|
Name |
Accession |
Description |
Interval |
E-value |
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
26-404 |
0e+00 |
|
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: 759.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 26 LTPEQAELRQTMAKFLQEHLAPKAQEIDRSNEFknLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGA 105
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEF--PRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 106 VGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPD 185
Cdd:cd01156 80 VALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 186 ADVLIVYAKTDLAavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLD 265
Cdd:cd01156 160 ADTLVVYAKTDPS--AGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 266 LERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVI 345
Cdd:cd01156 238 YERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVI 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238812321 346 LYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNA 404
Cdd:cd01156 318 LYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
30-400 |
0e+00 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 619.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 30 QAELRQTMAKFLQEHLAPKAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLS 109
Cdd:PLN02519 30 QLQFKESVQQFAQENIAPHAAAIDATNSFPKDVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 110 YGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVL 189
Cdd:PLN02519 110 YGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 190 IVYAKTDLAAvpASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERL 269
Cdd:PLN02519 190 VVYAKTDVAA--GSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 270 VLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSA 349
Cdd:PLN02519 268 VLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAA 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1238812321 350 ECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGR 400
Cdd:PLN02519 348 ERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR 398
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
25-401 |
1.49e-165 |
|
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: 469.32 E-value: 1.49e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 25 SLTPEQAELRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASG 104
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFP--RELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 105 AVGLSYGAHsNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGP 184
Cdd:COG1960 82 SLALPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 185 DADVLIVYAKTDLAavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGL 264
Cdd:COG1960 161 VADVILVLARTDPA--AGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 265 DLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGV 344
Cdd:COG1960 239 NAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1238812321 345 ILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRA 401
Cdd:COG1960 319 KLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARR 375
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
28-401 |
7.67e-148 |
|
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: 423.99 E-value: 7.67e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 28 PEQAELRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVG 107
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFP--REVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 108 LSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDAD 187
Cdd:cd01158 79 VIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 188 VLIVYAKTDLAAvpASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLE 267
Cdd:cd01158 159 FYIVFAVTDPSK--GYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 268 RLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILY 347
Cdd:cd01158 237 RIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLF 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1238812321 348 SAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRA 401
Cdd:cd01158 317 ASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKH 370
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
28-400 |
1.46e-126 |
|
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: 368.15 E-value: 1.46e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 28 PEQAELRQTMAKFLQEHLAPKAQEIDRSNEFknLREFWKQLGNLGVlgitapvqyggsglgylehvlvmeeisrasgavg 107
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEE--PWELLAELGLLLG---------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 108 lsygahsnlcINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDAD 187
Cdd:cd00567 45 ----------AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDAD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 188 VLIVYAKTDLAAvPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLE 267
Cdd:cd00567 115 LFIVLARTDEEG-PGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 268 RLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHC-TAKDCAGVIL 346
Cdd:cd00567 194 RLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKL 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1238812321 347 YSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGR 400
Cdd:cd00567 274 FATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
28-400 |
1.56e-108 |
|
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: 324.07 E-value: 1.56e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 28 PEQAELRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRAsGAVG 107
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVP--REVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARA-GGSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 108 LSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDAD 187
Cdd:cd01160 78 PGLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 188 VLIVYAKTDLAAVPASrGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLE 267
Cdd:cd01160 158 VVIVVARTGGEARGAG-GISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 268 RLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGH------CTAKDC 341
Cdd:cd01160 237 RLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRldvaeaSMAKYW 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238812321 342 AGvilysaECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGR 400
Cdd:cd01160 317 AT------ELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
27-392 |
1.30e-105 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 318.03 E-value: 1.30e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 27 TPEQAELRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAV 106
Cdd:PTZ00461 38 TPEHAALRETVAKFSREVVDKHAREDDINMHFN--RDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 107 GLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGN-HYILNGNKFWITNGPD 185
Cdd:PTZ00461 116 CLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 186 ADVLIVYAKTDlaavpasRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLD 265
Cdd:PTZ00461 196 ADVFLIYAKVD-------GKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 266 LERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVI 345
Cdd:PTZ00461 269 LERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAK 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1238812321 346 LYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSE 392
Cdd:PTZ00461 349 LFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
26-401 |
1.78e-98 |
|
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: 298.20 E-value: 1.78e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 26 LTPEQAELRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGA 105
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFP--VDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 106 VGlSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPD 185
Cdd:cd01162 79 TA-AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 186 ADVLIVYAKTDlaaVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLD 265
Cdd:cd01162 158 SDVYVVMARTG---GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 266 LERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTA-KDCAGV 344
Cdd:cd01162 235 GGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAvKLCAMA 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1238812321 345 ILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRA 401
Cdd:cd01162 315 KRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARA 371
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
20-398 |
1.96e-97 |
|
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: 296.69 E-value: 1.96e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 20 QSVCSSLTPEQAELRQTMAKFLQEHLAPKAQEIDRSNEFKNL-------REFWKQLGNLGVLGITAPVQYGGSGLGYLEH 92
Cdd:cd01161 10 DIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNdqlekipRKTLTQLKELGLFGLQVPEEYGGLGLNNTQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 93 VLVMEEISRASGaVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKK--GNH 170
Cdd:cd01161 90 ARLAEIVGMDLG-FSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 171 YILNGNKFWITNGPDADVLIVYAKTDLAAVPASR--GITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAAN 248
Cdd:cd01161 169 YVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVkdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVEN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 249 ILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVA 328
Cdd:cd01161 249 VLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTS 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238812321 329 KACDEGHCT--AKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVI 398
Cdd:cd01161 329 GNMDRGLKAeyQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
26-400 |
1.65e-85 |
|
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: 265.22 E-value: 1.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 26 LTPEQAELRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEIsrASGA 105
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYP--WPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEEL--AYGC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 106 VGLSYGAHSN-LCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGP 184
Cdd:cd01157 77 TGVQTAIEANsLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 185 DADVLIVYAKTDL-AAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSG 263
Cdd:cd01157 157 KANWYFLLARSDPdPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 264 LDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAG 343
Cdd:cd01157 237 FDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASI 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1238812321 344 VILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGR 400
Cdd:cd01157 317 AKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISR 373
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
24-402 |
5.85e-84 |
|
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: 261.52 E-value: 5.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 24 SSLTPEQAELRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITaPVQYGGSGLGYLEHVLVMEEISRAS 103
Cdd:cd01151 11 DLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFD--RKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 104 GAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNG 183
Cdd:cd01151 88 SGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 184 PDADVLIVYAKTDLAAvpasrGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENkGVYVLMSG 263
Cdd:cd01151 168 PIADVFVVWARNDETG-----KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAE-GLRGPFKC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 264 LDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAG 343
Cdd:cd01151 242 LNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISL 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238812321 344 VILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAK---LYEigaGTSEVRRLVIGRAF 402
Cdd:cd01151 322 LKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLEsvnTYE---GTHDIHALILGRAI 380
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
25-401 |
5.63e-67 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 217.29 E-value: 5.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 25 SLTPEQ----AELRQTMAK-FLQEHLApkaqEIDRSNEFKnlREFWKQLGN--LGVLGItaPVQYGGSGLGYLEHVLVME 97
Cdd:PRK12341 4 SLTEEQelllASIRELITRnFPEEYFR----TCDENGTYP--REFMRALADngISMLGV--PEEFGGTPADYVTQMLVLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 98 EISRASGAVglsYGAHSNLCINQLVRNGNEAQKEK-YLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGN 176
Cdd:PRK12341 76 EVSKCGAPA---FLITNGQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 177 KFWITNGPDADVLIVYAKTDLAAVPASRgITAFIVEKGMPGFSTsKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKG 256
Cdd:PRK12341 153 KTFITGAKEYPYMLVLARDPQPKDPKKA-FTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 257 VYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHC 336
Cdd:PRK12341 231 FLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQS 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238812321 337 TAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRA 401
Cdd:PRK12341 311 LRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQ 375
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
25-401 |
3.25e-52 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 178.87 E-value: 3.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 25 SLTPEQ----AELRQTMAKflqEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEIS 100
Cdd:PRK03354 4 NLNDEQelfvAGIRELMAS---ENWEAYFAECDRDSVYP--ERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 101 RASGAVGLSYGAHSNlcINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWI 180
Cdd:PRK03354 79 RLGAPTYVLYQLPGG--FNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 181 TNGPDADVLIVYAKTdlAAVPASRGITAFIVEKGMPGFSTSKkLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVL 260
Cdd:PRK03354 157 TSSAYTPYIVVMARD--GASPDKPVYTEWFVDMSKPGIKVTK-LEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 261 MSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKD 340
Cdd:PRK03354 234 KEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGD 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238812321 341 CAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRA 401
Cdd:PRK03354 314 AAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRA 374
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
28-401 |
9.07e-50 |
|
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: 172.53 E-value: 9.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 28 PEQAELRQTMAKFLQEHLAP---KAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRAsG 104
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPelrEESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAA-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 105 AVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGP 184
Cdd:cd01152 80 APVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 185 DADVLIVYAKTDLaAVPASRGITAFIVEKGMPGFsTSKKLDKLgMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGL 264
Cdd:cd01152 160 YADWAWLLVRTDP-EAPKHRGISILLVDMDSPGV-TVRPIRSI-NGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 265 DLERLVLAGGPLGLMQAVLDhtipYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGV 344
Cdd:cd01152 237 NFERVSIGGSAATFFELLLA----RLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIA 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238812321 345 ILYSAECATQVALDGIQCFG-----GNGYINDFPMGRFLRD---AKLYEIGAGTSEVRRLVIGRA 401
Cdd:cd01152 313 KLFGSELAQELAELALELLGtaallRDPAPGAELAGRWEADylrSRATTIYGGTSEIQRNIIAER 377
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
27-141 |
1.03e-49 |
|
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: 163.79 E-value: 1.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 27 TPEQAELRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAV 106
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFP--RELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASV 78
|
90 100 110
....*....|....*....|....*....|....*
gi 1238812321 107 GLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGE 141
Cdd:pfam02771 79 ALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
26-400 |
1.60e-48 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 170.03 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 26 LTPEQAELRQTMAKFLQEHLAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPvQYGGSGLGYLEHVLVMEEISRASGA 105
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFP--FHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 106 VGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPD 185
Cdd:PLN02526 106 CSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 186 ADVLIVYAKTdlaavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDC------KIPAANILGHENKgvyv 259
Cdd:PLN02526 186 ADVLVIFARN-----TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVfvpdedRLPGVNSFQDTNK---- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 260 lmsGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAK 339
Cdd:PLN02526 257 ---VLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPG 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238812321 340 DCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGR 400
Cdd:PLN02526 334 HASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGR 394
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
36-400 |
3.19e-47 |
|
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: 166.41 E-value: 3.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 36 TMAKFLQEHLAPKAQEIDRSN-EFKNLR--------EFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAV 106
Cdd:cd01153 4 EVARLAENVLAPLNADGDREGpVFDDGRvvvpppfkEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 107 GLSYGAHSnlCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGN-HYILNGNKFWITNG-- 183
Cdd:cd01153 84 MYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGeh 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 184 --PDADVLIVYAKTDlAAVPASRGITAFIVEK----GMPGFSTSKKLD-KLGMRGSNTCELIFEDCKipaANILGHENKG 256
Cdd:cd01153 162 dmSENIVHLVLARSE-GAPPGVKGLSLFLVPKflddGERNGVTVARIEeKMGLHGSPTCELVFDNAK---GELIGEEGMG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 257 VYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQ--------KIGHFQLMQGKMADMYTRLMACRQYVYNVA 328
Cdd:cd01153 238 LAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDlikaapavTIIHHPDVRRSLMTQKAYAEGSRALDLYTA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 329 KACDEGH---------CTAKDCAGVIL-----YSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVR 394
Cdd:cd01153 318 TVQDLAErkategedrKALSALADLLTpvvkgFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQ 397
|
....*..
gi 1238812321 395 RL-VIGR 400
Cdd:cd01153 398 ALdLIGR 404
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
254-401 |
2.69e-43 |
|
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: 148.17 E-value: 2.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 254 NKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDE 333
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238812321 334 GHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRA 401
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARR 148
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
121-404 |
5.09e-37 |
|
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: 139.04 E-value: 5.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 121 LVRNGNEAQKEkYLPKLISGEY----IGALAMSEPNAGSDVVSMKLKAEK-KGNHYILNGNKfWITNGPDADVLIVYAKT 195
Cdd:cd01154 123 LRKYGPEELKQ-YLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLARP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 196 DlAAVPASRGITAFIVEKGMP-----GFSTSKKLDKLGMRGSNTCELIFEDCKipaANILGHENKGVYVLMSGLDLERLV 270
Cdd:cd01154 201 E-GAPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDAE---AYLIGDEGKGIYYILEMLNISRLD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 271 LAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDE-GHCTAKDCAGVIL--- 346
Cdd:cd01154 277 NAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRaAADKPVEAHMARLatp 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238812321 347 ----YSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNA 404
Cdd:cd01154 357 vaklIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVLVK 418
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
59-400 |
6.07e-33 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 130.37 E-value: 6.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 59 KNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAV----GLSYGAhsnlcINQLVRNGNEAQKEKYL 134
Cdd:PTZ00456 99 KGFKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFsmypGLSIGA-----ANTLMAWGSEEQKEQYL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 135 PKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGN-HYILNGNKFWITNGpDAD-----VLIVYAKTDlAAVPASRGITA 208
Cdd:PTZ00456 174 TKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAG-DHDlteniVHIVLARLP-NSLPTTKGLSL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 209 FIVEKGMP----GFSTSKKLD------KLGMRGSNTCELIFEDCKipaANILGHENKGVYVLMSGLDLERLVLAGGPLGL 278
Cdd:PTZ00456 252 FLVPRHVVkpdgSLETAKNVKciglekKMGIKGSSTCQLSFENSV---GYLIGEPNAGMKQMFTFMNTARVGTALEGVCH 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 279 MQAVLDHTIPYlhVREAFGQKighfQLMQGKMADMYTRLMAC----RQYVYnVAKACDEG--------------HCTAKD 340
Cdd:PTZ00456 329 AELAFQNALRY--ARERRSMR----ALSGTKEPEKPADRIIChanvRQNIL-FAKAVAEGgrallldvgrlldiHAAAKD 401
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238812321 341 CAG-------VILYS-------AECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRL-VIGR 400
Cdd:PTZ00456 402 AATrealdheIGFYTpiakgclTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGR 476
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
145-240 |
9.66e-33 |
|
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: 118.54 E-value: 9.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 145 ALAMSEPNAGSDVVSMKLKA-EKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvpASRGITAFIVEKGMPGFSTSKK 223
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDD--RHGGISLFLVPKDAPGVSVRRI 78
|
90
....*....|....*..
gi 1238812321 224 LDKLGMRGSNTCELIFE 240
Cdd:pfam02770 79 ETKLGVRGLPTGELVFD 95
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
32-401 |
1.28e-32 |
|
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: 126.74 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 32 ELRQTMAKFLQEHLAPKAQEIDRSNE------------FKNLREFWKQLG--NLGVlgitaPVQYGGSGLGYLEHVLVME 97
Cdd:cd01155 5 ELRARVKAFMEEHVYPAEQEFLEYYAeggdrwwtpppiIEKLKAKAKAEGlwNLFL-----PEVSGLSGLTNLEYAYLAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 98 EISR---ASGAVGLSYGAHSNLCInqLVRNGNEAQKEKYLPKLISGEYIGALAMSEPN-AGSDVVSMKLKAEKKGNHYIL 173
Cdd:cd01155 80 ETGRsffAPEVFNCQAPDTGNMEV--LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 174 NGNKFWITNG--PDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKLDKLG---MRGSNtCELIFEDCKIPAAN 248
Cdd:cd01155 158 NGRKWWSSGAgdPRCKIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGyddAPHGH-AEITFDNVRVPASN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 249 ILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVA 328
Cdd:cd01155 237 LILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAA 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238812321 329 KACDEGhcTAKDCAGVILYSAECATQVALD----GIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRA 401
Cdd:cd01155 317 HMIDTV--GNKAARKEIAMIKVAAPRMALKiidrAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARM 391
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
32-393 |
6.16e-19 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 89.08 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 32 ELRQTMAKFLQEHLAPKAQEIDR---SN-------EFKNLREFWKQLG--NL--------------------GVLGITAP 79
Cdd:PLN02876 408 ELRKKLIKFMEDHIYPMENEFYKlaqSSsrwtvhpEEERLKELAKKEGlwNLwipldsaararkllfednkhMVSGDSAD 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 80 vQYGGSGLGYLEHVLVMEEISRASGAVG-LSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPN-AGSDV 157
Cdd:PLN02876 488 -QLLGAGLSNLEYGYLCEIMGRSVWAPQvFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDA 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 158 VSMKLKAEKKGNHYILNGNKFWiTNG---PDADVLIVYAKTDLAAvPASRGITAFIVEKGMPGFSTSKKLDKLGMRGS-- 232
Cdd:PLN02876 567 TNIECSIRRQGDSYVINGTKWW-TSGamdPRCRVLIVMGKTDFNA-PKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAph 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 233 NTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERL----VLAGGPLGLMQAVLDHTIPylhvREAFGQKIGHFQLMQG 308
Cdd:PLN02876 645 GHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLhhcmRLIGAAERGMQLMVQRALS----RKAFGKLIAQHGSFLS 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 309 KMADMYTRLMACRQYVYNVAKACDE-GHCTAKdcaGVILYSAECATQVAL----DGIQCFGGNGYINDFPMGRFLRDAKL 383
Cdd:PLN02876 721 DLAKCRVELEQTRLLVLEAADQLDRlGNKKAR---GIIAMAKVAAPNMALkvldMAMQVHGAAGVSSDTVLAHLWATART 797
|
410
....*....|
gi 1238812321 384 YEIGAGTSEV 393
Cdd:PLN02876 798 LRIADGPDEV 807
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
45-289 |
6.02e-15 |
|
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: 75.82 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 45 LAPKAQEIDRSNEFKnlREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLcINQLVRN 124
Cdd:cd01163 10 IAEGAAERDRQRGLP--YEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGF-VEALLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 125 GNEAQKEKYLPKLISGEYIGAlAMSE---PNAGSDVVSMklkaEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvp 201
Cdd:cd01163 87 GPEQFRKRWFGRVLNGWIFGN-AVSErgsVRPGTFLTAT----VRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 202 asrgITAFIVEKGMPGFSTSKKLDKLGMR--GSNTceLIFEDCKIPAANILGHENKGVYVLMSGLdLERLVLAGGPLGLM 279
Cdd:cd01163 160 ----LVFAAVPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAGIA 232
|
250
....*....|
gi 1238812321 280 QAVLDHTIPY 289
Cdd:cd01163 233 RAALDDAVAY 242
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
51-313 |
1.07e-14 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 76.15 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 51 EIDRSNEFKNL-REFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRN-GNEA 128
Cdd:PRK13026 99 DWDIVQNRKDLpPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLGPGELLTHyGTQE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 129 QKEKYLPKLISGEYIGALAMSEPNAGSDVVSMK-----LKAEKKGNHYI---LNGNKFWITNGPDADVL----IVYAKTD 196
Cdd:PRK13026 179 QKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEVLglrLTWDKRYITLAPVATVLglafKLRDPDG 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 197 LAAVPASRGITAFIVEKGMPGFSTSKKLDKLGMR---GSNTCELIFedckIPAANILG---HENKGVYVLMSGLDLERlv 270
Cdd:PRK13026 259 LLGDKKELGITCALIPTDHPGVEIGRRHNPLGMAfmnGTTRGKDVF----IPLDWIIGgpdYAGRGWRMLVECLSAGR-- 332
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1238812321 271 laGGPLGLMQAVLDH-----TIPYLHVREAFGQKIGHFQLMQGKMADM 313
Cdd:PRK13026 333 --GISLPALGTASGHmatrtTGAYAYVRRQFGMPIGQFEGVQEALARI 378
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
63-367 |
2.59e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 71.77 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 63 EFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQ-LVRNGNEAQKEKYLPKLISGE 141
Cdd:PRK09463 113 EVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLGPGElLLHYGTDEQKDHYLPRLARGE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 142 YIGALAMSEPNAGSDVVSMK-----LKAEKKGNHYI---LNGNKFWITNGPDADVL-----------IVYAKTDLaavpa 202
Cdd:PRK09463 193 EIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLgmrLTWNKRYITLAPIATVLglafklydpdgLLGDKEDL----- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 203 srGITAFIVEKGMPGFSTSKKLDKLG---MRGSNTCELIFedckIPAANILG---HENKGVYVLMSGLDLERLV-LAGGP 275
Cdd:PRK09463 268 --GITCALIPTDTPGVEIGRRHFPLNvpfQNGPTRGKDVF----IPLDYIIGgpkMAGQGWRMLMECLSVGRGIsLPSNS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 276 LGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADM--YTRLM-ACRQYvynVAKACDEGHCTAKDCAGVILYSAECA 352
Cdd:PRK09463 342 TGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIagNAYLMdAARTL---TTAAVDLGEKPSVLSAIAKYHLTERG 418
|
330
....*....|....*
gi 1238812321 353 TQVALDGIQCFGGNG 367
Cdd:PRK09463 419 RQVINDAMDIHGGKG 433
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
140-403 |
1.07e-11 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 66.31 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 140 GEYIGaLAMSEPNAGSDVVSMKLKAEK-KGNHYILNGNKfWITNGPDADVLIVYAKTDlaavpasRGITAFIVEKGMP-G 217
Cdd:PRK11561 177 GLLIG-MGMTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAK-------GGLSCFFVPRFLPdG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 218 FSTSKKL----DKLGMRGSNTCELIFEDCkipAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVR 293
Cdd:PRK11561 248 QRNAIRLerlkDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQR 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 294 EAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEgHCTAKDCAGVILYSAECATQVALDGI-------QCFGGN 366
Cdd:PRK11561 325 QVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDR-RADAKEALWARLFTPAAKFVICKRGIpfvaeamEVLGGI 403
|
250 260 270
....*....|....*....|....*....|....*..
gi 1238812321 367 GYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFN 403
Cdd:PRK11561 404 GYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLN 440
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
59-283 |
4.36e-11 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 64.52 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 59 KNLREFWKQLGNLGvlGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLI 138
Cdd:PTZ00457 53 EQIRSNDKILGNLY--GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 139 SGEYIGALAMSEPNaGSDVVSMKLKAEKKGN-HYILNGNKFWItNGPDADVLIVYAKT------DLAAVPASRgITAFIV 211
Cdd:PTZ00457 131 DGTIMMGWATEEGC-GSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKTltqtaaEEGATEVSR-NSFFIC 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238812321 212 EKGMPGFSTskkldklgmrgsNTCELIFEDckIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVL 283
Cdd:PTZ00457 208 AKDAKGVSV------------NGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVV 265
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
96-263 |
7.65e-08 |
|
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: 54.26 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 96 MEEISRASGAVGLSYGA----HSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGN 169
Cdd:cd01150 84 MLALTNSLGGYDLSLGAklglHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 170 HYILN-----GNKFWITN-GPDADVLIVYAKTdlaAVPASR-GITAFIVE-------KGMPGFSTSKKLDKLGMRGSNTC 235
Cdd:cd01150 164 EFVINtpdftATKWWPGNlGKTATHAVVFAQL---ITPGKNhGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNG 240
|
170 180
....*....|....*....|....*...
gi 1238812321 236 ELIFEDCKIPAANILgheNKGVYVLMSG 263
Cdd:cd01150 241 FLQFRNVRIPRENLL---NRFGDVSPDG 265
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
95-313 |
6.76e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 51.40 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 95 VMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGNHYI 172
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 173 LN-----GNKFWITNGP-DADVLIVYAKTDLAAvPASRGIT-----AFIV-------EKGMPGFSTSKKLDKLGMRGSNT 234
Cdd:PLN02636 206 INtpndgAIKWWIGNAAvHGKFATVFARLKLPT-HDSKGVSdmgvhAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDN 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 235 CELIFEDCKIPAANILGH----------------ENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQ 298
Cdd:PLN02636 285 GALRFRSVRIPRDNLLNRfgdvsrdgkytsslptINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGP 364
|
250 260
....*....|....*....|.
gi 1238812321 299 ------KIGHFQLMQGKMADM 313
Cdd:PLN02636 365 pkqpeiSILDYQSQQHKLMPM 385
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
125-250 |
1.49e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 47.15 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 125 GNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGNHYILN-----GNKFWITN-GPDADVLIVYAKtd 196
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAK-- 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238812321 197 LAAVPASRGITAFIVE-------KGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANIL 250
Cdd:PTZ00460 188 LIVNGKNKGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLL 248
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
43-381 |
1.14e-04 |
|
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: 43.88 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 43 EHLAPKAQEidRSNEFKNLREFWKQ----LGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVG---LSYGAHSn 115
Cdd:cd01159 4 EDLAPLIRE--RAPEAERARRLPDEvvraLREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAwvaSIVATHS- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 116 lciNQLVRNGNEAQKEKYlpklisGEYIGALAmsepnagSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAK- 194
Cdd:cd01159 81 ---RMLAAFPPEAQEEVW------GDGPDTLL-------AGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 195 TDLAAVPASRgitAFIVEKGmpGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILghENKGVYVL---MSGLDLER--- 268
Cdd:cd01159 145 EDDDGGPLPR---AFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTL--TAGDMMAGdgpGGSTPVYRmpl 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238812321 269 -----LVLAGGPLGLMQAVLDhtipylHVREAFGQKIGHF---------QLMQGKMADMYTRLMACRQYVYNVAKACDEG 334
Cdd:cd01159 218 rqvfpLSFAAVSLGAAEGALA------EFLELAGKRVRQYgaavkmaeaPITQLRLAEAAAELDAARAFLERATRDLWAH 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238812321 335 HCTAK------------DCAGVILYSAECATQVALDGiqcfGGNGYINDFPMGRFLRDA 381
Cdd:cd01159 292 ALAGGpidveerarirrDAAYAAKLSAEAVDRLFHAA----GGSALYTASPLQRIWRDI 346
|
|
| |
