|
Name |
Accession |
Description |
Interval |
E-value |
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
59-430 |
0e+00 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 612.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 59 DEEIMMKQTVKKFAQEHVAPLVSSMDENSKMEKSVIQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDASVALL 138
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 139 CDIQNTIINNLFRKHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRADKSGNYYVLNGSKMWISHAEHAELF 217
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 218 LVFANVDPSSGYRGITCFLVDRDTEGFQIGKRENKMGIRASSTCQLTFENVKVPETNILGKIGHGYKYAIGSLNEGRIGI 297
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 298 AAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLVEAGRPFIKEASMAKYYASEV 377
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17647119 378 AGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQLNTIAKHIDA 430
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
56-428 |
3.81e-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: 466.62 E-value: 3.81e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 56 TLTDEEIMMKQTVKKFAQEHVAPLVSSMDENSKMEKSVIQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDASV 135
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 136 ALLCDIQNTIINNLFRkHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRADKSGNYYVLNGSKMWISHAEHA 214
Cdd:COG1960 84 ALPVGVHNGAAEALLR-FGTEEQKERYLPRLASgEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 215 ELFLVFANVDPSSGYRGITCFLVDRDTEGFQIGKRENKMGIRASSTCQLTFENVKVPETNILGKIGHGYKYAIGSLNEGR 294
Cdd:COG1960 163 DVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 295 IGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLVEAGRPFIKEASMAKYYA 374
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFA 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 17647119 375 SEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:COG1960 323 TEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRL 376
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
57-430 |
4.44e-123 |
|
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: 362.11 E-value: 4.44e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 57 LTDEEIMMKQTVKKFAQEHVAPLVSSMDENSKMEKSVIQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDASVA 136
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 137 L-------LCdiqntiINNLFRkHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRADKSGNYYVLNGSKMWI 208
Cdd:cd01156 82 LsygahsnLC------INQIYR-NGSAAQKEKYLPKLISgEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 209 SHAEHAELFLVFANVDPSSGYRGITCFLVDRDTEGFQIGKRENKMGIRASSTCQLTFENVKVPETNILGKIGHGYKYAIG 288
Cdd:cd01156 155 TNGPDADTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 289 SLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLVEAGRPFIKEAS 368
Cdd:cd01156 235 GLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAA 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17647119 369 MAKYYASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQLNTIAKHIDA 430
Cdd:cd01156 315 GVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
148-426 |
4.50e-115 |
|
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: 340.03 E-value: 4.50e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 148 NLFRKHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRADKSGNYYVLNGSKMWISHAEHAELFLVFANVDPS 226
Cdd:cd00567 46 ALLLAYGTEEQKERYLPPLASgEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 227 -SGYRGITCFLVDRDTEGFQIGKRENKMGIRASSTCQLTFENVKVPETNILGKIGHGYKYAIGSLNEGRIGIAAQMLGLA 305
Cdd:cd00567 126 gPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVALGAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 306 QGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLVEAGRPFI-KEASMAKYYASEVAGLTTSK 384
Cdd:cd00567 206 RAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEArLEAAMAKLFATEAAREVADL 285
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 17647119 385 CIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQLNTIAK 426
Cdd:cd00567 286 AMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
60-428 |
1.21e-100 |
|
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: 304.81 E-value: 1.21e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 60 EEIMMKQTVKKFAQEHVAPLVSSMDENSKMEKSVIQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDASVALLC 139
Cdd:cd01160 2 EHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 140 dIQNTIINNLFRKHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRADKSGNYYVLNGSKMWISHAEHAELFL 218
Cdd:cd01160 82 -LHTDIVSPYITRAGSPEQKERVLPQMVAgKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 219 VFANVD-PSSGYRGITCFLVDRDTEGFQIGKRENKMGIRASSTCQLTFENVKVPETNILGKIGHGYKYAIGSLNEGRIGI 297
Cdd:cd01160 161 VVARTGgEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 298 AAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLVEAGRPFIKEASMAKYYASEV 377
Cdd:cd01160 241 AAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATEL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 17647119 378 AGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:cd01160 321 QNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
57-426 |
3.62e-99 |
|
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: 302.08 E-value: 3.62e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 57 LTDEEIMMKQTVKKFAQEHVAPLVssMDENSKMEKSVIQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAkVDASVA 136
Cdd:cd01161 27 QTEELNMLVGPVEKFFEEVNDPAK--NDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVG-MDLGFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 137 LLCDIQNTIINNLFRKHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRADKS--GNYYVLNGSKMWISHAEH 213
Cdd:cd01161 104 VTLGAHQSIGFKGILLFGTEAQKEKYLPKLASgEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWITNGGI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 214 AELFLVFANVD----PSSGYRGITCFLVDRDTEGFQIGKRENKMGIRASSTCQLTFENVKVPETNILGKIGHGYKYAIGS 289
Cdd:cd01161 184 ADIFTVFAKTEvkdaTGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 290 LNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLVEAG--RPFIKEA 367
Cdd:cd01161 264 LNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGlkAEYQIEA 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 17647119 368 SMAKYYASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQLNTIAK 426
Cdd:cd01161 344 AISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIAL 402
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
57-428 |
1.89e-93 |
|
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: 286.26 E-value: 1.89e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 57 LTDEEIMMKQTVKKFAQEHVAPLVSSMDENSKMEKSVIQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDASVA 136
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 137 LLCDIQNTIINNLFRkHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRADKSGNYYVLNGSKMWISHAEHAE 215
Cdd:cd01162 81 AYISIHNMCAWMIDS-FGNDEQRERFLPDLCTmEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 216 LFLVFANVDpSSGYRGITCFLVDRDTEGFQIGKRENKMGIRASSTCQLTFENVKVPETNILGKIGHGYKYAIGSLNEGRI 295
Cdd:cd01162 160 VYVVMARTG-GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 296 GIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLVEAGRP-FIKEASMAKYYA 374
Cdd:cd01162 239 NIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPdAVKLCAMAKRFA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 17647119 375 SEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:cd01162 319 TDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARAL 372
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
32-428 |
1.31e-87 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 272.52 E-value: 1.31e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 32 VLKSSQPEALVSLTNNAVAFAPLQTLTDEEIMMKQTVKKFAQEHVAPLVSSMDENSKMEKSV----IQGLFqqGLMGIEV 107
Cdd:PLN02519 1 MLLSAAKARRRGLARRFSSSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlwkLMGDF--NLHGITA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 108 EAQYGGTEASFFCSVLVIEELAKVDASVALLCDIQ-NTIINNLFRkHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDS 185
Cdd:PLN02519 79 PEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHsNLCINQLVR-NGTPAQKEKYLPKLISgEHVGALAMSEPNSGSDV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 186 FAMKTRADKSGNYYVLNGSKMWISHAEHAELFLVFANVDPSSGYRGITCFLVDRDTEGFQIGKRENKMGIRASSTCQLTF 265
Cdd:PLN02519 158 VSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 266 ENVKVPETNILGKIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEA 345
Cdd:PLN02519 238 ENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 346 TRLLTYNAARLVEAGRPFIKEASMAKYYASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQLNTIA 425
Cdd:PLN02519 318 SRSYVYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIG 397
|
...
gi 17647119 426 KHI 428
Cdd:PLN02519 398 REL 400
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
57-430 |
9.39e-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: 266.76 E-value: 9.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 57 LTDEEIMMKQTVKKFAQEHVAPLVSSMDENSKMEKSVIQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDASVA 136
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 137 LLCDiQNTIINNLFRKHASEEQKATYLPKLVTEKL-GSFCLSEAGAGSDSFAMKTRADKSGNYYVLNGSKMWISHAEHAE 215
Cdd:cd01157 81 TAIE-ANSLGQMPVIISGNDEQKKKYLGRMTEEPLmCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 216 LFLVFANVDP---SSGYRGITCFLVDRDTEGFQIGKRENKMGIRASSTCQLTFENVKVPETNILGKIGHGYKYAIGSLNE 292
Cdd:cd01157 160 WYFLLARSDPdpkCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 293 GRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLVEAGRPFIKEASMAKY 372
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 17647119 373 YASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQLNTIAK-HIDA 430
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISReHLGK 378
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
57-419 |
2.88e-79 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 250.35 E-value: 2.88e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 57 LTDEEIMMKQTVKKFAQEHVAPLVSSMDENSKMEKSVIQGLFQQGLMGIEVEAqYGGTEASFFCSVLVIEELAKVDASVA 136
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKG-YGCAGLSSVAYGLIAREVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 137 LLCDIQNTIINNLFRKHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRADKSGNYYVLNGSKMWISHAEHAE 215
Cdd:cd01151 92 SFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASgELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 216 LFLVFANVDPSSGYRGitcFLVDRDTEGFQIGKRENKMGIRASSTCQLTFENVKVPETNILGKIgHGYKYAIGSLNEGRI 295
Cdd:cd01151 172 VFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNARY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 296 GIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLVEAGRPFIKEASMAKYYAS 375
Cdd:cd01151 248 GIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNC 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 17647119 376 EVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNI 419
Cdd:cd01151 328 GKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDI 371
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
40-419 |
7.79e-79 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 249.85 E-value: 7.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 40 ALVSLTNNAVAFAPLQTLTDEEIMMKQTVKKFAQEHVAPLVSSMDENSKMEKSVIQGLFQQGLMGIEVEAQYGGTEASFF 119
Cdd:PTZ00461 20 AAATMTSASRAFMDLYNPTPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 120 CSVLVIEELAKVDASVALLCDIQNTIINNLFRKHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRADKSGN- 197
Cdd:PTZ00461 100 AAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTgEHVGAMGMSEPGAGTDVLGMRTTAKKDSNg 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 198 YYVLNGSKMWISHAEHAELFLVFANVDPSsgyrgITCFLVDRDTEGFQIGKRENKMGIRASSTCQLTFENVKVPETNILG 277
Cdd:PTZ00461 180 NYVLNGSKIWITNGTVADVFLIYAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 278 KIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLV 357
Cdd:PTZ00461 255 EEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNV 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647119 358 EAGRPFIKEASMAKYYASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKI-----GTIYEGASNI 419
Cdd:PTZ00461 335 HPGNKNRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLleiggGTIEAHHKNI 401
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
67-428 |
2.22e-62 |
|
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: 206.86 E-value: 2.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 67 TVKKFAQEHVAPLVSSMDEN------------SKMEKSViQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDAS 134
Cdd:cd01153 4 EVARLAENVLAPLNADGDREgpvfddgrvvvpPPFKEAL-DAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 135 VALLCDIQNTIinNLFRKHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRA--DKSGNYYvLNGSKMWISHA 211
Cdd:cd01153 83 LMYASGTQGAA--ATLLAHGTEAQREKWIPRLAEgEWTGTMCLTEPDAGSDLGALRTKAvyQADGSWR-INGVKRFISAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 212 EHAE----LFLVFANV-DPSSGYRGITCFLV-----DRDTEGFQIGKRENKMGIRASSTCQLTFENVKVPetnILGKIGH 281
Cdd:cd01153 160 EHDMseniVHLVLARSeGAPPGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 282 GYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQglqhQVA---------QVATQ---LEATRLL 349
Cdd:cd01153 237 GLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAP----AVTiihhpdvrrSLMTQkayAEGSRAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 350 TYNAARLVEAGRPFIKEAS--------------MAKYYASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEG 415
Cdd:cd01153 313 DLYTATVQDLAERKATEGEdrkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEG 392
|
410
....*....|...
gi 17647119 416 ASNIQLNTIAKHI 428
Cdd:cd01153 393 TTGIQALDLIGRK 405
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
57-432 |
5.04e-57 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 192.25 E-value: 5.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 57 LTDEEIMMKQTVKKF-AQEHVAPLVSSMDENSKMEKSVIQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDASV 135
Cdd:PRK12341 5 LTEEQELLLASIRELiTRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 136 ALLCDIQNtiINNLfRKHASEEQKATYLPKLVTEKLGSFCL--SEAGAGSDSFAMKTRAD-KSGNYYvLNGSKMWISHAE 212
Cdd:PRK12341 85 FLITNGQC--IHSM-RRFGSAEQLRKTAESTLETGDPAYALalTEPGAGSDNNSATTTYTrKNGKVY-LNGQKTFITGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 213 HAELFLVFA-NVDPSSGYRGITCFLVDRDTEGFQIGKREnKMGIRASSTCQLTFENVKVPETNILGKIGHGYKYAIGSLN 291
Cdd:PRK12341 161 EYPYMLVLArDPQPKDPKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 292 EGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLVEAGRPFIKEASMAK 371
Cdd:PRK12341 240 MERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAK 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647119 372 YYASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQLNTIAKHIDAEY 432
Cdd:PRK12341 320 LYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDY 380
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
280-428 |
1.73e-56 |
|
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: 183.22 E-value: 1.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 280 GHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLVEA 359
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17647119 360 GRPFIKEASMAKYYASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
57-419 |
4.34e-48 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 169.65 E-value: 4.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 57 LTDEEIMMKQTVKKFAQEHVAPLVSSMDENSKMEKSVIQGLFQQGLMGIEVEAqYGGTEASFFCSVLVIEELAKVDASVA 136
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIKG-YGCPGLSITASAIATAEVARVDASCS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 137 LLCDIQNTIINNLFRKHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRADKSGNYYVLNGSKMWISHAEHAE 215
Cdd:PLN02526 108 TFILVHSSLAMLTIALCGSEAQKQKYLPSLAQlDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 216 LFLVFANvdpSSGYRGITCFLVDRDTEGFQIGKRENKMGIRASSTCQLTFENVKVPETNILGKIgHGYKYAIGSLNEGRI 295
Cdd:PLN02526 188 VLVIFAR---NTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSRV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 296 GIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLVEAGRPFIKEASMAKYYAS 375
Cdd:PLN02526 264 MVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWIT 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 17647119 376 EVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNI 419
Cdd:PLN02526 344 KKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDI 387
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
97-428 |
2.37e-47 |
|
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: 166.75 E-value: 2.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 97 LFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDASVALLCDIQNTIINNLFRkHASEEQKATYLPKLVTEKLgSFCL 176
Cdd:cd01152 44 LAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILA-YGTDEQKRRFLPPILSGEE-IWCQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 177 --SEAGAGSDSFAMKTRADKSGNYYVLNGSKMWISHAEHAELFLVFANVDPSS-GYRGITCFLVDRDTEGFQIGKRENKM 253
Cdd:cd01152 122 gfSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEApKHRGISILLVDMDSPGVTVRPIRSIN 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 254 GirASSTCQLTFENVKVPETNILGKIGHGYKYAIGSLNEGR---IGIAAQMLGLAQGCFDYTIPYIKERMqfgkrifDFQ 330
Cdd:cd01152 202 G--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERvsiGGSAATFFELLLARLLLLTRDGRPLI-------DDP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 331 GLQHQVAQVATQLEATRLLTYNAARLVEAGRPFIKEASMAKYYASEVAGLTTSKCIEWMG--------GVGYTKDYPVEK 402
Cdd:cd01152 273 LVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGtaallrdpAPGAELAGRWEA 352
|
330 340
....*....|....*....|....*.
gi 17647119 403 FFRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:cd01152 353 DYLRSRATTIYGGTSEIQRNIIAERL 378
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
56-432 |
3.19e-41 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 150.37 E-value: 3.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 56 TLTDEEIMMKQTVKKF-AQEHVAPLVSSMDENSKMEKSVIQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDAS 134
Cdd:PRK03354 4 NLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 135 VALLCDIQNTIinNLFRKHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRADKSGNYYVLNGSKMWISHAEH 213
Cdd:PRK03354 84 TYVLYQLPGGF--NTFLREGTQEQIDKIMAFRGTgKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 214 AELFLVFANVDPSSGYRGITCFLVDRDTEGFQIGKREnKMGIRASSTCQLTFENVKVPETNILGKIGHGYKYAIGSLNEG 293
Cdd:PRK03354 162 TPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 294 RIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLVEAGRPFIKEASMAKYY 373
Cdd:PRK03354 241 RFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 17647119 374 ASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQLNTIAKHIDAEY 432
Cdd:PRK03354 321 CANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQY 379
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
132-420 |
9.29e-40 |
|
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: 147.13 E-value: 9.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 132 DASVALLCDIqnTIINN---LFRKHASEEQKATYLPKLVTEK----LGSFCLSEAGAGSDSFAMKTRADKS-GNYYVLNG 203
Cdd:cd01154 104 DAAAGLLCPL--TMTDAavyALRKYGPEELKQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSgGGVYRLNG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 204 SKmWISHAEHAELFLVFAN-VDPSSGYRGITCFLVDRDTE-----GFQIGKRENKMGIRASSTCQLTFENVkvpETNILG 277
Cdd:cd01154 182 HK-WFASAPLADAALVLARpEGAPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 278 KIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLV 357
Cdd:cd01154 258 DEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAF 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17647119 358 ---EAGRPfiKEASMA-------KYYASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQ 420
Cdd:cd01154 338 draAADKP--VEAHMArlatpvaKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
66-426 |
1.10e-37 |
|
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: 140.99 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 66 QTVKKFAQEHVAPLVSSMDE------NSKMEKS-VIQGLFQ----QGLMGIEVEAQYGGTEASFFCSVLVIEELAK-VDA 133
Cdd:cd01155 8 ARVKAFMEEHVYPAEQEFLEyyaeggDRWWTPPpIIEKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRsFFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 134 SVALLCDIQNTIINNLFRKHASEEQKATYLPKLVTEKLGS-FCLSEAG-AGSDSFAMKTRADKSGNYYVLNGSKMWISHA 211
Cdd:cd01155 88 PEVFNCQAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSaFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 212 EH--AELFLVFANVDPS--SGYRGITCFLVDRDTEGFQIgkrenkmgIRASST----------CQLTFENVKVPETNILG 277
Cdd:cd01155 168 GDprCKIAIVMGRTDPDgaPRHRQQSMILVPMDTPGVTI--------IRPLSVfgyddaphghAEITFDNVRVPASNLIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 278 KIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLV 357
Cdd:cd01155 240 GEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMI 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647119 358 EAGRPFI--KEASMAKYYASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQLNTIAK 426
Cdd:cd01155 320 DTVGNKAarKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
70-428 |
6.31e-37 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 142.70 E-value: 6.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 70 KFAQEHVAPLVSSMDENS------------KMEKSVIQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDASVAL 137
Cdd:PTZ00456 69 KLATQTLLPLYESSDSEGcvllkdgnvttpKGFKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSM 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 138 LCDIQNTIINNLFrKHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRADKSGN-YYVLNGSKMWISHAEHAE 215
Cdd:PTZ00456 149 YPGLSIGAANTLM-AWGSEEQKEQYLTKLVSgEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDHDL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 216 ----LFLVFANVdPSS--GYRGITCFLVDR---------DTE-GFQIGKRENKMGIRASSTCQLTFENVKvpeTNILGKI 279
Cdd:PTZ00456 228 teniVHIVLARL-PNSlpTTKGLSLFLVPRhvvkpdgslETAkNVKCIGLEKKMGIKGSSTCQLSFENSV---GYLIGEP 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 280 GHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQF------------GKRIFDFQGLQHQVAQVATQLEATR 347
Cdd:PTZ00456 304 NAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNILFAKAVAEGGR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 348 LLTYNAARLV----EAGRPFIKEA---------SMAKYYASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYE 414
Cdd:PTZ00456 384 ALLLDVGRLLdihaAAKDAATREAldheigfytPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYE 463
|
410
....*....|....*
gi 17647119 415 GASNIQ-LNTIAKHI 428
Cdd:PTZ00456 464 GTTGIQaLDFIGRKV 478
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
58-168 |
4.78e-34 |
|
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: 122.96 E-value: 4.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 58 TDEEIMMKQTVKKFAQEHVAPLVSSMDENSKMEKSVIQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDASVAL 137
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|.
gi 17647119 138 LCDIQNTIINNLFRKHASEEQKATYLPKLVT 168
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
173-266 |
1.62e-30 |
|
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: 113.14 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 173 SFCLSEAGAGSDSFAMKTRA-DKSGNYYVLNGSKMWISHAEHAELFLVFANVDPSSGYRGITCFLVDRDTEGFQIGKREN 251
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 17647119 252 KMGIRASSTCQLTFE 266
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
296-417 |
1.40e-24 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 98.19 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 296 GIAAQMLGLAQGCFDYTIPYIKER--MQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAA----RLVEAGRPF----IK 365
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRvrAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVtpalRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 17647119 366 EASMAKYYASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGAS 417
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
149-426 |
2.10e-22 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 100.25 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 149 LFRKHASEEQKATYLPKLVTEKLGSFCLSEAG-AGSDSFAMKTRADKSGNYYVLNGSKMWISHA--EHAELFLVFANVDP 225
Cdd:PLN02876 529 LLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTDF 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 226 SSG-YRGITCFLVDRDTEGFQIGKRENKMGIRAS--STCQLTFENVKVPETNILGKIGHGYKYAIGSLNEGRIGIAAQML 302
Cdd:PLN02876 609 NAPkHKQQSMILVDIQTPGVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLI 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 303 GLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAQVATQLEATRLLTYNAA-RLVEAGRPFIKEA-SMAKYYASEVAGL 380
Cdd:PLN02876 689 GAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAAdQLDRLGNKKARGIiAMAKVAAPNMALK 768
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 17647119 381 TTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGASNIQLNTIAK 426
Cdd:PLN02876 769 VLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAK 814
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
53-378 |
3.73e-20 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 93.10 E-value: 3.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 53 PLQTLTDEEimmkqtvKKFAQEHVAPLVSSMDE-----NSK-MEKSVIQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIE 126
Cdd:PRK13026 74 PKPTLTAEE-------QAFIDNEVETLLTMLDDwdivqNRKdLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 127 ELAKVDASVALLCDIQNTI-INNLFRKHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMK-----TRADKSGNYY 199
Cdd:PRK13026 147 KIATRSVSAAVTVMVPNSLgPGELLTHYGTQEQKDYWLPRLADgTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 200 V---LNGSKMWISHAEHAE-LFLVFANVDP-----SSGYRGITCFLVDRDTEGFQIGKRENKMGIRasstcqltFEN--- 267
Cdd:PRK13026 227 LglrLTWDKRYITLAPVATvLGLAFKLRDPdgllgDKKELGITCALIPTDHPGVEIGRRHNPLGMA--------FMNgtt 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 268 ----VKVPETNILG---KIGHGYKYAIGSLNEGRiGIAAQMLGLAQG--CFDYTIPYIKERMQFGKRIFDFQGLQHQVAQ 338
Cdd:PRK13026 299 rgkdVFIPLDWIIGgpdYAGRGWRMLVECLSAGR-GISLPALGTASGhmATRTTGAYAYVRRQFGMPIGQFEGVQEALAR 377
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 17647119 339 VAT---QLEATRLLTynAARLVEAGRPFIKEAsMAKYYASEVA 378
Cdd:PRK13026 378 IAGntyLLEAARRLT--TTGLDLGVKPSVVTA-IAKYHMTELA 417
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
84-407 |
4.83e-16 |
|
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: 79.32 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 84 DENSKMEKSVIQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDASVALLCDIQNTIinnlfrkhaseEQKATYL 163
Cdd:cd01159 18 ERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATH-----------SRMLAAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 164 PKLVTEKLgsfcLSEAGAG--SDSFAMKTRADKSGNYYVLNGSKMWISHAEHAELFLVFANVDPSSGYRGITCFLVDRdt 241
Cdd:cd01159 87 PPEAQEEV----WGDGPDTllAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAFVVPR-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 242 EGFQIGKRENKMGIRASSTCQLTFENVKVPETNIL-----------GKIGHGYKYAIGSLNEgrIGIAAQMLGLAQGCFD 310
Cdd:cd01159 161 AEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagdmmagdgpGGSTPVYRMPLRQVFP--LSFAAVSLGAAEGALA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 311 YTIPYIKERMQ---FGKRIFDFQGLQHQVAQVATQLEATRLLTYNAARLVEA----GRPF-IKEASMAKYYASEVAGLTT 382
Cdd:cd01159 239 EFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAhalaGGPIdVEERARIRRDAAYAAKLSA 318
|
330 340
....*....|....*....|....*...
gi 17647119 383 S---KCIEWMGGVGYTKDYPVEKFFRDA 407
Cdd:cd01159 319 EavdRLFHAAGGSALYTASPLQRIWRDI 346
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
99-376 |
9.04e-14 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 73.31 E-value: 9.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 99 QQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDASVALLCDIQNTI-INNLFRKHASEEQKATYLPKLVT-EKLGSFCL 176
Cdd:PRK09463 120 EHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLgPGELLLHYGTDEQKDHYLPRLARgEEIPCFAL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 177 SEAGAGSDSFAMK-----TRADKSGN---YYVLNGSKMWISHAEHAELF-LVFANVDP-----SSGYRGITCFLVDRDTE 242
Cdd:PRK09463 200 TSPEAGSDAGSIPdtgvvCKGEWQGEevlGMRLTWNKRYITLAPIATVLgLAFKLYDPdgllgDKEDLGITCALIPTDTP 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 243 GFQIGKRENKMGIRasstcqltFEN-------VKVPETNILG---KIGHGYKYAIGSLNEGR-IGIAAQMLGLAQGCFDY 311
Cdd:PRK09463 280 GVEIGRRHFPLNVP--------FQNgptrgkdVFIPLDYIIGgpkMAGQGWRMLMECLSVGRgISLPSNSTGGAKLAALA 351
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17647119 312 TIPYIKERMQFGKRIFDFQGLQHQVAQVAT---QLEATRLLTYNAarLVEAGRPFIKEAsMAKYYASE 376
Cdd:PRK09463 352 TGAYARIRRQFKLPIGKFEGIEEPLARIAGnayLMDAARTLTTAA--VDLGEKPSVLSA-IAKYHLTE 416
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
143-428 |
2.51e-12 |
|
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: 68.51 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 143 NTIINNlfrkhASEEQKATYLPKLVTEKL-GSFCLSEAGAGSDSFAMKTRA--DKSGNYYVLN-----GSKMWIS----H 210
Cdd:cd01150 111 NAIKNL-----GTDEHQDYWLQGANNLEIiGCFAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWWPGnlgkT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 211 AEHAelfLVFANVDPSSGYRGITCFLVD-RDTEGFQ------IGKRENKMGIRASSTCQLTFENVKVPETNILGK----- 278
Cdd:cd01150 186 ATHA---VVFAQLITPGKNHGLHAFIVPiRDPKTHQplpgvtVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRfgdvs 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 279 -----------IGHGYKYAIGSLNEGRIGIAaqMLGLAQGCFDYTIP--YIKERMQFGKR-------IFDFQGLQHqvaQ 338
Cdd:cd01150 263 pdgtyvspfkdPNKRYGAMLGTRSGGRVGLI--YDAAMSLKKAATIAirYSAVRRQFGPKpsdpevqILDYQLQQY---R 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 339 VATQLEATRLLTYNAARLVEAGRPFIKEASMA---------------KYYASEVAGLTTSKCIEWMGGVGYTKDYPVEKF 403
Cdd:cd01150 338 LFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGnsellaelhalsaglKAVATWTAAQGIQECREACGGHGYLAMNRLPTL 417
|
330 340
....*....|....*....|....*
gi 17647119 404 FRDAKIGTIYEGASNIQLNTIAKHI 428
Cdd:cd01150 418 RDDNDPFCTYEGDNTVLLQQTANYL 442
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
94-359 |
7.25e-12 |
|
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: 66.58 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 94 IQGLFQQGLMGIEVEAQYGGTEASFFCSVLVIEELAKVDASVAllcdiqntiinNLFRKH----------ASEEQKATYL 163
Cdd:cd01163 28 VALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIA-----------QALRAHfgfvealllaGPEQFRKRWF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 164 PKLVTEKLGSFCLSEAG-AGSDSFAMKTRADksGNYYVLNGSKMWISHAEHAELFLVFAnVDPSSgyrGITCFLVDRDTE 242
Cdd:cd01163 97 GRVLNGWIFGNAVSERGsVRPGTFLTATVRD--GGGYVLNGKKFYSTGALFSDWVTVSA-LDEEG---KLVFAAVPTDRP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 243 GFQIGKRENKMGIR--ASSTcqLTFENVKVPETNILGKighGYKYAIGSLNEGRIGI--AAQMLGLAQGCFDYTIPYIKE 318
Cdd:cd01163 171 GITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLPR---PNAPDRGTLLTAIYQLvlAAVLAGIARAALDDAVAYVRS 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17647119 319 RmqfgKRIF----------DFQGLQHqVAQVATQLEATRLLTYNAARLVEA 359
Cdd:cd01163 246 R----TRPWihsgaesardDPYVQQV-VGDLAARLHAAEALVLQAARALDA 291
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
176-419 |
5.67e-11 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 64.39 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 176 LSEAGAGSDSFAMKTRADK-SGNYYVLNGSKmWISHAEHAELFLVFANVDpssgyRGITCFLVDR-----DTEGFQIGKR 249
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAK-----GGLSCFFVPRflpdgQRNAIRLERL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 250 ENKMGIRASSTCQLTFENVKvpeTNILGKIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDf 329
Cdd:PRK11561 258 KDKLGNRSNASSEVEFQDAI---GWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIE- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 330 QGLQHQV-AQVATQLEATRLLTYNAARLVEAgRPFIKEASM-------AKYYASEVAGLTTSKCIEWMGGVGYTKDYPVE 401
Cdd:PRK11561 334 QPLMRQVlSRMALQLEGQTALLFRLARAWDR-RADAKEALWarlftpaAKFVICKRGIPFVAEAMEVLGGIGYCEESELP 412
|
250
....*....|....*...
gi 17647119 402 KFFRDAKIGTIYEGASNI 419
Cdd:PRK11561 413 RLYREMPVNSIWEGSGNI 430
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
124-432 |
2.88e-08 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 56.02 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 124 VIEELAKVDASVALLCDIQ-----NTIINNLFRKHaseeqKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRA--DKS 195
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVQyslwgGSVINLGTKKH-----RDKYFDGIDNlDYPGCFAMTELHHGSNVQGLQTTAtfDPL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 196 GNYYVLN-----GSKMWISHAE-HAELFLVFANVD-PSSGYRGIT-----CFLVD-RDTE------GFQIGKRENKMGIR 256
Cdd:PLN02636 201 TDEFVINtpndgAIKWWIGNAAvHGKFATVFARLKlPTHDSKGVSdmgvhAFIVPiRDMKthqvlpGVEIRDCGHKVGLN 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 257 ASSTCQLTFENVKVPETNILGKIGH-----GYKYAIGSLNE-----------GRIGIAAQMLGLAQGCFDYTIPYIKERM 320
Cdd:PLN02636 281 GVDNGALRFRSVRIPRDNLLNRFGDvsrdgKYTSSLPTINKrfaatlgelvgGRVGLAYGSVGVLKASNTIAIRYSLLRQ 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 321 QFGK------RIFDFQGLQHQVAQVATQLEATRLLT-YNAARLVEAGRPFIKE---------ASMAKYYASEVAGlTTSK 384
Cdd:PLN02636 361 QFGPpkqpeiSILDYQSQQHKLMPMLASTYAFHFATeYLVERYSEMKKTHDDQlvadvhalsAGLKAYITSYTAK-ALST 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 17647119 385 CIEWMGGVGYTKdypVEKF--FR-DAKIGTIYEGASNIQLNTIAKHIDAEY 432
Cdd:PLN02636 440 CREACGGHGYAA---VNRFgsLRnDHDIFQTFEGDNTVLLQQVAADLLKQY 487
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
150-336 |
3.61e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 49.07 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 150 FRKHASEEQKATYLPKLVT-EKLGSFCLSEAGAGSDSFAMKTRA--DKSGNYYVLN-----GSKMWISH-AEHAELFLVF 220
Cdd:PTZ00460 106 FQVLGTDEQINLWMPSLLNfEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVY 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 221 ANVDPSSGYRGITCFLV---DRDT----EGFQIGKRENKMGIRASSTCQLTFENVKVPETNILGK----------IGHGy 283
Cdd:PTZ00460 186 AKLIVNGKNKGVHPFMVrirDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARyikvsedgqvERQG- 264
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17647119 284 kyaigslNEgRIGIAAQMLGLAQGCFDYT----------IPYIKERMQFGK------RIFDFQGLQHQV 336
Cdd:PTZ00460 265 -------NP-KVSYASMMYMRNLIIDQYPrfaaqaltvaIRYSIYRQQFTNdnkqenSVLEYQTQQQKL 325
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
172-276 |
6.13e-03 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 38.99 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647119 172 GSFCLSEAGAGSDSFAMKTRA--DKSGNYYVLN-----GSKMWIS-HAEHAELFLVFANVDPSSGYRGITCFLVD-RDTE 242
Cdd:PLN02312 187 GCFAMTELGHGSNVRGIETVTtyDPKTEEFVINtpcesAQKYWIGgAANHATHTIVFSQLHINGKNEGVHAFIAQiRDQD 266
|
90 100 110
....*....|....*....|....*....|....*....
gi 17647119 243 G-----FQIGKRENKMGIRASSTCQLTFENVKVPETNIL 276
Cdd:PLN02312 267 GnicpnIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLL 305
|
|
| |
