSKGI 181
Cdd:PTZ00461 136 PAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSnGNYVLNGSKIWITNGTVADVFLIYAKV------DGKI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 182 STFVIPADADGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGDGFAIAMKGLDGGRLNIATCSLGGAQAALLRA 261
Cdd:PTZ00461 210 TAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELM 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 262 RNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDSGDpEATLHCAMAKRFATDACFEVANEALQLHGG 341
Cdd:PTZ00461 290 TSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGN-KNRLGSDAAKLFATPIAKKVADSAIQVMGG 368
|
330 340 350
....*....|....*....|....*....|....*...
gi 1952118256 342 YGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRLL 379
Cdd:PTZ00461 369 MGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLL 406
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
21-379 |
1.54e-47 |
|
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: 166.41 E-value: 1.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 21 EKSMAPHAAQWDAEHIFPVDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELA----------AACPSTAafitih 90
Cdd:cd01155 26 LEYYAEGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGrsffapevfnCQAPDTG------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 91 NMAtwMVASFASDDLRQEIVPRLASGEWLASYCLTEPG-AGSDAASLRTRAVRDGESYVINGSKMFISGAGATD--ILVL 167
Cdd:cd01155 100 NME--VLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGDPRckIAIV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 168 MART-GDADSGSKGISTFVIPADADGVSYGKNEEKMGWHSQPT--RLVTLEDVRVPASNRVGNEGDGFAIAMKGLDGGRL 244
Cdd:cd01155 178 MGRTdPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 245 NIATCSLGGAQAAL----LRARNymheRQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDSGDPEATLH-CAM 319
Cdd:cd01155 258 HHCMRLIGAAERALelmcQRAVS----REAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAARKeIAM 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 320 AKRFATDACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRLL 379
Cdd:cd01155 334 IKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMEL 393
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
79-378 |
1.19e-42 |
|
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: 154.07 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 79 ACPstaafITIHNMATWMVASFASDDLRQEiVPRLASGE----WLASYCLTEPGAGSDAASLRTRAVRD-GESYVINGSK 153
Cdd:cd01154 110 LCP-----LTMTDAAVYALRKYGPEELKQY-LPGLLSDRyktgLLGGTWMTEKQGGSDLGANETTAERSgGGVYRLNGHK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 154 MFISGAGAtDILVLMARTGDADSGSKGISTFVIP-ADADGvsyGKN-------EEKMGWHSQPTRLVTLEDVrvpASNRV 225
Cdd:cd01154 184 WFASAPLA-DAALVLARPEGAPAGARGLSLFLVPrLLEDG---TRNgyrirrlKDKLGTRSVATGEVEFDDA---EAYLI 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 226 GNEGDGFAIAMKGLDGGRLNIATCSLGGAQAALLRARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFK 305
Cdd:cd01154 257 GDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 306 LD---SGDPE----ATLHCAMAKRFATDACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRL 378
Cdd:cd01154 337 FDraaADKPVeahmARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVL 416
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
5-378 |
2.79e-41 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 150.00 E-value: 2.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 5 LTEDQQAFRDAARAFAEKSMAPHAAQWDAEHIFPVDVMKEAGAMGFMGMyTPESLGGMGLSRLDTSVIVEELAAACPSTA 84
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGG-TIKGYGCPGLSITASAIATAEVARVDASCS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 85 AFITIHN-MATWMVASFASDDLRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVRDGESYVINGSKMFISGAGATD 163
Cdd:PLN02526 108 TFILVHSsLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 164 ILVLMARtgdaDSGSKGISTFVIPADADGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVGNEgDGFAIAMKGLDGGR 243
Cdd:PLN02526 188 VLVIFAR----NTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 244 LNIATCSLGGAQAALLRARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAarqMVRLG--AFKLDSGDPEATLHCAMAK 321
Cdd:PLN02526 263 VMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQA---MFLVGwrLCKLYESGKMTPGHASLGK 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952118256 322 RFATDACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIARRL 378
Cdd:PLN02526 340 AWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
49-379 |
8.78e-34 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 132.30 E-value: 8.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 49 GFMGMYTPESLGGMGLSRLDTSVIVEELAAACPSTAAFITIHNMATWMVASFASDDLRQEIVPRLASGEWLASYCLTEPG 128
Cdd:PTZ00456 112 GWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQ 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 129 AGSDAASLRTRAVRDGE-SYVINGSKMFISgAGATD-----ILVLMARTGDADSGSKGISTFVIP---ADADG-VSYGKN 198
Cdd:PTZ00456 192 CGTDLGQVKTKAEPSADgSYKITGTKIFIS-AGDHDlteniVHIVLARLPNSLPTTKGLSLFLVPrhvVKPDGsLETAKN 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 199 ------EEKMGWHSQPTRLVTLEDvrvPASNRVGNEGDGFAIAMKGLDGGRLNIATCSLGGA----QAALLRARNYMHER 268
Cdd:PTZ00456 271 vkciglEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAelafQNALRYARERRSMR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 269 QQFG--KPLAAFQALQFKlADMVTNLVAARQMVRLG-AFKLDSG--------DPEATLHCAM----------AKRFATDA 327
Cdd:PTZ00456 348 ALSGtkEPEKPADRIICH-ANVRQNILFAKAVAEGGrALLLDVGrlldihaaAKDAATREALdheigfytpiAKGCLTEW 426
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1952118256 328 CFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRL-IIARRLL 379
Cdd:PTZ00456 427 GVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVL 479
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
6-117 |
1.17e-33 |
|
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: 121.03 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 6 TEDQQAFRDAARAFAEKSMAPHAAQWDAEHIFPVDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELAAACPSTAA 85
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 1952118256 86 FITIHN-MATWMVASFASDDLRQEIVPRLASGE 117
Cdd:pfam02771 81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
121-215 |
1.89e-26 |
|
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: 101.59 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 121 SYCLTEPGAGSDAASLRTRAV-RDGESYVINGSKMFISGAGATDILVLMARTGDADsGSKGISTFVIPADADGVSYGKNE 199
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAAdGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDD-RHGGISLFLVPKDAPGVSVRRIE 79
|
90
....*....|....*.
gi 1952118256 200 EKMGWHSQPTRLVTLE 215
Cdd:pfam02770 80 TKLGVRGLPTGELVFD 95
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
102-376 |
1.19e-22 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 99.87 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 102 SDDLRQEIVPrLASGEWLASYCLTEPG-AGSDAASLRTRAVRDGESYVINGSKMFISGA--GATDILVLMARTGDADSGS 178
Cdd:PLN02876 535 KEQQLEWLIP-LLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTDFNAPKH 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 179 KGISTFVIPADADGVS-------YGKNEEKMGwHSQptrlVTLEDVRVPASNRVGNEGDGFAIAMKGLDGGRLNIATCSL 251
Cdd:PLN02876 614 KQQSMILVDIQTPGVQikrpllvFGFDDAPHG-HAE----ISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLI 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 252 GGAQaallRARNYMHE----RQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDS-GDPEATLHCAMAKRFATD 326
Cdd:PLN02876 689 GAAE----RGMQLMVQralsRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRlGNKKARGIIAMAKVAAPN 764
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1952118256 327 ACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNEIMRLIIAR 376
Cdd:PLN02876 765 MALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAK 814
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
40-343 |
2.17e-20 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 93.10 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 40 DVMKEAGamgFMGMYTPESLGGMGLSRLDTSVIVEELAAACPSTAAfitihnmaTWMV----------ASFASDDLRQEI 109
Cdd:PRK13026 115 DYLKKEG---FFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAV--------TVMVpnslgpgellTHYGTQEQKDYW 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 110 VPRLASGEWLASYCLTEPGAGSDAASLR-----TRAVRDGESYV---INGSKMFISGAGATDILVLMARTGD-----ADS 176
Cdd:PRK13026 184 LPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEVLglrLTWDKRYITLAPVATVLGLAFKLRDpdgllGDK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 177 GSKGISTFVIPADADGVSYGK--NEEKMGWHSQPTRlvtLEDVRVPASNRVG---NEGDGFAIAMKGLDGGRlNIATCSL 251
Cdd:PRK13026 264 KELGITCALIPTDHPGVEIGRrhNPLGMAFMNGTTR---GKDVFIPLDWIIGgpdYAGRGWRMLVECLSAGR-GISLPAL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 252 GGA--QAALLRARNYMHERQQFGKPLAAFQALQFKLADMVTN---LVAARQMVRLGafkLDSGDPEATLhCAMAKRFATD 326
Cdd:PRK13026 340 GTAsgHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNtylLEAARRLTTTG---LDLGVKPSVV-TAIAKYHMTE 415
|
330
....*....|....*..
gi 1952118256 327 ACFEVANEALQLHGGYG 343
Cdd:PRK13026 416 LARDVVNDAMDIHAGKG 432
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
49-346 |
1.52e-19 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 90.65 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 49 GFMGMYTPESLGGMGLSRLDTSVIVEELAAACpSTAAfitihnmATWMVAS----------FASDDLRQEIVPRLASGEW 118
Cdd:PRK09463 122 GFFGMIIPKEYGGLEFSAYAHSRVLQKLASRS-GTLA-------VTVMVPNslgpgelllhYGTDEQKDHYLPRLARGEE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 119 LASYCLTEPGAGSDAASLR-----TRAVRDGESYV---INGSKMFIS-GAGATdILVLMARTGDADS--GSK---GISTF 184
Cdd:PRK09463 194 IPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLgmrLTWNKRYITlAPIAT-VLGLAFKLYDPDGllGDKedlGITCA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 185 VIPADADGVSYGKNEEKMGWHSQ--PTRLvtlEDVRVPASNRVG---NEGDGFAIAMKGLDGGR-LNIATCSLGGAQAAL 258
Cdd:PRK09463 273 LIPTDTPGVEIGRRHFPLNVPFQngPTRG---KDVFIPLDYIIGgpkMAGQGWRMLMECLSVGRgISLPSNSTGGAKLAA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 259 LRARNYMHERQQFGKPLAAFQALQFKLADMVTNLVAARQMVRLGAFKLDSGDPEATLhCAMAKRFATDACFEVANEALQL 338
Cdd:PRK09463 350 LATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLGEKPSVL-SAIAKYHLTERGRQVINDAMDI 428
|
....*...
gi 1952118256 339 HGGYGYIR 346
Cdd:PRK09463 429 HGGKGICL 436
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
25-360 |
3.31e-16 |
|
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: 79.29 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 25 APHAAQWDAEHIFPVDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELAAACPSTAAFITIHNMATWMVASFASDD 104
Cdd:cd01163 11 AEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVEALLLAGPEQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 105 LRQEIVPRLASGEWLAsycltepGAGSDAASLR-----TRAVRDGESYVINGSKMFISGAGATDILVLMArtgdADSGSK 179
Cdd:cd01163 91 FRKRWFGRVLNGWIFG-------NAVSERGSVRpgtflTATVRDGGGYVLNGKKFYSTGALFSDWVTVSA----LDEEGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 180 GIStFVIPADADGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGDGFAIAMKGLdGGRLNIATCSLGGAQAALL 259
Cdd:cd01163 160 LVF-AAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAGIARAALD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 260 RARNYMHERQQFGKPLAAFQA-----LQFKLADMVTNLVAARQMVRLGAFKLD-------SGDPEATLHCAM----AKRF 323
Cdd:cd01163 238 DAVAYVRSRTRPWIHSGAESArddpyVQQVVGDLAARLHAAEALVLQAARALDaaaaagtALTAEARGEAALavaaAKVV 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 1952118256 324 ATDACFEVANEALQLHGGYGYIREYPLERYLRDLRVH 360
Cdd:cd01163 318 VTRLALDATSRLFEVGGASATAREHNLDRHWRNARTH 354
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
246-368 |
5.00e-16 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 73.92 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 246 IATCSLGGAQAALLRARNYMHERQQ--FGKPLAAFQALQFKLADMVTNLVAARQMVRLGA----FKLDSGDPEATLHCA- 318
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVTPALRAe 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1952118256 319 --MAKRFATDACFEVANEALQLHGGYGYIREYPLERYLRDLRVHQILEGTNE 368
Cdd:pfam08028 82 arRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
27-359 |
1.74e-15 |
|
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: 77.00 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 27 HAAQWDAEHIFPVDVMKEAGAMGFMGMYTPESLGGMGLSRLDTSVIVEELAAACPSTAAFITIHNMATWMVASFaSDDLR 106
Cdd:cd01159 13 RAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATHSRMLAAF-PPEAQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 107 QEIvprlasgewlasycLTEPGAGSDAASLRT--RAVRDGESYVINGSKMFISGAGATDILVLMARTGDADsGSKGISTF 184
Cdd:cd01159 92 EEV--------------WGDGPDTLLAGSYAPggRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDD-GGPLPRAF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 185 VIPADadGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASnRVGNEGDGFAI--AMKGLDGGR--------LNIATCSLGGA 254
Cdd:cd01159 157 VVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEH-RTLTAGDMMAGdgPGGSTPVYRmplrqvfpLSFAAVSLGAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 255 QAALLRARNYMHERQQ---FGKPLAAFQALQFKLADMVTNLVAA-----RQMVRLGAFKLDSG--DPEATLHCAMAKRFA 324
Cdd:cd01159 234 EGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAArafleRATRDLWAHALAGGpiDVEERARIRRDAAYA 313
|
330 340 350
....*....|....*....|....*....|....*
gi 1952118256 325 TDACFEVANEALQLHGGYGYIREYPLERYLRDLRV 359
Cdd:cd01159 314 AKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHA 348
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
124-378 |
1.20e-13 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 72.09 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 124 LTEPGAGSDAASLRTRAVR-DGESYVINGSKMFISGAGATDILVLMARTGdadsgskGISTFVIP-----ADADGVSYGK 197
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERlADGSYRLVGHKWFFSVPQSDAHLVLAQAKG-------GLSCFFVPrflpdGQRNAIRLER 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 198 NEEKMGWHSQPTRLVTLEDvrvpASN-RVGNEGDGF--AIAMKGLDggRLNIATCSLGGAQAALLRARNYMHERQQFGKP 274
Cdd:PRK11561 257 LKDKLGNRSNASSEVEFQD----AIGwLLGEEGEGIrlILKMGGMT--RFDCALGSHGLMRRAFSVAIYHAHQRQVFGKP 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 275 LAAFQALQFKLADMVTNLVAARQMV-RLGAFKLDSGDPEATlhcAMAKRFATDACFEVAN-------EALQLHGGYGYIR 346
Cdd:PRK11561 331 LIEQPLMRQVLSRMALQLEGQTALLfRLARAWDRRADAKEA---LWARLFTPAAKFVICKrgipfvaEAMEVLGGIGYCE 407
|
250 260 270
....*....|....*....|....*....|..
gi 1952118256 347 EYPLERYLRDLRVHQILEGTNEIMRLIIARRL 378
Cdd:PRK11561 408 ESELPRLYREMPVNSIWEGSGNIMCLDVLRVL 439
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
97-379 |
8.73e-11 |
|
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: 63.50 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 97 VASFASDDLRQEIVPRLASGEWLASYCLTEPGAGSDAASLRTRAVRD--GESYVIN-----GSKMFISGAGATDIL-VLM 168
Cdd:cd01150 113 IKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDplTQEFVINtpdftATKWWPGNLGKTATHaVVF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 169 AR--TGDADsgsKGISTFVIPA-DAD------GVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGD--------- 230
Cdd:cd01150 193 AQliTPGKN---HGLHAFIVPIrDPKthqplpGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDvspdgtyvs 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 231 -------GFAIAMKGLDGGRLNIATCSLGGAQAALLRARNYMHERQQFGKP---------------------LAAFQALQ 282
Cdd:cd01150 270 pfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKpsdpevqildyqlqqyrlfpqLAAAYAFH 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 283 FKLADMVTNLVAARQMVRLGAFKLdsgDPEATLHCAMAKRFATDACFEVANEALQLHGGYGYIReyplERYLRDLR---- 358
Cdd:cd01150 350 FAAKSLVEMYHEIIKELLQGNSEL---LAELHALSAGLKAVATWTAAQGIQECREACGGHGYLA----MNRLPTLRddnd 422
|
330 340
....*....|....*....|.
gi 1952118256 359 VHQILEGTNEIMRLIIARRLL 379
Cdd:cd01150 423 PFCTYEGDNTVLLQQTANYLL 443
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
60-236 |
3.44e-10 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 61.44 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 60 GGMGLSRLDTSVIVEELAAACPSTAAFITIH-NMATWMVASFASDDLRQEIVPRLASGEWLASYClTEPGAGSDAASLRT 138
Cdd:PTZ00457 75 GGLGLGHTAHALIYEEVGTNCDSKLLSTIQHsGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISMNTT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 139 RAV-RDGESYVINGSKMFISGAGATDILVLmARTGDADSGSKGIST------FVIPADADGVSYGKNeekmgwhsqptrL 211
Cdd:PTZ00457 154 KASlTDDGSYVLTGQKRCEFAASATHFLVL-AKTLTQTAAEEGATEvsrnsfFICAKDAKGVSVNGD------------S 220
|
170 180
....*....|....*....|....*
gi 1952118256 212 VTLEDvrVPASNRVGNEGDGFAIAM 236
Cdd:PTZ00457 221 VVFEN--TPAADVVGVVGEGFKDAM 243
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
117-379 |
1.33e-03 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 41.00 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 117 EWLASYCLTEPGAGSDAASLRTRAVRD--GESYVIN-----GSKMFISGAG-----ATDILVLMARTGDADSGSK-GIST 183
Cdd:PLN02636 172 DYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVINtpndgAIKWWIGNAAvhgkfATVFARLKLPTHDSKGVSDmGVHA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 184 FVIPADA-------DGVSYGKNEEKMGWHSQPTRLVTLEDVRVPASNRVGNEGD----------------GFAIAMKGLD 240
Cdd:PLN02636 252 FIVPIRDmkthqvlPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDvsrdgkytsslptinkRFAATLGELV 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952118256 241 GGRLNIATCSLGGAQAALLRARNYMHERQQFGKP------LAAFQALQFKLADMVTNL----VAARQMVRLGAFKLDSGD 310
Cdd:PLN02636 332 GGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQHKLMPMLASTyafhFATEYLVERYSEMKKTHD 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952118256 311 PE--ATLHCAMA--KRFATDACFEVANEALQLHGGYGYIreyPLERY--LR-DLRVHQILEGTNEIMRLIIARRLL 379
Cdd:PLN02636 412 DQlvADVHALSAglKAYITSYTAKALSTCREACGGHGYA---AVNRFgsLRnDHDIFQTFEGDNTVLLQQVAADLL 484
|
|
| |
