|
Name |
Accession |
Description |
Interval |
E-value |
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
42-421 |
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: 747.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 42 GLNEEQKQLRHTISKFVQENLAPKAQEIDQSNDFknLREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASA 121
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEF--PRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 122 AVGLSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNGP 201
Cdd:cd01156 79 SVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 202 DADVLVVYAKTDLTavPASRGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSGL 281
Cdd:cd01156 159 DADTLVVYAKTDPS--AGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 282 DLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHITAKDCAGV 361
Cdd:cd01156 237 DYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 362 ILYTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGRAFNA 421
Cdd:cd01156 317 ILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
43-417 |
0e+00 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 622.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 43 LNEEQKQLRHTISKFVQENLAPKAQEIDQSNDFKNLREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAA 122
Cdd:PLN02519 26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 123 VGLSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNGPD 202
Cdd:PLN02519 106 VGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 203 ADVLVVYAKTDLTAvpASRGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSGLD 282
Cdd:PLN02519 186 AQTLVVYAKTDVAA--GSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 283 LERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHITAKDCAGVI 362
Cdd:PLN02519 264 LERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVI 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 6981112 363 LYTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGR 417
Cdd:PLN02519 344 LCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR 398
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
43-418 |
2.02e-164 |
|
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: 467.01 E-value: 2.02e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 43 LNEEQKQLRHTISKFVQENLAPKAQEIDQSNDFKnlREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAA 122
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFP--RELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 123 VGLSYGAHsNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNGPD 202
Cdd:COG1960 83 LALPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 203 ADVLVVYAKTDLTavPASRGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSGLD 282
Cdd:COG1960 162 ADVILVLARTDPA--AGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 283 LERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHITAKDCAGVI 362
Cdd:COG1960 240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981112 363 LYTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGRA 418
Cdd:COG1960 320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARR 375
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
45-418 |
5.17e-149 |
|
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: 427.84 E-value: 5.17e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 45 EEQKQLRHTISKFVQENLAPKAQEIDQSNDFKnlREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAAVG 124
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFP--REVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 125 LSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNGPDAD 204
Cdd:cd01158 79 VIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 205 VLVVYAKTDLTAvpASRGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSGLDLE 284
Cdd:cd01158 159 FYIVFAVTDPSK--GYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 285 RLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHITAKDCAGVILY 364
Cdd:cd01158 237 RIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLF 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 6981112 365 TAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGRA 418
Cdd:cd01158 317 ASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKH 370
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
45-417 |
4.15e-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: 360.06 E-value: 4.15e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 45 EEQKQLRHTISKFVQENLAPKAQEIDQSNDFknLREFWKQLGSLGVlgitapvqyggsglgylehvlvmeeisrasaavg 124
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEE--PWELLAELGLLLG---------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 125 lsygahsnlcINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNGPDAD 204
Cdd:cd00567 45 ----------AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDAD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 205 VLVVYAKTDlTAVPASRGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSGLDLE 284
Cdd:cd00567 115 LFIVLARTD-EEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 285 RLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHI-TAKDCAGVIL 363
Cdd:cd00567 194 RLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKL 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 6981112 364 YTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGR 417
Cdd:cd00567 274 FATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
45-417 |
9.69e-106 |
|
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: 317.52 E-value: 9.69e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 45 EEQKQLRHTISKFVQENLAPKAQEIDQSNDFKnlREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAaVG 124
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVP--REVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGG-SG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 125 LSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNGPDAD 204
Cdd:cd01160 78 PGLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 205 VLVVYAKTDLTAVPASrGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSGLDLE 284
Cdd:cd01160 158 VVIVVARTGGEARGAG-GISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 285 RLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHITAKDCAGVILY 364
Cdd:cd01160 237 RLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYW 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 6981112 365 TAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGR 417
Cdd:cd01160 317 ATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
6-409 |
5.51e-103 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 311.87 E-value: 5.51e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 6 RLLGRRVSSWRLRPLpSPLAVPQRAHSmlpvddDINGLNEEQKQLRHTISKFVQENLAPKAQEIDQSNDFKnlREFWKQL 85
Cdd:PTZ00461 7 SSLGRRSATCGWTAA-ATMTSASRAFM------DLYNPTPEHAALRETVAKFSREVVDKHAREDDINMHFN--RDLFKQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 86 GSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAAVGLSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAM 165
Cdd:PTZ00461 78 GDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 166 SEPNAGSDVVSMRLKAEKKGD-HYVLNGNKFWITNGPDADVLVVYAKTDltavpasRGITAFIVEKDMPGFSTSKKLDKL 244
Cdd:PTZ00461 158 SEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVFLIYAKVD-------GKITAFVVERGTKGFTQGPKIDKC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 245 GMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQ 324
Cdd:PTZ00461 231 GMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 325 GKMADMYTRLMACRQYVYNVARACDEGHITAKDCAGVILYTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIG 404
Cdd:PTZ00461 311 RYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIG 390
|
....*
gi 6981112 405 GGTSE 409
Cdd:PTZ00461 391 GGTIE 395
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
32-415 |
5.16e-101 |
|
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: 306.70 E-value: 5.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 32 SMLPVDDDIN-GLNEEQKQLRHTISKFVQENLAPKaqEIDQSNDFKnlREFWKQLGSLGVLGITAPVQYGGSGLGYLEHV 110
Cdd:cd01161 15 QVFPYPSVLTeEQTEELNMLVGPVEKFFEEVNDPA--KNDQLEKIP--RKTLTQLKELGLFGLQVPEEYGGLGLNNTQYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 111 LVMEEISRAsAAVGLSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKK--GDHY 188
Cdd:cd01161 91 RLAEIVGMD-LGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 189 VLNGNKFWITNGPDADVLVVYAKTDLTAVPASR--GITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANI 266
Cdd:cd01161 170 VLNGSKIWITNGGIADIFTVFAKTEVKDATGSVkdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 267 LSQESKGVYVLMSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVAR 346
Cdd:cd01161 250 LGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSG 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981112 347 ACDEGHIT--AKDCAGVILYTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVI 415
Cdd:cd01161 330 NMDRGLKAeyQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
43-418 |
3.52e-100 |
|
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: 303.21 E-value: 3.52e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 43 LNEEQKQLRHTISKFVQENLAPKAQEIDQSNDFKnlREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAA 122
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFP--VDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 123 VGlSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNGPD 202
Cdd:cd01162 79 TA-AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 203 ADVLVVYAKTDltaVPASRGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSGLD 282
Cdd:cd01162 158 SDVYVVMARTG---GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 283 LERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHITA-KDCAGV 361
Cdd:cd01162 235 GGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAvKLCAMA 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981112 362 ILYTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGRA 418
Cdd:cd01162 315 KRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARA 371
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
43-417 |
8.61e-86 |
|
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: 266.37 E-value: 8.61e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 43 LNEEQKQLRHTISKFVQENLAPKAQEIDQSNDFKnlREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAA 122
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYP--WPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 123 VGLSYGAHSnLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNGPD 202
Cdd:cd01157 79 VQTAIEANS-LGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 203 ADVLVVYAKTDLT-AVPASRGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSGL 281
Cdd:cd01157 158 ANWYFLLARSDPDpKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 282 DLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHITAKDCAGV 361
Cdd:cd01157 238 DKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981112 362 ILYTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGR 417
Cdd:cd01157 318 KAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISR 373
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
43-419 |
1.91e-85 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 265.76 E-value: 1.91e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 43 LNEEQKQLRHTISKFVQENLAPKAQEIDQSNDFKnlREFWKQLGSLGVLGITaPVQYGGSGLGYLEHVLVMEEISRASAA 122
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFD--RKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDSG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 123 VGLSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNGPD 202
Cdd:cd01151 90 YRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 203 ADVLVVYAKTDLTAvpasrGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSqESKGVYVLMSGLD 282
Cdd:cd01151 170 ADVFVVWARNDETG-----KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLP-GAEGLRGPFKCLN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 283 LERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHIT-------- 354
Cdd:cd01151 244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATpeqisllk 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981112 355 AKDCaGVILYTAECATQValdgiqcLGGNGYINDFPMGRFLRDAK---LYEiggGTSEVRRLVIGRAF 419
Cdd:cd01151 324 RNNC-GKALEIARTAREM-------LGGNGISDEYHIIRHMVNLEsvnTYE---GTHDIHALILGRAI 380
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
43-424 |
1.56e-66 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 216.90 E-value: 1.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 43 LNEEQKQLRHTISKFVQENlAPKA--QEIDQSNDFKnlREFWKQL--GSLGVLGItaPVQYGGSGLGYLEHVLVMEEISR 118
Cdd:PRK12341 5 LTEEQELLLASIRELITRN-FPEEyfRTCDENGTYP--REFMRALadNGISMLGV--PEEFGGTPADYVTQMLVLEEVSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 119 ASAAVglsYGAHSNLCINQIVRNGNEAQKEK-YLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWI 197
Cdd:PRK12341 80 CGAPA---FLITNGQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 198 TNGPDADVLVVYAKTDLTAVPASRgITAFIVEKDMPGFSTsKKLDKLGMRGSNTCELVFEDCKVPAANILSQESKGVYVL 277
Cdd:PRK12341 157 TGAKEYPYMLVLARDPQPKDPKKA-FTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 278 MSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHITAKD 357
Cdd:PRK12341 235 MYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTS 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981112 358 CAGVILYTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGRAFNADFR 424
Cdd:PRK12341 315 AALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDYQ 381
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
43-424 |
1.85e-54 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 185.42 E-value: 1.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 43 LNEEQKQLRHTISKFV-QENLAPKAQEIDQSNDFKnlREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASA 121
Cdd:PRK03354 5 LNDEQELFVAGIRELMaSENWEAYFAECDRDSVYP--ERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 122 AVGLSYGAHSNlcINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNGP 201
Cdd:PRK03354 83 PTYVLYQLPGG--FNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 202 DADVLVVYAKTdlTAVPASRGITAFIVEKDMPGFSTSKkLDKLGMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSGL 281
Cdd:PRK03354 161 YTPYIVVMARD--GASPDKPVYTEWFVDMSKPGIKVTK-LEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 282 DLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHITAKDCAGV 361
Cdd:PRK03354 238 DHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMC 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981112 362 ILYTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGRAFNADFR 424
Cdd:PRK03354 318 KYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
38-417 |
6.32e-51 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 176.97 E-value: 6.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 38 DDIngLNEEQKQLRHTISKFVQENLAPKAQEIDQSNDFKnlREFWKQLGSLGVLGITAPvQYGGSGLGYLEHVLVMEEIS 117
Cdd:PLN02526 26 DDL--LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFP--FHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 118 RASAAVGLSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWI 197
Cdd:PLN02526 101 RVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 198 TNGPDADVLVVYAKTDLTavpasRGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILS-----QESK 272
Cdd:PLN02526 181 GNSTFADVLVIFARNTTT-----NQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPgvnsfQDTN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 273 GVyvlmsgLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGH 352
Cdd:PLN02526 256 KV------LAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGK 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981112 353 ITAKDCAGVILYTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAK---LYEiggGTSEVRRLVIGR 417
Cdd:PLN02526 330 MTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEpiyTYE---GTYDINALVTGR 394
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
44-158 |
3.33e-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: 162.63 E-value: 3.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 44 NEEQKQLRHTISKFVQENLAPKAQEIDQSNDFKnlREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAAV 123
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFP--RELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASV 78
|
90 100 110
....*....|....*....|....*....|....*
gi 6981112 124 GLSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGE 158
Cdd:pfam02771 79 ALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
45-418 |
3.59e-49 |
|
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: 171.38 E-value: 3.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 45 EEQKQLRHTISKFVQENLAP---KAQEIDQSNDFKNLREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASA 121
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPelrEESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 122 AV-GLSYGAHsnLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNG 200
Cdd:cd01152 81 PVpFNQIGID--LAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 201 PDADVLVVYAKTDlTAVPASRGITAFIVEKDMPGFsTSKKLDKLgMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSG 280
Cdd:cd01152 159 HYADWAWLLVRTD-PEAPKHRGISILLVDMDSPGV-TVRPIRSI-NGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 281 LDLERLVLAGGPLGIMQAVLDhtipYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEGHITAKDCAG 360
Cdd:cd01152 236 LNFERVSIGGSAATFFELLLA----RLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASI 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981112 361 VILYTAECATQVALDGIQCLG-----GNGYINDFPMGRFLRD---AKLYEIGGGTSEVRRLVIGRA 418
Cdd:cd01152 312 AKLFGSELAQELAELALELLGtaallRDPAPGAELAGRWEADylrSRATTIYGGTSEIQRNIIAER 377
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
53-417 |
1.05e-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: 167.95 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 53 TISKFVQENLAPKAQEIDQSN-DFKNLR--------EFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAAV 123
Cdd:cd01153 4 EVARLAENVLAPLNADGDREGpVFDDGRvvvpppfkEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 124 GLSYGAHSnlCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGD-HYVLNGNKFWITNG-- 200
Cdd:cd01153 84 MYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGeh 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 201 --PDADVLVVYAKTDlTAVPASRGITAFIVEK-----DMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPaanILSQESKG 273
Cdd:cd01153 162 dmSENIVHLVLARSE-GAPPGVKGLSLFLVPKflddgERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 274 VYVLMSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQF-------------QLMQGKMadmytRLMACRQY 340
Cdd:cd01153 238 LAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAApavtiihhpdvrrSLMTQKA-----YAEGSRAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 341 VYNVARACDEGHITAKD---------CAGVIL-----YTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGG 406
Cdd:cd01153 313 DLYTATVQDLAERKATEgedrkalsaLADLLTpvvkgFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEG 392
|
410
....*....|..
gi 6981112 407 TSEVRRL-VIGR 417
Cdd:cd01153 393 TTGIQALdLIGR 404
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
272-418 |
4.05e-44 |
|
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: 150.87 E-value: 4.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 272 KGVYVLMSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEG 351
Cdd:pfam00441 2 RGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981112 352 HITAKDCAGVILYTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGRA 418
Cdd:pfam00441 82 GPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARR 148
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
138-421 |
1.69e-38 |
|
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: 143.67 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 138 IVRNGNEAQKEKYLPKLISGE---FIGALAMSEPNAGSDVVSMRLKAEK-KGDHYVLNGNKfWITNGPDADVLVVYAKTD 213
Cdd:cd01154 123 LRKYGPEELKQYLPGLLSDRYktgLLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLARPE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 214 lTAVPASRGITAFIVEKDMP-----GFSTSKKLDKLGMRGSNTCELVFEDCKvpaANILSQESKGVYVLMSGLDLERLVL 288
Cdd:cd01154 202 -GAPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDAE---AYLIGDEGKGIYYILEMLNISRLDN 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 289 AGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDE-GHITAKDCAGVIL---- 363
Cdd:cd01154 278 AVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRaAADKPVEAHMARLatpv 357
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981112 364 ---YTAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGRAFNA 421
Cdd:cd01154 358 aklIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVLVK 418
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
162-257 |
1.18e-32 |
|
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: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 162 ALAMSEPNAGSDVVSMRLKA-EKKGDHYVLNGNKFWITNGPDADVLVVYAKTDLTAvpASRGITAFIVEKDMPGFSTSKK 240
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDD--RHGGISLFLVPKDAPGVSVRRI 78
|
90
....*....|....*..
gi 6981112 241 LDKLGMRGSNTCELVFE 257
Cdd:pfam02770 79 ETKLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
10-417 |
2.35e-32 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 129.22 E-value: 2.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 10 RRVSSWRLRPLPSPLAVPQRAHSMLPVDDDINGLNEE----------------QKQLRHTI----SKFVQENLAPKAQEI 69
Cdd:PTZ00456 3 RRVCSSAAASHAAAVSASARSLQYQPRIRDVQFLVEEvfnmydhyeklgktdvTKELMDSLleeaSKLATQTLLPLYESS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 70 D-------QSNDF---KNLREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAAV----GLSYGAhsnlcI 135
Cdd:PTZ00456 83 DsegcvllKDGNVttpKGFKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFsmypGLSIGA-----A 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 136 NQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGD-HYVLNGNKFWITNGpDAD-----VLVVY 209
Cdd:PTZ00456 158 NTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAG-DHDlteniVHIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 210 AKTDlTAVPASRGITAFIVEKDMP----GFSTSKKLD------KLGMRGSNTCELVFEDCKvpaANILSQESKGVYVLMS 279
Cdd:PTZ00456 237 ARLP-NSLPTTKGLSLFLVPRHVVkpdgSLETAKNVKciglekKMGIKGSSTCQLSFENSV---GYLIGEPNAGMKQMFT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 280 GLDLERLVLAGGPLGIMQAVLDHTIPYlhVREAFGQKIGQFQLMQGKMAD-------MYTRLMAC-------RQYVYNVA 345
Cdd:PTZ00456 313 FMNTARVGTALEGVCHAELAFQNALRY--ARERRSMRALSGTKEPEKPADriichanVRQNILFAkavaeggRALLLDVG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 346 RACDEgHITAKDCAG-------VILYT-------AECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVR 411
Cdd:PTZ00456 391 RLLDI-HAAAKDAATrealdheIGFYTpiakgclTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQ 469
|
....*..
gi 6981112 412 RL-VIGR 417
Cdd:PTZ00456 470 ALdFIGR 476
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
48-418 |
1.72e-31 |
|
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: 124.04 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 48 KQLRHTISKFVQENLAPKAQEID---QSND---------FKNLREFWKqlgSLGVLGITAPVQYGGSGLGYLEHVLVMEE 115
Cdd:cd01155 4 QELRARVKAFMEEHVYPAEQEFLeyyAEGGdrwwtpppiIEKLKAKAK---AEGLWNLFLPEVSGLSGLTNLEYAYLAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 116 ISR---ASAAVGLSYGAHSNLCInqIVRNGNEAQKEKYLPKLISGEFIGALAMSEPN-AGSDVVSMRLKAEKKGDHYVLN 191
Cdd:cd01155 81 TGRsffAPEVFNCQAPDTGNMEV--LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 192 GNKFWITNG--PDADVLVVYAKTDLTAVPASRGITAFIVEKDMPGFSTSKKLDKLG---MRGSNtCELVFEDCKVPAANI 266
Cdd:cd01155 159 GRKWWSSGAgdPRCKIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGyddAPHGH-AEITFDNVRVPASNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 267 LSQESKGVYVLMSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVAR 346
Cdd:cd01155 238 ILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAH 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981112 347 ACDEGhiTAKDCAGVILYTAECATQVALD----GIQCLGGNGYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGRA 418
Cdd:cd01155 318 MIDTV--GNKAARKEIAMIKVAAPRMALKiidrAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARM 391
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
101-410 |
6.79e-20 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 92.17 E-value: 6.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 101 GSGLGYLEHVLVMEEISRAS-AAVGLSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPN-AGSDVVSMR 178
Cdd:PLN02876 491 GAGLSNLEYGYLCEIMGRSVwAPQVFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 179 LKAEKKGDHYVLNGNKFWiTNG---PDADVLVVYAKTDLTAvPASRGITAFIVEKDMPGFSTSKKLDKLGMRGS--NTCE 253
Cdd:PLN02876 571 CSIRRQGDSYVINGTKWW-TSGamdPRCRVLIVMGKTDFNA-PKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAphGHAE 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 254 LVFEDCKVPAANILSQESKGVYVLMSGLDLERL----VLAGGPLGIMQAVLDHTIPylhvREAFGQKIGQFQLMQGKMAD 329
Cdd:PLN02876 649 ISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLhhcmRLIGAAERGMQLMVQRALS----RKAFGKLIAQHGSFLSDLAK 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 330 MYTRLMACRQYVYNVARACDE-GHITAKdcaGVILYTAECATQVAL----DGIQCLGGNGYINDFPMGRFLRDAKLYEIG 404
Cdd:PLN02876 725 CRVELEQTRLLVLEAADQLDRlGNKKAR---GIIAMAKVAAPNMALkvldMAMQVHGAAGVSSDTVLAHLWATARTLRIA 801
|
....*.
gi 6981112 405 GGTSEV 410
Cdd:PLN02876 802 DGPDEV 807
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
62-306 |
2.35e-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: 80.06 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 62 LAPKAQEIDQSNDFKnlREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAAVGLSYGAHSNLcINQIVRN 141
Cdd:cd01163 10 IAEGAAERDRQRGLP--YEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGF-VEALLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 142 GNEAQKEKYLPKLISGEFIGAlAMSE---PNAGSDVVSMrlkaEKKGDHYVLNGNKFWITNGPDADVLVVYAKTDLTAvp 218
Cdd:cd01163 87 GPEQFRKRWFGRVLNGWIFGN-AVSErgsVRPGTFLTAT----VRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 219 asrgITAFIVEKDMPGFSTSKKLDKLGMR--GSNTceLVFEDCKVPAANIL---SQESKGVYVLMsgldLERLVLAGGPL 293
Cdd:cd01163 160 ----LVFAAVPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLprpNAPDRGTLLTA----IYQLVLAAVLA 229
|
250
....*....|...
gi 6981112 294 GIMQAVLDHTIPY 306
Cdd:cd01163 230 GIARAALDDAVAY 242
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
80-330 |
2.31e-14 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 74.99 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 80 EFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAAVGLSYgahsnlcinqIVRN-----------GNEAQKE 148
Cdd:PRK13026 112 EVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTV----------MVPNslgpgellthyGTQEQKD 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 149 KYLPKLISGEFIGALAMSEPNAGSDVVSMR-----LKAEKKGDHYV---LNGNKFWITNGPDADVL----VVYAKTDLTA 216
Cdd:PRK13026 182 YWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEVLglrLTWDKRYITLAPVATVLglafKLRDPDGLLG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 217 VPASRGITAFIVEKDMPGFSTSKKLDKLGMR---GSNTCELVFedckVPAANIL---SQESKGVYVLMSGLDLERlvlaG 290
Cdd:PRK13026 262 DKKELGITCALIPTDHPGVEIGRRHNPLGMAfmnGTTRGKDVF----IPLDWIIggpDYAGRGWRMLVECLSAGR----G 333
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6981112 291 GPLGIMQAVLDH-----TIPYLHVREAFGQKIGQFQLMQGKMADM 330
Cdd:PRK13026 334 ISLPALGTASGHmatrtTGAYAYVRRQFGMPIGQFEGVQEALARI 378
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
157-420 |
2.61e-13 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 71.71 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 157 GEFIGaLAMSEPNAGSDVVSMRLKAEK-KGDHYVLNGNKfWITNGPDADVLVVYAKTDltavpasRGITAFIVEKDMP-G 234
Cdd:PRK11561 177 GLLIG-MGMTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAK-------GGLSCFFVPRFLPdG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 235 FSTSKKL----DKLGMRGSNTCELVFEDCkvpAANILSQESKGVYVLMSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVR 310
Cdd:PRK11561 248 QRNAIRLerlkDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQR 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 311 EAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEgHITAKDCAGVILYTAECATQVALDGI-------QCLGGN 383
Cdd:PRK11561 325 QVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDR-RADAKEALWARLFTPAAKFVICKRGIpfvaeamEVLGGI 403
|
250 260 270
....*....|....*....|....*....|....*..
gi 6981112 384 GYINDFPMGRFLRDAKLYEIGGGTSEVRRLVIGRAFN 420
Cdd:PRK11561 404 GYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLN 440
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
89-384 |
3.95e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 71.39 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 89 GVLGITAPVQYGGSGLGYLEHVLVMEEISRASAAVGLSYGahsnlcinqiVRN-----------GNEAQKEKYLPKLISG 157
Cdd:PRK09463 122 GFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVM----------VPNslgpgelllhyGTDEQKDHYLPRLARG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 158 EFIGALAMSEPNAGSDVVSMR-----LKAEKKGDHYV---LNGNKFWITNGPDADVL-----------VVYAKTDLtavp 218
Cdd:PRK09463 192 EEIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLgmrLTWNKRYITLAPIATVLglafklydpdgLLGDKEDL---- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 219 asrGITAFIVEKDMPGFSTSKKLDKLG---MRGSNTCELVFedckVPAANIL---SQESKGVYVLMSGLDLERLV-LAGG 291
Cdd:PRK09463 268 ---GITCALIPTDTPGVEIGRRHFPLNvpfQNGPTRGKDVF----IPLDYIIggpKMAGQGWRMLMECLSVGRGIsLPSN 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 292 PLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADM--YTRLM-ACRQYvynVARACDEGH----ITAkdcagvIL- 363
Cdd:PRK09463 341 STGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIagNAYLMdAARTL---TTAAVDLGEkpsvLSA------IAk 411
|
330 340
....*....|....*....|..
gi 6981112 364 -YTAECATQVALDGIQCLGGNG 384
Cdd:PRK09463 412 yHLTERGRQVINDAMDIHGGKG 433
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
124-327 |
1.09e-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: 66.58 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 124 GLSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKA--EKKGDHYVLN-----GNKFW 196
Cdd:cd01150 99 GAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWW 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 197 ITN-GPDADVLVVYAKtdLTAVPASRGITAFIVE-------KDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILS 268
Cdd:cd01150 179 PGNlGKTATHAVVFAQ--LITPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 269 QESK----GVYV------------LMSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQ-------FQLMQG 325
Cdd:cd01150 257 RFGDvspdGTYVspfkdpnkrygaMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKPSDpevqildYQLQQY 336
|
..
gi 6981112 326 KM 327
Cdd:cd01150 337 RL 338
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
76-300 |
2.53e-11 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 65.29 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 76 KNLREFWKQLGSLGvlGITAPVQYGGSGLGYLEHVLVMEEISRASAAVGLSYGAHSNLCINQIVRNGNEAQKEKYLPKLI 155
Cdd:PTZ00457 53 EQIRSNDKILGNLY--GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 156 SGEFIGALAMSEPNaGSDVVSMRLKAEKKGD-HYVLNGNKFWItNGPDADVLVVYAKTdLTAVPASRGITA------FIV 228
Cdd:PTZ00457 131 DGTIMMGWATEEGC-GSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKT-LTQTAAEEGATEvsrnsfFIC 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981112 229 EKDMPGFSTskkldklgmrgsNTCELVFEDckVPAANILSQESKGVYVLMSGLDLERLVLAGGPLGIMQAVL 300
Cdd:PTZ00457 208 AKDAKGVSV------------NGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVV 265
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
112-330 |
8.34e-08 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 54.48 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 112 VMEEISRASAAVGLSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKA--EKKGDHYV 189
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 190 LN-----GNKFWITNGP-DADVLVVYAKTDLTAvPASRGIT-----AFIVE-KDM------PGFSTSKKLDKLGMRGSNT 251
Cdd:PLN02636 206 INtpndgAIKWWIGNAAvHGKFATVFARLKLPT-HDSKGVSdmgvhAFIVPiRDMkthqvlPGVEIRDCGHKVGLNGVDN 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 252 CELVFEDCKVPAANILSQ----ESKGVYV----------------LMSGldleRLVLAGGPLGIMQAVLDHTIPYLHVRE 311
Cdd:PLN02636 285 GALRFRSVRIPRDNLLNRfgdvSRDGKYTsslptinkrfaatlgeLVGG----RVGLAYGSVGVLKASNTIAIRYSLLRQ 360
|
250 260
....*....|....*....|....*
gi 6981112 312 AFGQ------KIGQFQLMQGKMADM 330
Cdd:PLN02636 361 QFGPpkqpeiSILDYQSQQHKLMPM 385
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
60-398 |
3.75e-06 |
|
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: 48.50 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 60 ENLAPKAQEidQSNDFKNLREFWKQ----LGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAAVG---LSYGAHSN 132
Cdd:cd01159 4 EDLAPLIRE--RAPEAERARRLPDEvvraLREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAwvaSIVATHSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 133 lcinQIVRNGNEAQKEKYlpklisGEFIGALAmsepnagSDVVSMRLKAEKKGDHYVLNGNKFWITNGPDADVLVVYAK- 211
Cdd:cd01159 82 ----MLAAFPPEAQEEVW------GDGPDTLL-------AGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 212 TDLTAVPASRgitAFIVEKDmpGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSqeSKGVYVL---MSGLDLER--- 285
Cdd:cd01159 145 EDDDGGPLPR---AFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLT--AGDMMAGdgpGGSTPVYRmpl 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 286 -----LVLAGGPLGIMQAVLDHTIPYLHVR---EAFGQKIGQFQLMQGKMADMYTRLMACRQYVYNVARACDEgHITAKD 357
Cdd:cd01159 218 rqvfpLSFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWA-HALAGG 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 6981112 358 CAGVILyTAECATQVALDGIQCL----------GGNGYINDFPMGRFLRDA 398
Cdd:cd01159 297 PIDVEE-RARIRRDAAYAAKLSAeavdrlfhaaGGSALYTASPLQRIWRDI 346
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
142-269 |
2.77e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 46.38 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 142 GNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKA--EKKGDHYVLN-----GNKFWITN-GPDADVLVVYAKtd 213
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAK-- 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981112 214 LTAVPASRGITAFIVE-------KDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSQ 269
Cdd:PTZ00460 188 LIVNGKNKGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAR 250
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
130-276 |
1.43e-03 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 40.98 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 130 HSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKA--EKKGDHYVLN-----GNKFWITN-GP 201
Cdd:PLN02443 102 HWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTAtfDPKTDEFVIHsptltSSKWWPGGlGK 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981112 202 DADVLVVYAKtdLTAVPASRGITAFIVE-------KDMPGFSTSKKLDKLGMRGSNTCE---LVFEDCKVPAANILSQES 271
Cdd:PLN02443 182 VSTHAVVYAR--LITNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLS 259
|
....*....
gi 6981112 272 K----GVYV 276
Cdd:PLN02443 260 KvtreGKYV 268
|
|
| |
