|
Name |
Accession |
Description |
Interval |
E-value |
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
17-390 |
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: 713.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 17 LRPPLAGFVSQRahsLLPVDDAINGLSEEQRqEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSY 96
Cdd:cd01156 9 LRQSVREFAQKE---IAPLAAKIDRDNEFPR-DLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 97 GAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLI 176
Cdd:cd01156 85 GAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDADTLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 177 VYAKTDLAavPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLV 256
Cdd:cd01156 165 VYAKTDPS--AGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERLV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 257 LAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAE 336
Cdd:cd01156 243 LAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAAE 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1444691830 337 CATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNA 390
Cdd:cd01156 323 KATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
51-386 |
0e+00 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 586.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 51 WKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIG 130
Cdd:PLN02519 65 WKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 131 ALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvpASRGITAFIVEKGMPGFSTSKKL 210
Cdd:PLN02519 145 ALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAA--GSKGITAFIIEKGMPGFSTAQKL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 211 DKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQ 290
Cdd:PLN02519 223 DKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQ 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 291 LMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLY 370
Cdd:PLN02519 303 FIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLY 382
|
330
....*....|....*.
gi 1444691830 371 EIGAGTSEVRRLVIGR 386
Cdd:PLN02519 383 EIGAGTSEIRRMLIGR 398
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
49-387 |
8.08e-150 |
|
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: 428.87 E-value: 8.08e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 49 EFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHsNLCINQLVRNGNEAQKEKYLPKLISGEY 128
Cdd:COG1960 40 ELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLALPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEW 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 129 IGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAavPASRGITAFIVEKGMPGFSTSK 208
Cdd:COG1960 119 IGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADVILVLARTDPA--AGHRGISLFLVPKDTPGVTVGR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 209 KLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGH 288
Cdd:COG1960 197 IEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIAD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 289 FQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAK 368
Cdd:COG1960 277 FQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDAR 356
|
330
....*....|....*....
gi 1444691830 369 LYEIGAGTSEVRRLVIGRA 387
Cdd:COG1960 357 ILTIYEGTNEIQRLIIARR 375
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
48-387 |
5.44e-137 |
|
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: 395.87 E-value: 5.44e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 48 QEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGE 127
Cdd:cd01158 33 REVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 128 YIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvpASRGITAFIVEKGMPGFSTS 207
Cdd:cd01158 113 KIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFYIVFAVTDPSK--GYRGITAFIVERDTPGLSVG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 208 KKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIG 287
Cdd:cd01158 191 KKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 288 HFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDA 367
Cdd:cd01158 271 DFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDA 350
|
330 340
....*....|....*....|
gi 1444691830 368 KLYEIGAGTSEVRRLVIGRA 387
Cdd:cd01158 351 KITEIYEGTSEIQRLVIAKH 370
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
102-386 |
1.50e-118 |
|
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: 347.35 E-value: 1.50e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 102 LCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKT 181
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLART 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 182 DLAAvPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGP 261
Cdd:cd00567 123 DEEG-PGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 262 LGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHC-TAKDCAGVILYSAECATQ 340
Cdd:cd00567 202 LGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKLFATEAARE 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1444691830 341 VALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGR 386
Cdd:cd00567 282 VADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
48-386 |
1.77e-98 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 297.87 E-value: 1.77e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 48 QEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRAsGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGE 127
Cdd:cd01160 33 REVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARA-GGSGPGLSLHTDIVSPYITRAGSPEQKERVLPQMVAGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 128 YIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASrGITAFIVEKGMPGFSTS 207
Cdd:cd01160 112 KIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGGEARGAG-GISLFLVERGTPGFSRG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 208 KKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIG 287
Cdd:cd01160 191 RKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 288 HFQLMQGKMADMYTRLMACRQYVYNVAKACDEGH------CTAKDCAGvilysaECATQVALDGIQCFGGNGYINDFPMG 361
Cdd:cd01160 271 QLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRldvaeaSMAKYWAT------ELQNRVAYECVQLHGGWGYMREYPIA 344
|
330 340
....*....|....*....|....*
gi 1444691830 362 RFLRDAKLYEIGAGTSEVRRLVIGR 386
Cdd:cd01160 345 RAYRDARVQPIYGGTTEIMKELISR 369
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
35-384 |
3.48e-96 |
|
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: 293.22 E-value: 3.48e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 35 VDDAINGLSEEQRQEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGaVGLSYGAHSNLCINQLVRNGNEA 114
Cdd:cd01161 46 NDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLG-FSVTLGAHQSIGFKGILLFGTEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 115 QKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKK--GNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASR-- 190
Cdd:cd01161 125 QKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVkd 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 191 GITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLD 270
Cdd:cd01161 205 KITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 271 HTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCT--AKDCAGVILYSAECATQVALDGIQC 348
Cdd:cd01161 285 KAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAeyQIEAAISKVFASEAAWLVVDEAIQI 364
|
330 340 350
....*....|....*....|....*....|....*.
gi 1444691830 349 FGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVI 384
Cdd:cd01161 365 HGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
17-378 |
1.13e-95 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 291.84 E-value: 1.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 17 LRPPLAGFVSQRAHSLLPVDDaINGlseEQRQEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSY 96
Cdd:PTZ00461 44 LRETVAKFSREVVDKHAREDD-INM---HFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 97 GAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGN-HYILNGNKFWITNGPDADVL 175
Cdd:PTZ00461 120 LAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 176 IVYAKTDlaavpasRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERL 255
Cdd:PTZ00461 200 LIYAKVD-------GKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 256 VLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSA 335
Cdd:PTZ00461 273 TLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFAT 352
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1444691830 336 ECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSE 378
Cdd:PTZ00461 353 PIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
52-387 |
4.87e-91 |
|
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: 278.94 E-value: 4.87e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 52 KQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGlSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGA 131
Cdd:cd01162 39 RKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA-AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLAS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 132 LAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDlaaVPASRGITAFIVEKGMPGFSTSKKLD 211
Cdd:cd01162 118 YCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVVMARTG---GEGPKGISCFVVEKGTPGLSFGANEK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 212 KLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQL 291
Cdd:cd01162 195 KMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 292 MQGKMADMYTRLMACRQYVYNVAKACDEGHCTA-KDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLY 370
Cdd:cd01162 275 LQFKLADMATELVASRLMVRRAASALDRGDPDAvKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVH 354
|
330
....*....|....*..
gi 1444691830 371 EIGAGTSEVRRLVIGRA 387
Cdd:cd01162 355 QILEGTNEIMRLIIARA 371
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
52-386 |
6.93e-77 |
|
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: 242.49 E-value: 6.93e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 52 KQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEIsrASGAVGLSYGAHSN-LCINQLVRNGNEAQKEKYLPKLISGEYIG 130
Cdd:cd01157 39 KRAWELGLMNTHIPEDCGGLGLGTFDTCLITEEL--AYGCTGVQTAIEANsLGQMPVIISGNDEQKKKYLGRMTEEPLMC 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 131 ALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDL-AAVPASRGITAFIVEKGMPGFSTSKK 209
Cdd:cd01157 117 AYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPdPKCPASKAFTGFIVEADTPGIQPGRK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 210 LDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHF 289
Cdd:cd01157 197 ELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEH 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 290 QLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKL 369
Cdd:cd01157 277 QAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKI 356
|
330
....*....|....*..
gi 1444691830 370 YEIGAGTSEVRRLVIGR 386
Cdd:cd01157 357 YQIYEGTSQIQRLIISR 373
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
52-388 |
3.18e-75 |
|
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: 238.41 E-value: 3.18e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 52 KQLGNLGVLGITaPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGA 131
Cdd:cd01151 51 EEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGC 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 132 LAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvpasrGITAFIVEKGMPGFSTSKKLD 211
Cdd:cd01151 130 FGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADVFVVWARNDETG-----KIRGFILERGMKGLSAPKIQG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 212 KLGMRGSNTCELIFEDCKIPAANILGHENkGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQL 291
Cdd:cd01151 205 KFSLRASITGEIVMDNVFVPEENLLPGAE-GLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 292 MQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAK--- 368
Cdd:cd01151 284 VQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLEsvn 363
|
330 340
....*....|....*....|
gi 1444691830 369 LYEigaGTSEVRRLVIGRAF 388
Cdd:cd01151 364 TYE---GTHDIHALILGRAI 380
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
48-387 |
8.41e-66 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 213.82 E-value: 8.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 48 QEFWKQLGN--LGVLGItaPVQYGGSGLGYLEHVLVMEEISRASGAVglsYGAHSNLCINQLVRNGNEAQKEK-YLPKLI 124
Cdd:PRK12341 40 REFMRALADngISMLGV--PEEFGGTPADYVTQMLVLEEVSKCGAPA---FLITNGQCIHSMRRFGSAEQLRKtAESTLE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 125 SGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASRgITAFIVEKGMPGF 204
Cdd:PRK12341 115 TGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLARDPQPKDPKKA-FTLWWVDSSKPGI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 205 STsKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQ 284
Cdd:PRK12341 194 KI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 285 KIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFL 364
Cdd:PRK12341 273 PIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFW 352
|
330 340
....*....|....*....|...
gi 1444691830 365 RDAKLYEIGAGTSEVRRLVIGRA 387
Cdd:PRK12341 353 RDVRCERIGGGTDEIMIYIAGRQ 375
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
48-387 |
7.65e-51 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 175.02 E-value: 7.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 48 QEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNlcINQLVRNGNEAQKEKYLPKLISGE 127
Cdd:PRK03354 40 ERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVLYQLPGG--FNTFLREGTQEQIDKIMAFRGTGK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 128 YIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTdlAAVPASRGITAFIVEKGMPGFSTS 207
Cdd:PRK03354 118 QMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARD--GASPDKPVYTEWFVDMSKPGIKVT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 208 KkLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIG 287
Cdd:PRK03354 196 K-LEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 288 HFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDA 367
Cdd:PRK03354 275 RFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDL 354
|
330 340
....*....|....*....|
gi 1444691830 368 KLYEIGAGTSEVRRLVIGRA 387
Cdd:PRK03354 355 RVDRVSGGSDEMQILTLGRA 374
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
58-386 |
2.64e-46 |
|
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: 163.71 E-value: 2.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 58 GVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSnlCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEP 137
Cdd:cd01153 49 GWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 138 NAGSDVVSMKLKAEKKGN-HYILNGNKFWITNG----PDADVLIVYAKTDlAAVPASRGITAFIVEK----GMPGFSTSK 208
Cdd:cd01153 127 DAGSDLGALRTKAVYQADgSWRINGVKRFISAGehdmSENIVHLVLARSE-GAPPGVKGLSLFLVPKflddGERNGVTVA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 209 KLD-KLGMRGSNTCELIFEDCKipaANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQ--- 284
Cdd:cd01153 206 RIEeKMGLHGSPTCELVFDNAK---GELIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDlik 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 285 -----KIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGH---------CTAKDCAGVIL-----YSAECATQVALDG 345
Cdd:cd01153 283 aapavTIIHHPDVRRSLMTQKAYAEGSRALDLYTATVQDLAErkategedrKALSALADLLTpvvkgFGSEAALEAVSDA 362
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1444691830 346 IQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRL-VIGR 386
Cdd:cd01153 363 IQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALdLIGR 404
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
44-387 |
1.83e-45 |
|
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: 160.59 E-value: 1.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 44 EEQRQEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRAsGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKL 123
Cdd:cd01152 34 REDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAA-GAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 124 ISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLaAVPASRGITAFIVEKGMPG 203
Cdd:cd01152 113 LSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDP-EAPKHRGISILLVDMDSPG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 204 FsTSKKLDKLgMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDhtipYLHVREAFG 283
Cdd:cd01152 192 V-TVRPIRSI-NGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLLA----RLLLLTRDG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 284 QKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFG-----GNGYINDF 358
Cdd:cd01152 266 RPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGtaallRDPAPGAE 345
|
330 340 350
....*....|....*....|....*....|..
gi 1444691830 359 PMGRFLRD---AKLYEIGAGTSEVRRLVIGRA 387
Cdd:cd01152 346 LAGRWEADylrSRATTIYGGTSEIQRNIIAER 377
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
53-386 |
4.20e-44 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 157.71 E-value: 4.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 53 QLGNLGVLGITAPvQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGAL 132
Cdd:PLN02526 68 KLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACW 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 133 AMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTdlaavPASRGITAFIVEKGMPGFSTSKKLDK 212
Cdd:PLN02526 147 ALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFARN-----TTTNQINGFIVKKGAPGLKATKIENK 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 213 LGMRGSNTCELIFEDC------KIPAANILGHENKgvyvlmsGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKI 286
Cdd:PLN02526 222 IGLRMVQNGDIVLKDVfvpdedRLPGVNSFQDTNK-------VLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 287 GHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRD 366
Cdd:PLN02526 295 AAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCD 374
|
330 340
....*....|....*....|
gi 1444691830 367 AKLYEIGAGTSEVRRLVIGR 386
Cdd:PLN02526 375 LEPIYTYEGTYDINALVTGR 394
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
240-387 |
1.18e-42 |
|
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: 146.25 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 240 NKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDE 319
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444691830 320 GHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRA 387
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARR 148
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
107-390 |
1.59e-36 |
|
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: 137.50 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 107 LVRNGNEAQKEkYLPKLISGEY----IGALAMSEPNAGSDVVSMKLKAEK-KGNHYILNGNKfWITNGPDADVLIVYAKT 181
Cdd:cd01154 123 LRKYGPEELKQ-YLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLARP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 182 DlAAVPASRGITAFIVEKGMP-----GFSTSKKLDKLGMRGSNTCELIFEDCKipaANILGHENKGVYVLMSGLDLERLV 256
Cdd:cd01154 201 E-GAPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDAE---AYLIGDEGKGIYYILEMLNISRLD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 257 LAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDE-GHCTAKDCAGVIL--- 332
Cdd:cd01154 277 NAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRaAADKPVEAHMARLatp 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444691830 333 ----YSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNA 390
Cdd:cd01154 357 vaklIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVLVK 418
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
48-127 |
1.11e-35 |
|
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: 126.42 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 48 QEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGE 127
Cdd:pfam02771 34 RELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
131-226 |
1.31e-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: 117.77 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 131 ALAMSEPNAGSDVVSMKLKA-EKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAvpASRGITAFIVEKGMPGFSTSKK 209
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDD--RHGGISLFLVPKDAPGVSVRRI 78
|
90
....*....|....*..
gi 1444691830 210 LDKLGMRGSNTCELIFE 226
Cdd:pfam02770 79 ETKLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
48-386 |
1.35e-32 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 129.22 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 48 QEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAV----GLSYGAhsnlcINQLVRNGNEAQKEKYLPKL 123
Cdd:PTZ00456 102 KEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFsmypGLSIGA-----ANTLMAWGSEEQKEQYLTKL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 124 ISGEYIGALAMSEPNAGSDVVSMKLKAEKKGN-HYILNGNKFWITNGpDAD-----VLIVYAKTDlAAVPASRGITAFIV 197
Cdd:PTZ00456 177 VSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAG-DHDlteniVHIVLARLP-NSLPTTKGLSLFLV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 198 EKGMP----GFSTSKKLD------KLGMRGSNTCELIFEDCKipaANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQA 267
Cdd:PTZ00456 255 PRHVVkpdgSLETAKNVKciglekKMGIKGSSTCQLSFENSV---GYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAEL 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 268 VLDHTIPYlhVREAFGQKighfQLMQGKMADMYTRLMAC----RQYVYnVAKACDEG--------------HCTAKDCAG 329
Cdd:PTZ00456 332 AFQNALRY--ARERRSMR----ALSGTKEPEKPADRIIChanvRQNIL-FAKAVAEGgrallldvgrlldiHAAAKDAAT 404
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444691830 330 -------VILYS-------AECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRL-VIGR 386
Cdd:PTZ00456 405 realdheIGFYTpiakgclTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGR 476
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
65-387 |
1.46e-29 |
|
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: 117.88 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 65 PVQYGGSGLGYLEHVLVMEEISR---ASGAVGLSYGAHSNLCInqLVRNGNEAQKEKYLPKLISGEYIGALAMSEPN-AG 140
Cdd:cd01155 61 PEVSGLSGLTNLEYAYLAEETGRsffAPEVFNCQAPDTGNMEV--LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvAS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 141 SDVVSMKLKAEKKGNHYILNGNKFWITNG--PDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKLDKLG---M 215
Cdd:cd01155 139 SDATNIECSIERDGDDYVINGRKWWSSGAgdPRCKIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGyddA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 216 RGSNtCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGK 295
Cdd:cd01155 219 PHGH-AEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHW 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 296 MADMYTRLMACRQYVYNVAKACDEGhcTAKDCAGVILYSAECATQVALD----GIQCFGGNGYINDFPMGRFLRDAKLYE 371
Cdd:cd01155 298 IAKSRIEIEQARLLVLKAAHMIDTV--GNKAARKEIAMIKVAAPRMALKiidrAIQVHGAAGVSQDTPLANMYAWARTLR 375
|
330
....*....|....*.
gi 1444691830 372 IGAGTSEVRRLVIGRA 387
Cdd:cd01155 376 IADGPDEVHLRSIARM 391
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
70-386 |
8.23e-18 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 85.62 E-value: 8.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 70 GSGLGYLEHVLVMEEISRASGAVG-LSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPN-AGSDVVSMK 147
Cdd:PLN02876 491 GAGLSNLEYGYLCEIMGRSVWAPQvFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 148 LKAEKKGNHYILNGNKFWiTNG---PDADVLIVYAKTDLAAvPASRGITAFIVEKGMPGFSTSKKLDKLGMRGS--NTCE 222
Cdd:PLN02876 571 CSIRRQGDSYVINGTKWW-TSGamdPRCRVLIVMGKTDFNA-PKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAphGHAE 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 223 LIFEDCKIPAANILGHENKGVYVLMSGLDLERL----VLAGGPLGLMQAVLDHTIPylhvREAFGQKIGHFQLMQGKMAD 298
Cdd:PLN02876 649 ISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLhhcmRLIGAAERGMQLMVQRALS----RKAFGKLIAQHGSFLSDLAK 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 299 MYTRLMACRQYVYNVAKACDE-GHCTAKdcaGVILYSAECATQVAL----DGIQCFGGNGYINDFPMGRFLRDAKLYEIG 373
Cdd:PLN02876 725 CRVELEQTRLLVLEAADQLDRlGNKKAR---GIIAMAKVAAPNMALkvldMAMQVHGAAGVSSDTVLAHLWATARTLRIA 801
|
330
....*....|...
gi 1444691830 374 AGTSEVRRLVIGR 386
Cdd:PLN02876 802 DGPDEVHLGTIAK 814
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
48-299 |
1.16e-14 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 75.76 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 48 QEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRN-GNEAQKEKYLPKLISG 126
Cdd:PRK13026 111 PEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLGPGELLTHyGTQEQKDYWLPRLADG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 127 EYIGALAMSEPNAGSDVVSMK-----LKAEKKGNHYI---LNGNKFWITNGPDADVL----IVYAKTDLAAVPASRGITA 194
Cdd:PRK13026 191 TEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEVLglrLTWDKRYITLAPVATVLglafKLRDPDGLLGDKKELGITC 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 195 FIVEKGMPGFSTSKKLDKLGMR---GSNTCELIFedckIPAANILG---HENKGVYVLMSGLDLERlvlaGGPLGLMQAV 268
Cdd:PRK13026 271 ALIPTDHPGVEIGRRHNPLGMAfmnGTTRGKDVF----IPLDWIIGgpdYAGRGWRMLVECLSAGR----GISLPALGTA 342
|
250 260 270
....*....|....*....|....*....|....*.
gi 1444691830 269 LDH-----TIPYLHVREAFGQKIGHFQLMQGKMADM 299
Cdd:PRK13026 343 SGHmatrtTGAYAYVRRQFGMPIGQFEGVQEALARI 378
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
27-275 |
2.76e-14 |
|
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: 73.51 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 27 QRAHSLLPV-------DDAINGLSEEQRQEfwkqLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAH 99
Cdd:cd01163 1 ARARPLAARiaegaaeRDRQRGLPYEEVAL----LRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 100 SNLcINQLVRNGNEAQKEKYLPKLISGEYIGAlAMSE---PNAGSDVVSMklkaEKKGNHYILNGNKFWITNGPDADVLI 176
Cdd:cd01163 77 FGF-VEALLLAGPEQFRKRWFGRVLNGWIFGN-AVSErgsVRPGTFLTAT----VRDGGGYVLNGKKFYSTGALFSDWVT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 177 VYAKTDLAAvpasrgITAFIVEKGMPGFSTSKKLDKLGMR--GSNTceLIFEDCKIPAANILGHENKGVYVLMSGLdLER 254
Cdd:cd01163 151 VSALDEEGK------LVFAAVPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQ 221
|
250 260
....*....|....*....|.
gi 1444691830 255 LVLAGGPLGLMQAVLDHTIPY 275
Cdd:cd01163 222 LVLAAVLAGIARAALDDAVAY 242
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
49-353 |
4.63e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 70.62 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 49 EFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQ-LVRNGNEAQKEKYLPKLISGE 127
Cdd:PRK09463 113 EVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLGPGElLLHYGTDEQKDHYLPRLARGE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 128 YIGALAMSEPNAGSDVVSMK-----LKAEKKGNHYI---LNGNKFWITNGPDADVL-----------IVYAKTDLaavpa 188
Cdd:PRK09463 193 EIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLgmrLTWNKRYITLAPIATVLglafklydpdgLLGDKEDL----- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 189 srGITAFIVEKGMPGFSTSKKLDKLG---MRGSNTCELIFedckIPAANILG---HENKGVYVLMSGLDLERLV-LAGGP 261
Cdd:PRK09463 268 --GITCALIPTDTPGVEIGRRHFPLNvpfQNGPTRGKDVF----IPLDYIIGgpkMAGQGWRMLMECLSVGRGIsLPSNS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 262 LGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADM--YTRLM-ACRQYvynVAKACDEGHCTAKDCAGVILYSAECA 338
Cdd:PRK09463 342 TGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIagNAYLMdAARTL---TTAAVDLGEKPSVLSAIAKYHLTERG 418
|
330
....*....|....*
gi 1444691830 339 TQVALDGIQCFGGNG 353
Cdd:PRK09463 419 RQVINDAMDIHGGKG 433
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
126-389 |
1.24e-11 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 65.93 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 126 GEYIGaLAMSEPNAGSDVVSMKLKAEK-KGNHYILNGNKfWITNGPDADVLIVYAKTDlaavpasRGITAFIVEKGMP-G 203
Cdd:PRK11561 177 GLLIG-MGMTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAK-------GGLSCFFVPRFLPdG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 204 FSTSKKL----DKLGMRGSNTCELIFEDCkipAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVR 279
Cdd:PRK11561 248 QRNAIRLerlkDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQR 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 280 EAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEgHCTAKDCAGVILYSAECATQVALDGI-------QCFGGN 352
Cdd:PRK11561 325 QVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDR-RADAKEALWARLFTPAAKFVICKRGIpfvaeamEVLGGI 403
|
250 260 270
....*....|....*....|....*....|....*..
gi 1444691830 353 GYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFN 389
Cdd:PRK11561 404 GYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLN 440
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
45-269 |
6.01e-11 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 63.75 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 45 EQRQEFWKQLGNLGvlGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLI 124
Cdd:PTZ00457 53 EQIRSNDKILGNLY--GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 125 SGEYIGALAMSEPNaGSDVVSMKLKAEKKGN-HYILNGNKFWItNGPDADVLIVYAKT------DLAAVPASRgITAFIV 197
Cdd:PTZ00457 131 DGTIMMGWATEEGC-GSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKTltqtaaEEGATEVSR-NSFFIC 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444691830 198 EKGMPGFSTskkldklgmrgsNTCELIFEDckIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVL 269
Cdd:PTZ00457 208 AKDAKGVSV------------NGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVV 265
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
82-249 |
7.83e-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: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 82 MEEISRASGAVGLSYGA----HSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGN 155
Cdd:cd01150 84 MLALTNSLGGYDLSLGAklglHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 156 HYILN-----GNKFWITN-GPDADVLIVYAKTdlaAVPASR-GITAFIVE-------KGMPGFSTSKKLDKLGMRGSNTC 221
Cdd:cd01150 164 EFVINtpdftATKWWPGNlGKTATHAVVFAQL---ITPGKNhGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNG 240
|
170 180
....*....|....*....|....*...
gi 1444691830 222 ELIFEDCKIPAANILgheNKGVYVLMSG 249
Cdd:cd01150 241 FLQFRNVRIPRENLL---NRFGDVSPDG 265
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
24-299 |
2.27e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 52.94 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 24 FVSQRAHSLLPVDDAinglSEEQRQEFWKQLGNLGVLGITAPVQYggsglgylehvlVMEE------ISRASGAV----G 93
Cdd:PLN02636 75 FFNSRPDLQTPVEIS----KDEHRELCMRQLTGLVREAGIRPMKY------------LVEDpakyfaITEAVGSVdmslG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 94 LSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGNHYILN-----GNKFWI 166
Cdd:PLN02636 139 IKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFVINtpndgAIKWWI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 167 TNGP-DADVLIVYAKTDLAAvPASRGIT-----AFIV-------EKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAA 233
Cdd:PLN02636 219 GNAAvHGKFATVFARLKLPT-HDSKGVSdmgvhAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRD 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 234 NILGH----------------ENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQ------KIGHFQL 291
Cdd:PLN02636 298 NLLNRfgdvsrdgkytsslptINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPpkqpeiSILDYQS 377
|
....*...
gi 1444691830 292 MQGKMADM 299
Cdd:PLN02636 378 QQHKLMPM 385
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
111-236 |
1.40e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 47.15 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 111 GNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA--EKKGNHYILN-----GNKFWITN-GPDADVLIVYAKtd 182
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAK-- 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444691830 183 LAAVPASRGITAFIVE-------KGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANIL 236
Cdd:PTZ00460 188 LIVNGKNKGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLL 248
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
27-236 |
4.30e-03 |
|
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: 38.87 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 27 QRAHSLLPVDDAINGLSEEQR---QEFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVG---LSYGAHS 100
Cdd:cd01159 1 ARAEDLAPLIRERAPEAERARrlpDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAwvaSIVATHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444691830 101 nlciNQLVRNGNEAQKEKYlpklisGEYIGALAmsepnagSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAK 180
Cdd:cd01159 81 ----RMLAAFPPEAQEEVW------GDGPDTLL-------AGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAI 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1444691830 181 -TDLAAVPASRgitAFIVEKGmpGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANIL 236
Cdd:cd01159 144 vEDDDGGPLPR---AFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTL 195
|
|
| |
