|
Name |
Accession |
Description |
Interval |
E-value |
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
114-484 |
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: 597.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 114 EEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVALI 193
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 194 SELQNTLINRLLIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQAGMF 272
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 273 YVMANVDPSLGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNRGRIGI 352
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 353 AAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYYAAEV 432
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1394717032 433 ATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCIA 484
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLL 372
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
111-481 |
1.29e-165 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 472.79 E-value: 1.29e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 111 TLTEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAV 190
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 191 ALIseLQNTLIN-RLLIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQ 268
Cdd:COG1960 84 ALP--VGVHNGAaEALLRFGTEEQKERYLPRLASgEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 269 AGMFYVMANVDPSLGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNRG 348
Cdd:COG1960 162 ADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 349 RIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYY 428
Cdd:COG1960 242 RLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLF 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1394717032 429 AAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 481
Cdd:COG1960 322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIAR 374
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
112-481 |
4.32e-113 |
|
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: 338.62 E-value: 4.32e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 112 LTEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVA 191
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 192 L-ISELQNTLINRLlIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQA 269
Cdd:cd01156 82 LsYGAHSNLCINQI-YRNGSAAQKEKYLPKLISgEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 270 GMFYVMANVDPSLGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNRGR 349
Cdd:cd01156 161 DTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 350 IGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYYA 429
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1394717032 430 AEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 481
Cdd:cd01156 321 AEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGR 372
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
114-481 |
1.68e-112 |
|
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: 335.41 E-value: 1.68e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 114 EEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGidlgtewggtgssffstilvveelakvdaavali 193
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLGAA---------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 194 selqntlinrLLIVHGTEKQKRTYLPRLAKD-MVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQAGMF 272
Cdd:cd00567 47 ----------LLLAYGTEEQKERYLPPLASGeAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 273 YVMANVDPS-LGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNRGRIG 351
Cdd:cd00567 117 IVLARTDEEgPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 352 IAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFI-KEASMAKYYAA 430
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEArLEAAMAKLFAT 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1394717032 431 EVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 481
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
112-486 |
2.12e-101 |
|
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: 308.60 E-value: 2.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 112 LTEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVA 191
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 192 LISELQNT---LINRLlivhGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAE 267
Cdd:cd01162 81 AYISIHNMcawMIDSF----GNDEQRERFLPDLCTmEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 268 QAGMFYVMANVDPSlGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNR 347
Cdd:cd01162 157 DSDVYVVMARTGGE-GPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 348 GRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKP-FIKEASMAK 426
Cdd:cd01162 236 GRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPdAVKLCAMAK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 427 YYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCIAQE 486
Cdd:cd01162 316 RFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
112-487 |
1.59e-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: 305.16 E-value: 1.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 112 LTEEEQLLKETVKKFAQERIAPfvKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTG-SSFFSTILVveELAKVDAAV 190
Cdd:cd01161 27 QTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGlNNTQYARLA--EIVGMDLGF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 191 ALISELQNTLINRLLIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKK--GDYYIINGSKMWISSAE 267
Cdd:cd01161 103 SVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASgEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWITNGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 268 QAGMFYVMAN---VDPSLGYR-GITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIG 343
Cdd:cd01161 183 IADIFTVFAKtevKDATGSVKdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 344 MLNRGRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETG--KPFIKE 421
Cdd:cd01161 263 ILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGlkAEYQIE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394717032 422 ASMAKYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCIAQEY 487
Cdd:cd01161 343 AAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHA 408
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
112-481 |
1.80e-96 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 296.03 E-value: 1.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 112 LTEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVA 191
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 192 LISElQNTLINRLLIVHGTEKQKRTYLPRLAKD-MVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQAG 270
Cdd:cd01157 81 TAIE-ANSLGQMPVIISGNDEQKKKYLGRMTEEpLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 271 MFYVMANVDP---SLGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNR 347
Cdd:cd01157 160 WYFLLARSDPdpkCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 348 GRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKY 427
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1394717032 428 YAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 481
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISR 373
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
114-483 |
4.30e-95 |
|
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: 292.48 E-value: 4.30e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 114 EEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVALI 193
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 194 SeLQNTLINRLLIVHGTEKQKRTYLPRL-AKDMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQAGMF 272
Cdd:cd01160 81 S-LHTDIVSPYITRAGSPEQKERVLPQMvAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 273 YVMANVD-PSLGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNRGRIG 351
Cdd:cd01160 160 IVVARTGgEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 352 IAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYYAAE 431
Cdd:cd01160 240 IAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1394717032 432 VATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCI 483
Cdd:cd01160 320 LQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
112-486 |
2.77e-84 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 265.59 E-value: 2.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 112 LTEEEQL-LKETVKKFAQERIAPFVKKMDADGKIEESV----LQGLFelGLMGIDLGTEWGGTGSSFFSTILVVEELAKV 186
Cdd:PLN02519 25 LFDDTQLqFKESVQQFAQENIAPHAAAIDATNSFPKDVnlwkLMGDF--NLHGITAPEEYGGLGLGYLYHCIAMEEISRA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 187 DAAVALISELQNTLINRLLIVHGTEKQKRTYLPRL-AKDMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISS 265
Cdd:PLN02519 103 SGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLiSGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 266 AEQAGMFYVMANVDPSLGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGML 345
Cdd:PLN02519 183 GPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 346 NRGRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMA 425
Cdd:PLN02519 263 DLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGV 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394717032 426 KYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCIAQE 486
Cdd:PLN02519 343 ILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
112-474 |
7.57e-77 |
|
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: 245.73 E-value: 7.57e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 112 LTEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLgTEWGGTGSSFFSTILVVEELAKVDAAVA 191
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATI-KGYGCAGLSSVAYGLIAREVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 192 LISELQNTLINRLLIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQAG 270
Cdd:cd01151 92 SFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASgELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 271 MFYVMANVDPSLGYRGitcFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLgQGYKYAIGMLNRGRI 350
Cdd:cd01151 172 VFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNARY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 351 GIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYYAA 430
Cdd:cd01151 248 GIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNC 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1394717032 431 EVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNI 474
Cdd:cd01151 328 GKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDI 371
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
113-481 |
4.91e-70 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 228.67 E-value: 4.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 113 TEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVAL 192
Cdd:PTZ00461 38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 193 ISELQNTLINRLLIVHGTEKQKRTYLPR-LAKDMVGSFCLSEAGSGSDAFSLKTRAEKKGD-YYIINGSKMWISSAEQAG 270
Cdd:PTZ00461 118 AYLAHSMLFVNNFYYSASPAQRARWLPKvLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVAD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 271 MFYVMANVDPSlgyrgITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNRGRI 350
Cdd:PTZ00461 198 VFLIYAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 351 GIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYYAA 430
Cdd:PTZ00461 273 TLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFAT 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1394717032 431 EVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 481
Cdd:PTZ00461 353 PIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITK 403
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
121-475 |
3.49e-67 |
|
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: 221.11 E-value: 3.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 121 ETVKKFAQERIAPFVKKMDADG------------KIEESVlQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDA 188
Cdd:cd01153 3 EEVARLAENVLAPLNADGDREGpvfddgrvvvppPFKEAL-DAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 189 AVALISELQNTLinRLLIVHGTEKQKRTYLPRLA-KDMVGSFCLSEAGSGSDAFSLKTRAEKKGD-YYIINGSKMWISSA 266
Cdd:cd01153 82 PLMYASGTQGAA--ATLLAHGTEAQREKWIPRLAeGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 267 EQAG----MFYVMANV-DPSLGYRGITCFIV-----DRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPetnILGQLGQ 336
Cdd:cd01153 160 EHDMseniVHLVLARSeGAPPGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 337 GYKYAIGMLNRGRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQG---MQHQIA--QVATQ---LEAARLLT-YN 407
Cdd:cd01153 237 GLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAvtiIHHPDVrrSLMTQkayAEGSRALDlYT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 408 AT-----RLAETGKPFIKEAS--------MAKYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNI 474
Cdd:cd01153 317 ATvqdlaERKATEGEDRKALSaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
|
.
gi 1394717032 475 Q 475
Cdd:cd01153 397 Q 397
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
335-481 |
6.01e-58 |
|
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: 188.23 E-value: 6.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 335 GQGYKYAIGMLNRGRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAET 414
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394717032 415 GKPFIKEASMAKYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 481
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
112-487 |
6.16e-57 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 193.41 E-value: 6.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 112 LTEEEQLLKETVKKF-AQERIAPFVKKMDADGKIEESVLQGLFE--LGLMGIDlgTEWGGTGSSFFSTILVVEELAKVDA 188
Cdd:PRK12341 5 LTEEQELLLASIRELiTRNFPEEYFRTCDENGTYPREFMRALADngISMLGVP--EEFGGTPADYVTQMLVLEEVSKCGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 189 AVALISELQNtlINRLLiVHGTEKQKRTYLPRLAKDMVGSFCL--SEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSA 266
Cdd:PRK12341 83 PAFLITNGQC--IHSMR-RFGSAEQLRKTAESTLETGDPAYALalTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 267 EQAGMFYVMA-NVDPSLGYRGITCFIVDRDTEGLcagKKED--KLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIG 343
Cdd:PRK12341 160 KEYPYMLVLArDPQPKDPKKAFTLWWVDSSKPGI---KINPlhKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 344 MLNRGRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEAS 423
Cdd:PRK12341 237 NFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAA 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394717032 424 MAKYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCIAQEY 487
Cdd:PRK12341 317 LAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDY 380
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
152-481 |
6.75e-51 |
|
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: 177.54 E-value: 6.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 152 LFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVALISELQNTLINRLLiVHGTEKQKRTYLPRLA--KDMvgsF 229
Cdd:cd01152 44 LAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTIL-AYGTDEQKRRFLPPILsgEEI---W 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 230 CL--SEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQAGMFYVMANVDPSL-GYRGITCFIVDRDTEGLCAGKKED 306
Cdd:cd01152 120 CQgfSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEApKHRGISILLVDMDSPGVTVRPIRS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 307 KLGlrASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNRGRigiaAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQG 386
Cdd:cd01152 200 ING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFER----VSIGGSAATFFELLLARLLLLTRDGRPLIDDPL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 387 MQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYYAAEVATLTTSKCIEWMGGAGFTKDYP--------VEKY 458
Cdd:cd01152 274 VRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWEAD 353
|
330 340
....*....|....*....|...
gi 1394717032 459 YRDCKIGTIYEGTSNIQLSTIAK 481
Cdd:cd01152 354 YLRSRATTIYGGTSEIQRNIIAE 376
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
112-474 |
5.18e-48 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 170.80 E-value: 5.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 112 LTEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGidlGT--EWGGTGSSFFSTILVVEELAKVDAA 189
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAG---GTikGYGCPGLSITASAIATAEVARVDAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 190 VALISELQNTLINRLLIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQ 268
Cdd:PLN02526 106 CSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQlDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 269 AGMFYVMA-NVDPSlgyrGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLgQGYKYAIGMLNR 347
Cdd:PLN02526 186 ADVLVIFArNTTTN----QINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 348 GRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKY 427
Cdd:PLN02526 261 SRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKA 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1394717032 428 YAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNI 474
Cdd:PLN02526 341 WITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDI 387
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
111-487 |
1.07e-44 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 161.15 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 111 TLTEEEQLLKETVKKF-AQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAA 189
Cdd:PRK03354 4 NLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 190 VALISELQ---NTLINrllivHGTEKQKRTYLPRLA--KDMVGSFClSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWIS 264
Cdd:PRK03354 84 TYVLYQLPggfNTFLR-----EGTQEQIDKIMAFRGtgKQMWNSAI-TEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 265 SAEQAGMFYVMANVDPSLGYRGITCFIVDRDTEGLCAGKKEdKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGM 344
Cdd:PRK03354 158 SSAYTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 345 LNRGRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASM 424
Cdd:PRK03354 237 FDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAM 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394717032 425 AKYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCIAQEY 487
Cdd:PRK03354 317 CKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQY 379
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
215-475 |
3.37e-44 |
|
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: 160.61 E-value: 3.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 215 RTYLPRLA-----KDMVGSFCLSEAGSGSDAFSLKTRAEK-KGDYYIINGSKmWISSAEQAGMFYVMAN-VDPSLGYRGI 287
Cdd:cd01154 132 KQYLPGLLsdrykTGLLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLARpEGAPAGARGL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 288 TCFIVDRDTEGlcaGKK--------EDKLGLRASSTCPVTFENVkvpETNILGQLGQGYKYAIGMLNRGRIGIAAQMLGL 359
Cdd:cd01154 211 SLFLVPRLLED---GTRngyrirrlKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAVAALGI 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 360 AQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRL---AETGKPfiKEASMA-------KYYA 429
Cdd:cd01154 285 MRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAfdrAAADKP--VEAHMArlatpvaKLIA 362
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1394717032 430 AEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQ 475
Cdd:cd01154 363 CKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
205-481 |
7.37e-38 |
|
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: 142.53 E-value: 7.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 205 LIVHGTEKQKRTYL-PRLAKDMVGSFCLSEAG-SGSDAFSLKTRAEKKGDYYIINGSKMWISSA--EQAGMFYVMANVDP 280
Cdd:cd01155 104 LHRYGSEEQKKQWLePLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAgdPRCKIAIVMGRTDP 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 281 SLG--YRGITCFIVDRDTEGLcagKKEDKLGLRASSTCP-----VTFENVKVPETNILGQLGQGYKYAIGMLNRGRIGIA 353
Cdd:cd01155 184 DGAprHRQQSMILVPMDTPGV---TIIRPLSVFGYDDAPhghaeITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHC 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 354 AQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFI--KEASMAKYYAAE 431
Cdd:cd01155 261 MRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAarKEIAMIKVAAPR 340
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1394717032 432 VATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 481
Cdd:cd01155 341 MALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
113-223 |
1.70e-36 |
|
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: 130.66 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 113 TEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVAL 192
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|.
gi 1394717032 193 ISELQNTLINRLLIVHGTEKQKRTYLPRLAK 223
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
116-475 |
5.83e-33 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 132.30 E-value: 5.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 116 EQLLKETvKKFAQERIAPFVKKMDADG------------KIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEEL 183
Cdd:PTZ00456 61 DSLLEEA-SKLATQTLLPLYESSDSEGcvllkdgnvttpKGFKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELM 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 184 AKVDAAVALISELQNTLINRLLiVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKKGD-YYIINGSKM 261
Cdd:PTZ00456 140 ATANWGFSMYPGLSIGAANTLM-AWGSEEQKEQYLTKLVSgEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 262 WISSAEQ---AGMFY-VMANVDPSL-GYRGITCFIVDR---DTEGLCAGKK-------EDKLGLRASSTCPVTFENVKvp 326
Cdd:PTZ00456 219 FISAGDHdltENIVHiVLARLPNSLpTTKGLSLFLVPRhvvKPDGSLETAKnvkciglEKKMGIKGSSTCQLSFENSV-- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 327 eTNILGQLGQGYKYAIGMLNRGRIGIAAQMLGLAQGCFDQTLPYTKERVQF------------GKSIFDFQGMQHQIAQV 394
Cdd:PTZ00456 297 -GYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNILFA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 395 ATQLEAARLLTYNATRL----AETGKPFIKEA---------SMAKYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRD 461
Cdd:PTZ00456 376 KAVAEGGRALLLDVGRLldihAAAKDAATREAldheigfytPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRD 455
|
410
....*....|....
gi 1394717032 462 CKIGTIYEGTSNIQ 475
Cdd:PTZ00456 456 ARIGTLYEGTTGIQ 469
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
228-321 |
5.17e-27 |
|
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: 104.28 E-value: 5.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 228 SFCLSEAGSGSDAFSLKTRA-EKKGDYYIINGSKMWISSAEQAGMFYVMANVDPSLGYRGITCFIVDRDTEGLCAGKKED 306
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 1394717032 307 KLGLRASSTCPVTFE 321
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
351-472 |
7.02e-24 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 96.65 E-value: 7.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 351 GIAAQMLGLAQGCFDQTLPYTKERVQ--FGKSIFDFQGMQHQIAQVATQLEAARLLTYNAT----RLAETGKPF----IK 420
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVtpalRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1394717032 421 EASMAKYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTS 472
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
204-481 |
5.39e-22 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 99.48 E-value: 5.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 204 LLIVHGTEKQKRTYL-PRLAKDMVGSFCLSEAG-SGSDAFSLKTRAEKKGDYYIINGSKMWISSA--EQAGMFYVMANVD 279
Cdd:PLN02876 528 VLLRYGNKEQQLEWLiPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTD 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 280 PSLG-YRGITCFIVDRDTEGLcagKKEDKLGLRASSTCP-----VTFENVKVPETNILGQLGQGYKYAIGMLNRGRIGIA 353
Cdd:PLN02876 608 FNAPkHKQQSMILVDIQTPGV---QIKRPLLVFGFDDAPhghaeISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHC 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 354 AQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNAT-RLAETGKPFIKEA-SMAKYYAAE 431
Cdd:PLN02876 685 MRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAAdQLDRLGNKKARGIiAMAKVAAPN 764
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1394717032 432 VATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 481
Cdd:PLN02876 765 MALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAK 814
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
108-433 |
2.55e-21 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 97.34 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 108 PLQTLTEEEQllketvkKFAQERIAPFVKKMD------ADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVE 181
Cdd:PRK13026 74 PKPTLTAEEQ-------AFIDNEVETLLTMLDdwdivqNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 182 ELA--KVDAAVALIseLQNTLINRLLIVH-GTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLK-----TRAEKKGD 252
Cdd:PRK13026 147 KIAtrSVSAAVTVM--VPNSLGPGELLTHyGTQEQKDYWLPRLADgTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 253 YYI---INGSKMWISSAEQA---GMFYVMANVDPSLGYR---GITCFIVDRDTEGLCAGKKEDKLGLrASSTCPVTFENV 323
Cdd:PRK13026 225 EVLglrLTWDKRYITLAPVAtvlGLAFKLRDPDGLLGDKkelGITCALIPTDHPGVEIGRRHNPLGM-AFMNGTTRGKDV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 324 KVPETNILG---QLGQGYKYAIGMLNRGRiGIAAQMLGLAQG--CFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVAT-- 396
Cdd:PRK13026 304 FIPLDWIIGgpdYAGRGWRMLVECLSAGR-GISLPALGTASGhmATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGnt 382
|
330 340 350
....*....|....*....|....*....|....*...
gi 1394717032 397 -QLEAARLLTynATRLAETGKPFIKEAsMAKYYAAEVA 433
Cdd:PRK13026 383 yLLEAARRLT--TTGLDLGVKPSVVTA-IAKYHMTELA 417
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
165-431 |
1.73e-18 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 88.72 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 165 EWGGTGSSFFSTILVVEELAKVDAAVALISELQNTL-INRLLIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFS 242
Cdd:PRK09463 131 EYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLgPGELLLHYGTDEQKDHYLPRLARgEEIPCFALTSPEAGSDAGS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 243 LK-----TRAEKKGDYYI---INGSKMWISSAEqagmfyvMANV--------DPS--LGYR---GITCFIVDRDTEGLCA 301
Cdd:PRK09463 211 IPdtgvvCKGEWQGEEVLgmrLTWNKRYITLAP-------IATVlglafklyDPDglLGDKedlGITCALIPTDTPGVEI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 302 GKKEDKLGLrASSTCPVTFENVKVPETNILG---QLGQGYKYAIGMLNRGR-IGIAAQMLGLAQGCFDQTLPYTKERVQF 377
Cdd:PRK09463 284 GRRHFPLNV-PFQNGPTRGKDVFIPLDYIIGgpkMAGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQF 362
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1394717032 378 GKSIFDFQGMQH---QIAQVATQLEAARLLTYNATRLAEtgKPFIKEAsMAKYYAAE 431
Cdd:PRK09463 363 KLPIGKFEGIEEplaRIAGNAYLMDAARTLTTAAVDLGE--KPSVLSA-IAKYHLTE 416
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
231-474 |
3.31e-15 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 77.87 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 231 LSEAGSGSDAFSLKTRAEK-KGDYYIINGSKmWISSAEQAGMFYVMANVDpslgyRGITCFIVDR-----DTEGLCAGKK 304
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAK-----GGLSCFFVPRflpdgQRNAIRLERL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 305 EDKLGLRASSTCPVTFENVKvpeTNILGQLGQGYKYAIGMLNRGRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDF 384
Cdd:PRK11561 258 KDKLGNRSNASSEVEFQDAI---GWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQ 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 385 QGMQHQIAQVATQLEA-----------------------ARLLTYNAT-RLAETGKPFIKEAsmakyyaaevatlttskc 440
Cdd:PRK11561 335 PLMRQVLSRMALQLEGqtallfrlarawdrradakealwARLFTPAAKfVICKRGIPFVAEA------------------ 396
|
250 260 270
....*....|....*....|....*....|....
gi 1394717032 441 IEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNI 474
Cdd:PRK11561 397 MEVLGGIGYCEESELPRLYREMPVNSIWEGSGNI 430
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
129-434 |
1.08e-13 |
|
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: 72.36 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 129 ERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVALIseLQNT--LINRLLI 206
Cdd:cd01163 8 ARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQA--LRAHfgFVEALLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 207 VHGTEKQKRTYLPRLAKDMVGSfCLSEAGSGSDAFSLkTRAEKKGDYYIINGSKMWISSAEQAGMFYVMAnVDPslgyRG 286
Cdd:cd01163 86 AGPEQFRKRWFGRVLNGWIFGN-AVSERGSVRPGTFL-TATVRDGGGYVLNGKKFYSTGALFSDWVTVSA-LDE----EG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 287 -ITCFIVDRDTEGLCAGKKEDKLGLR--ASSTcpVTFENVKVPETNILGQ----LGQGYKYAIGMLNrgrigIAAQMLGL 359
Cdd:cd01163 159 kLVFAAVPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLPRpnapDRGTLLTAIYQLV-----LAAVLAGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 360 AQGCFDQTLPYTKERVQ------FGKSIFDFQGMQHqIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYYAAEVA 433
Cdd:cd01163 232 ARAALDDAVAYVRSRTRpwihsgAESARDDPYVQQV-VGDLAARLHAAEALVLQAARALDAAAAAGTALTAEARGEAALA 310
|
.
gi 1394717032 434 T 434
Cdd:cd01163 311 V 311
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
129-461 |
8.39e-13 |
|
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: 69.69 E-value: 8.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 129 ERIAPFVKK----MDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVALISELQNTlINRL 204
Cdd:cd01159 4 EDLAPLIRErapeAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVAT-HSRM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 205 LIVHGTEKQKRTYlprlakdmvgsfclseaGSG-----SDAFSLKTRAEKKGDYYIINGSKMWISSAEQAGMFYVMANVD 279
Cdd:cd01159 83 LAAFPPEAQEEVW-----------------GDGpdtllAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 280 PSLGYRGITCFIVDR------DTEglcagkkeDKLGLRASSTCPVTFENVKVPETNIL-----------GQLGQGYKYAI 342
Cdd:cd01159 146 DDDGGPLPRAFVVPRaeyeivDTW--------HVVGLRGTGSNTVVVDDVFVPEHRTLtagdmmagdgpGGSTPVYRMPL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 343 GMLNRgrIGIAAQMLGLAQGCFDQTLPYTKERVQ---FGKSIFDFQGMQHQIAQVATQLEAARLLTYNATR----LAETG 415
Cdd:cd01159 218 RQVFP--LSFAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRdlwaHALAG 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1394717032 416 KPF-IKEASMAKYYAAEVATLTTS---KCIEWMGGAGFTKDYPVEKYYRD 461
Cdd:cd01159 296 GPIdVEERARIRRDAAYAAKLSAEavdRLFHAAGGSALYTASPLQRIWRD 345
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
209-481 |
1.38e-09 |
|
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: 60.42 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 209 GTEKQKRTYLP-RLAKDMVGSFCLSEAGSGSDAFSLKTRA--EKKGDYYIIN-----GSKMWISSAEQAGMF-YVMANVD 279
Cdd:cd01150 117 GTDEHQDYWLQgANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWWPGNLGKTATHaVVFAQLI 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 280 PSLGYRGITCFIV---DRDTE----GLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQ---------------- 336
Cdd:cd01150 197 TPGKNHGLHAFIVpirDPKTHqplpGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDvspdgtyvspfkdpnk 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 337 GYKYAIGMLNRGRIGIAaqMLGLAQGCFDQTLP--YTKERVQFGK-------SIFDFQGMQHQIaqvATQLEAARLLTYN 407
Cdd:cd01150 277 RYGAMLGTRSGGRVGLI--YDAAMSLKKAATIAirYSAVRRQFGPkpsdpevQILDYQLQQYRL---FPQLAAAYAFHFA 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 408 ATRLAETGKPFIKEASMA---------------KYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTS 472
Cdd:cd01150 352 AKSLVEMYHEIIKELLQGnsellaelhalsaglKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDN 431
|
....*....
gi 1394717032 473 NIQLSTIAK 481
Cdd:cd01150 432 TVLLQQTAN 440
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
179-487 |
2.33e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 59.87 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 179 VVEELAKVDAAVALISELQNTLINRLLIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRA--EKKGDYYI 255
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNlDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 256 IN-----GSKMWISSAEQAGMF-YVMANVD-PSLGYRGIT-----CFIVD-RDTE------GLCAGKKEDKLGLRASSTC 316
Cdd:PLN02636 206 INtpndgAIKWWIGNAAVHGKFaTVFARLKlPTHDSKGVSdmgvhAFIVPiRDMKthqvlpGVEIRDCGHKVGLNGVDNG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 317 PVTFENVKVPETNILGQLGQ-----GYKYAIGMLNR-----------GRIGIAAQMLGLAQGCFDQTLPYTKERVQFGK- 379
Cdd:PLN02636 286 ALRFRSVRIPRDNLLNRFGDvsrdgKYTSSLPTINKrfaatlgelvgGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPp 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 380 -----SIFDFQGMQHQIAQVATQLEAARLLT-YNATRLAETGKPFIKE--------ASMAKYYAAEVATLTTSKCIEWMG 445
Cdd:PLN02636 366 kqpeiSILDYQSQQHKLMPMLASTYAFHFATeYLVERYSEMKKTHDDQlvadvhalSAGLKAYITSYTAKALSTCREACG 445
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1394717032 446 GAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCIAQEY 487
Cdd:PLN02636 446 GHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQY 487
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
136-359 |
6.03e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 45.64 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 136 KKMDADgkiEESVLQGLFE---------LGLMGIDLGTEWGGTGSSFFSTILVVEEL-AKVDAavALISELQNT-LINRL 204
Cdd:PTZ00457 38 RKLDGD---EAENLQSLLEqirsndkilGNLYGARIATEYGGLGLGHTAHALIYEEVgTNCDS--KLLSTIQHSgFCTYL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717032 205 LIVHGTEKQKRTYLPRLAKDMVGSFCLSEAGSGSDAFSLKTRAEKKGD-YYIINGSKMWIsSAEQAGMFYVMAN-VDPSL 282
Cdd:PTZ00457 113 LSTVGSKELKGKYLTAMSDGTIMMGWATEEGCGSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKtLTQTA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394717032 283 GYRGITcfIVDRDTEGLCAgkkEDKLGLRASSTCpVTFENvkVPETNILGQLGQGYKYAIGMLNRGRIGIAAQMLGL 359
Cdd:PTZ00457 192 AEEGAT--EVSRNSFFICA---KDAKGVSVNGDS-VVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGI 260
|
|
| |
