|
Name |
Accession |
Description |
Interval |
E-value |
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
11-381 |
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: 584.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 11 EEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVALI 90
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 91 SELQNTLINRLLIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQAGMF 169
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATgEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 170 YVMANVDPSLGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNRGRIGI 249
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 250 AAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYYAAEV 329
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1394717047 330 ATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCIA 381
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLL 372
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
8-378 |
1.10e-163 |
|
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: 463.54 E-value: 1.10e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 8 TLTEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAV 87
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 88 ALIseLQNTLIN-RLLIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQ 165
Cdd:COG1960 84 ALP--VGVHNGAaEALLRFGTEEQKERYLPRLASgEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 166 AGMFYVMANVDPSLGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNRG 245
Cdd:COG1960 162 ADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 246 RIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYY 325
Cdd:COG1960 242 RLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLF 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1394717047 326 AAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 378
Cdd:COG1960 322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIAR 374
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
9-378 |
2.93e-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: 335.15 E-value: 2.93e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 9 LTEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVA 88
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 89 L-ISELQNTLINRLlIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQA 166
Cdd:cd01156 82 LsYGAHSNLCINQI-YRNGSAAQKEKYLPKLISgEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 167 GMFYVMANVDPSLGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNRGR 246
Cdd:cd01156 161 DTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 247 IGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYYA 326
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1394717047 327 AEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 378
Cdd:cd01156 321 AEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGR 372
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
11-378 |
3.04e-111 |
|
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: 328.47 E-value: 3.04e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 11 EEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGidlgtewggtgssffstilvveelakvdaavali 90
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLGAA---------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 91 selqntlinrLLIVHGTEKQKRTYLPRLAKD-MVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQAGMF 169
Cdd:cd00567 47 ----------LLLAYGTEEQKERYLPPLASGeAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 170 YVMANVDPS-LGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNRGRIG 248
Cdd:cd00567 117 IVLARTDEEgPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 249 IAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFI-KEASMAKYYAA 327
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEArLEAAMAKLFAT 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1394717047 328 EVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 378
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
9-383 |
4.52e-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: 303.98 E-value: 4.52e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 9 LTEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVA 88
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 89 LISELQNT---LINRLlivhGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAE 164
Cdd:cd01162 81 AYISIHNMcawMIDSF----GNDEQRERFLPDLCTmEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 165 QAGMFYVMANVDPSlGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNR 244
Cdd:cd01162 157 DSDVYVVMARTGGE-GPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 245 GRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKP-FIKEASMAK 323
Cdd:cd01162 236 GRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPdAVKLCAMAK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 324 YYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCIAQE 383
Cdd:cd01162 316 RFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
9-384 |
1.03e-98 |
|
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: 299.38 E-value: 1.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 9 LTEEEQLLKETVKKFAQERIAPfvKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAkVDAAVA 88
Cdd:cd01161 27 QTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVG-MDLGFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 89 LISELQNTLINRLLIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKK--GDYYIINGSKMWISSAEQ 165
Cdd:cd01161 104 VTLGAHQSIGFKGILLFGTEAQKEKYLPKLASgEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWITNGGI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 166 AGMFYVMAN---VDPSLGYR-GITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGM 241
Cdd:cd01161 184 ADIFTVFAKtevKDATGSVKdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 242 LNRGRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETG--KPFIKEA 319
Cdd:cd01161 264 LNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGlkAEYQIEA 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394717047 320 SMAKYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCIAQEY 384
Cdd:cd01161 344 AISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHA 408
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
9-378 |
4.30e-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: 291.41 E-value: 4.30e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 9 LTEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVA 88
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 89 LISElQNTLINRLLIVHGTEKQKRTYLPRLAKD-MVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQAG 167
Cdd:cd01157 81 TAIE-ANSLGQMPVIISGNDEQKKKYLGRMTEEpLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 168 MFYVMANVDP---SLGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNR 244
Cdd:cd01157 160 WYFLLARSDPdpkCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 245 GRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKY 324
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1394717047 325 YAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 378
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISR 373
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
11-380 |
9.66e-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: 287.86 E-value: 9.66e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 11 EEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVALI 90
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 91 SeLQNTLINRLLIVHGTEKQKRTYLPRL-AKDMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQAGMF 169
Cdd:cd01160 81 S-LHTDIVSPYITRAGSPEQKERVLPQMvAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 170 YVMANVD-PSLGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNRGRIG 248
Cdd:cd01160 160 IVVARTGgEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 249 IAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYYAAE 328
Cdd:cd01160 240 IAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1394717047 329 VATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCI 380
Cdd:cd01160 320 LQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
9-383 |
3.11e-84 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 262.12 E-value: 3.11e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 9 LTEEEQL-LKETVKKFAQERIAPFVKKMDADGKIEESV----LQGLFelGLMGIDLGTEWGGTGSSFFSTILVVEELAKV 83
Cdd:PLN02519 25 LFDDTQLqFKESVQQFAQENIAPHAAAIDATNSFPKDVnlwkLMGDF--NLHGITAPEEYGGLGLGYLYHCIAMEEISRA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 84 DAAVALISELQNTLINRLLIVHGTEKQKRTYLPRL-AKDMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISS 162
Cdd:PLN02519 103 SGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLiSGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 163 AEQAGMFYVMANVDPSLGYRGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGML 242
Cdd:PLN02519 183 GPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 243 NRGRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMA 322
Cdd:PLN02519 263 DLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGV 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394717047 323 KYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCIAQE 383
Cdd:PLN02519 343 ILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
9-371 |
3.26e-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: 243.42 E-value: 3.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 9 LTEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLgTEWGGTGSSFFSTILVVEELAKVDAAVA 88
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATI-KGYGCAGLSSVAYGLIAREVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 89 LISELQNTLINRLLIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQAG 167
Cdd:cd01151 92 SFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASgELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 168 MFYVMANVDPSLGYRGitcFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLgQGYKYAIGMLNRGRI 247
Cdd:cd01151 172 VFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNARY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 248 GIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYYAA 327
Cdd:cd01151 248 GIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNC 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1394717047 328 EVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNI 371
Cdd:cd01151 328 GKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDI 371
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
10-378 |
2.05e-70 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 226.36 E-value: 2.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 10 TEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVAL 89
Cdd:PTZ00461 38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 90 ISELQNTLINRLLIVHGTEKQKRTYLPR-LAKDMVGSFCLSEAGSGSDAFSLKTRAEKKGD-YYIINGSKMWISSAEQAG 167
Cdd:PTZ00461 118 AYLAHSMLFVNNFYYSASPAQRARWLPKvLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVAD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 168 MFYVMANVDPSlgyrgITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNRGRI 247
Cdd:PTZ00461 198 VFLIYAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 248 GIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYYAA 327
Cdd:PTZ00461 273 TLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFAT 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1394717047 328 EVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 378
Cdd:PTZ00461 353 PIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITK 403
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
18-372 |
1.45e-66 |
|
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: 216.49 E-value: 1.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 18 ETVKKFAQERIAPFVKKMDADG------------KIEESVlQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDA 85
Cdd:cd01153 3 EEVARLAENVLAPLNADGDREGpvfddgrvvvppPFKEAL-DAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 86 AVALISELQNTLinRLLIVHGTEKQKRTYLPRLA-KDMVGSFCLSEAGSGSDAFSLKTRAEKKGD-YYIINGSKMWISSA 163
Cdd:cd01153 82 PLMYASGTQGAA--ATLLAHGTEAQREKWIPRLAeGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 164 EQAG----MFYVMANV-DPSLGYRGITCFIV-----DRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPetnILGQLGQ 233
Cdd:cd01153 160 EHDMseniVHLVLARSeGAPPGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 234 GYKYAIGMLNRGRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQG---MQHQIA--QVATQ---LEAARLLT-YN 304
Cdd:cd01153 237 GLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAvtiIHHPDVrrSLMTQkayAEGSRALDlYT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 305 AT-----RLAETGKPFIKEAS--------MAKYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNI 371
Cdd:cd01153 317 ATvqdlaERKATEGEDRKALSaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
|
.
gi 1394717047 372 Q 372
Cdd:cd01153 397 Q 397
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
9-384 |
1.46e-57 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 192.25 E-value: 1.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 9 LTEEEQLLKETVKKF-AQERIAPFVKKMDADGKIEESVLQGLFE--LGLMGIDlgTEWGGTGSSFFSTILVVEELAKVDA 85
Cdd:PRK12341 5 LTEEQELLLASIRELiTRNFPEEYFRTCDENGTYPREFMRALADngISMLGVP--EEFGGTPADYVTQMLVLEEVSKCGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 86 AVALISELQNtlINRLLiVHGTEKQKRTYLPRLAKDMVGSFCL--SEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSA 163
Cdd:PRK12341 83 PAFLITNGQC--IHSMR-RFGSAEQLRKTAESTLETGDPAYALalTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 164 EQAGMFYVMA-NVDPSLGYRGITCFIVDRDTEGLcagKKED--KLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIG 240
Cdd:PRK12341 160 KEYPYMLVLArDPQPKDPKKAFTLWWVDSSKPGI---KINPlhKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 241 MLNRGRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEAS 320
Cdd:PRK12341 237 NFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAA 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394717047 321 MAKYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCIAQEY 384
Cdd:PRK12341 317 LAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDY 380
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
232-378 |
1.50e-57 |
|
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: 184.38 E-value: 1.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 232 GQGYKYAIGMLNRGRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAET 311
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394717047 312 GKPFIKEASMAKYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 378
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
49-378 |
5.80e-52 |
|
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: 5.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 49 LFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVALISELQNTLINRLLiVHGTEKQKRTYLPRLA--KDMvgsF 126
Cdd:cd01152 44 LAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTIL-AYGTDEQKRRFLPPILsgEEI---W 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 127 CL--SEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQAGMFYVMANVDPSL-GYRGITCFIVDRDTEGLCAGKKED 203
Cdd:cd01152 120 CQgfSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEApKHRGISILLVDMDSPGVTVRPIRS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 204 KLGlrASSTCPVTFENVKVPETNILGQLGQGYKYAIGMLNRGRigiaAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQG 283
Cdd:cd01152 200 ING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFER----VSIGGSAATFFELLLARLLLLTRDGRPLIDDPL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 284 MQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYYAAEVATLTTSKCIEWMGGAGFTKDYP--------VEKY 355
Cdd:cd01152 274 VRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWEAD 353
|
330 340
....*....|....*....|...
gi 1394717047 356 YRDCKIGTIYEGTSNIQLSTIAK 378
Cdd:cd01152 354 YLRSRATTIYGGTSEIQRNIIAE 376
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
9-371 |
1.55e-48 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 169.26 E-value: 1.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 9 LTEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGidlGT--EWGGTGSSFFSTILVVEELAKVDAA 86
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAG---GTikGYGCPGLSITASAIATAEVARVDAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 87 VALISELQNTLINRLLIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWISSAEQ 165
Cdd:PLN02526 106 CSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQlDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 166 AGMFYVMA-NVDPSlgyrGITCFIVDRDTEGLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLgQGYKYAIGMLNR 244
Cdd:PLN02526 186 ADVLVIFArNTTTN----QINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 245 GRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKY 324
Cdd:PLN02526 261 SRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKA 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1394717047 325 YAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNI 371
Cdd:PLN02526 341 WITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDI 387
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
8-384 |
2.68e-45 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 160.00 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 8 TLTEEEQLLKETVKKF-AQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAA 86
Cdd:PRK03354 4 NLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 87 VALISELQ---NTLINrllivHGTEKQKRTYLPRLA--KDMVGSFClSEAGSGSDAFSLKTRAEKKGDYYIINGSKMWIS 161
Cdd:PRK03354 84 TYVLYQLPggfNTFLR-----EGTQEQIDKIMAFRGtgKQMWNSAI-TEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 162 SAEQAGMFYVMANVDPSLGYRGITCFIVDRDTEGLCAGKKEdKLGLRASSTCPVTFENVKVPETNILGQLGQGYKYAIGM 241
Cdd:PRK03354 158 SSAYTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 242 LNRGRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFIKEASM 321
Cdd:PRK03354 237 FDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAM 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394717047 322 AKYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCIAQEY 384
Cdd:PRK03354 317 CKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQY 379
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
112-372 |
5.75e-45 |
|
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: 159.84 E-value: 5.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 112 RTYLPRLA-----KDMVGSFCLSEAGSGSDAFSLKTRAEK-KGDYYIINGSKmWISSAEQAGMFYVMAN-VDPSLGYRGI 184
Cdd:cd01154 132 KQYLPGLLsdrykTGLLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLARpEGAPAGARGL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 185 TCFIVDRDTEGlcaGKK--------EDKLGLRASSTCPVTFENVkvpETNILGQLGQGYKYAIGMLNRGRIGIAAQMLGL 256
Cdd:cd01154 211 SLFLVPRLLED---GTRngyrirrlKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAVAALGI 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 257 AQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRL---AETGKPfiKEASMA-------KYYA 326
Cdd:cd01154 285 MRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAfdrAAADKP--VEAHMArlatpvaKLIA 362
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1394717047 327 AEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQ 372
Cdd:cd01154 363 CKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
102-378 |
1.04e-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: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 102 LIVHGTEKQKRTYL-PRLAKDMVGSFCLSEAG-SGSDAFSLKTRAEKKGDYYIINGSKMWISSA--EQAGMFYVMANVDP 177
Cdd:cd01155 104 LHRYGSEEQKKQWLePLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAgdPRCKIAIVMGRTDP 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 178 SLG--YRGITCFIVDRDTEGLcagKKEDKLGLRASSTCP-----VTFENVKVPETNILGQLGQGYKYAIGMLNRGRIGIA 250
Cdd:cd01155 184 DGAprHRQQSMILVPMDTPGV---TIIRPLSVFGYDDAPhghaeITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHC 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 251 AQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNATRLAETGKPFI--KEASMAKYYAAE 328
Cdd:cd01155 261 MRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAarKEIAMIKVAAPR 340
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1394717047 329 VATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 378
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 ... |
10-120 |
1.56e-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: 128.73 E-value: 1.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 10 TEEEQLLKETVKKFAQERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVAL 89
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|.
gi 1394717047 90 ISELQNTLINRLLIVHGTEKQKRTYLPRLAK 120
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
13-372 |
4.55e-33 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 130.37 E-value: 4.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 13 EQLLKETvKKFAQERIAPFVKKMDADG------------KIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEEL 80
Cdd:PTZ00456 61 DSLLEEA-SKLATQTLLPLYESSDSEGcvllkdgnvttpKGFKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELM 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 81 AKVDAAVALISELQNTLINRLLiVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRAEKKGD-YYIINGSKM 158
Cdd:PTZ00456 140 ATANWGFSMYPGLSIGAANTLM-AWGSEEQKEQYLTKLVSgEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 159 WISSAEQ---AGMFY-VMANVDPSL-GYRGITCFIVDR---DTEGLCAGKK-------EDKLGLRASSTCPVTFENVKvp 223
Cdd:PTZ00456 219 FISAGDHdltENIVHiVLARLPNSLpTTKGLSLFLVPRhvvKPDGSLETAKnvkciglEKKMGIKGSSTCQLSFENSV-- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 224 eTNILGQLGQGYKYAIGMLNRGRIGIAAQMLGLAQGCFDQTLPYTKERVQF------------GKSIFDFQGMQHQIAQV 291
Cdd:PTZ00456 297 -GYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNILFA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 292 ATQLEAARLLTYNATRL----AETGKPFIKEA---------SMAKYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRD 358
Cdd:PTZ00456 376 KAVAEGGRALLLDVGRLldihAAAKDAATREAldheigfytPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRD 455
|
410
....*....|....
gi 1394717047 359 CKIGTIYEGTSNIQ 372
Cdd:PTZ00456 456 ARIGTLYEGTTGIQ 469
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
125-218 |
3.05e-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: 103.51 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 125 SFCLSEAGSGSDAFSLKTRA-EKKGDYYIINGSKMWISSAEQAGMFYVMANVDPSLGYRGITCFIVDRDTEGLCAGKKED 203
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 1394717047 204 KLGLRASSTCPVTFE 218
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
248-369 |
4.60e-24 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 96.26 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 248 GIAAQMLGLAQGCFDQTLPYTKERVQ--FGKSIFDFQGMQHQIAQVATQLEAARLLTYNAT----RLAETGKPF----IK 317
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVtpalRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1394717047 318 EASMAKYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTS 369
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
101-378 |
1.53e-22 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 99.48 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 101 LLIVHGTEKQKRTYL-PRLAKDMVGSFCLSEAG-SGSDAFSLKTRAEKKGDYYIINGSKMWISSA--EQAGMFYVMANVD 176
Cdd:PLN02876 528 VLLRYGNKEQQLEWLiPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTD 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 177 PSLG-YRGITCFIVDRDTEGLcagKKEDKLGLRASSTCP-----VTFENVKVPETNILGQLGQGYKYAIGMLNRGRIGIA 250
Cdd:PLN02876 608 FNAPkHKQQSMILVDIQTPGV---QIKRPLLVFGFDDAPhghaeISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHC 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 251 AQMLGLAQGCFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVATQLEAARLLTYNAT-RLAETGKPFIKEA-SMAKYYAAE 328
Cdd:PLN02876 685 MRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAAdQLDRLGNKKARGIiAMAKVAAPN 764
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1394717047 329 VATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAK 378
Cdd:PLN02876 765 MALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAK 814
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
5-330 |
2.04e-21 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 96.18 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 5 PLQTLTEEEQllketvkKFAQERIAPFVKKMD------ADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVE 78
Cdd:PRK13026 74 PKPTLTAEEQ-------AFIDNEVETLLTMLDdwdivqNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 79 ELA--KVDAAVALIseLQNTLINRLLIVH-GTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLK-----TRAEKKGD 149
Cdd:PRK13026 147 KIAtrSVSAAVTVM--VPNSLGPGELLTHyGTQEQKDYWLPRLADgTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 150 YYI---INGSKMWISSAEQA---GMFYVMANVDPSLGYR---GITCFIVDRDTEGLCAGKKEDKLGLrASSTCPVTFENV 220
Cdd:PRK13026 225 EVLglrLTWDKRYITLAPVAtvlGLAFKLRDPDGLLGDKkelGITCALIPTDHPGVEIGRRHNPLGM-AFMNGTTRGKDV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 221 KVPETNILG---QLGQGYKYAIGMLNRGRiGIAAQMLGLAQG--CFDQTLPYTKERVQFGKSIFDFQGMQHQIAQVAT-- 293
Cdd:PRK13026 304 FIPLDWIIGgpdYAGRGWRMLVECLSAGR-GISLPALGTASGhmATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGnt 382
|
330 340 350
....*....|....*....|....*....|....*...
gi 1394717047 294 -QLEAARLLTynATRLAETGKPFIKEAsMAKYYAAEVA 330
Cdd:PRK13026 383 yLLEAARRLT--TTGLDLGVKPSVVTA-IAKYHMTELA 417
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
62-328 |
1.48e-18 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 87.56 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 62 EWGGTGSSFFSTILVVEELAKVDAAVALISELQNTL-INRLLIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFS 139
Cdd:PRK09463 131 EYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLgPGELLLHYGTDEQKDHYLPRLARgEEIPCFALTSPEAGSDAGS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 140 LK-----TRAEKKGDYYI---INGSKMWISSAEqagmfyvMANV--------DPS--LGYR---GITCFIVDRDTEGLCA 198
Cdd:PRK09463 211 IPdtgvvCKGEWQGEEVLgmrLTWNKRYITLAP-------IATVlglafklyDPDglLGDKedlGITCALIPTDTPGVEI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 199 GKKEDKLGLrASSTCPVTFENVKVPETNILG---QLGQGYKYAIGMLNRGR-IGIAAQMLGLAQGCFDQTLPYTKERVQF 274
Cdd:PRK09463 284 GRRHFPLNV-PFQNGPTRGKDVFIPLDYIIGgpkMAGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQF 362
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1394717047 275 GKSIFDFQGMQH---QIAQVATQLEAARLLTYNATRLAEtgKPFIKEAsMAKYYAAE 328
Cdd:PRK09463 363 KLPIGKFEGIEEplaRIAGNAYLMDAARTLTTAAVDLGE--KPSVLSA-IAKYHLTE 416
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
128-371 |
1.40e-15 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 78.25 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 128 LSEAGSGSDAFSLKTRAEK-KGDYYIINGSKmWISSAEQAGMFYVMANVDpslgyRGITCFIVDR-----DTEGLCAGKK 201
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAK-----GGLSCFFVPRflpdgQRNAIRLERL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 202 EDKLGLRASSTCPVTFENVKvpeTNILGQLGQGYKYAIGMLNRGRIGIAAQMLGLAQGCFDQTLPYTKERVQFGKSIFDF 281
Cdd:PRK11561 258 KDKLGNRSNASSEVEFQDAI---GWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQ 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 282 QGMQHQIAQVATQLEA-----------------------ARLLTYNAT-RLAETGKPFIKEAsmakyyaaevatlttskc 337
Cdd:PRK11561 335 PLMRQVLSRMALQLEGqtallfrlarawdrradakealwARLFTPAAKfVICKRGIPFVAEA------------------ 396
|
250 260 270
....*....|....*....|....*....|....
gi 1394717047 338 IEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTSNI 371
Cdd:PRK11561 397 MEVLGGIGYCEESELPRLYREMPVNSIWEGSGNI 430
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
26-331 |
6.07e-14 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 72.36 E-value: 6.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 26 ERIAPFVKKMDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVALIseLQNT--LINRLLI 103
Cdd:cd01163 8 ARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQA--LRAHfgFVEALLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 104 VHGTEKQKRTYLPRLAKDMVGSfCLSEAGSGSDAFSLkTRAEKKGDYYIINGSKMWISSAEQAGMFYVMAnVDPslgyRG 183
Cdd:cd01163 86 AGPEQFRKRWFGRVLNGWIFGN-AVSERGSVRPGTFL-TATVRDGGGYVLNGKKFYSTGALFSDWVTVSA-LDE----EG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 184 -ITCFIVDRDTEGLCAGKKEDKLGLR--ASSTcpVTFENVKVPETNILGQ----LGQGYKYAIGMLNrgrigIAAQMLGL 256
Cdd:cd01163 159 kLVFAAVPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLPRpnapDRGTLLTAIYQLV-----LAAVLAGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 257 AQGCFDQTLPYTKERVQ------FGKSIFDFQGMQHqIAQVATQLEAARLLTYNATRLAETGKPFIKEASMAKYYAAEVA 330
Cdd:cd01163 232 ARAALDDAVAYVRSRTRpwihsgAESARDDPYVQQV-VGDLAARLHAAEALVLQAARALDAAAAAGTALTAEARGEAALA 310
|
.
gi 1394717047 331 T 331
Cdd:cd01163 311 V 311
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
26-358 |
4.90e-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: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 26 ERIAPFVKK----MDADGKIEESVLQGLFELGLMGIDLGTEWGGTGSSFFSTILVVEELAKVDAAVALISELQNTlINRL 101
Cdd:cd01159 4 EDLAPLIRErapeAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVAT-HSRM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 102 LIVHGTEKQKRTYlprlakdmvgsfclseaGSG-----SDAFSLKTRAEKKGDYYIINGSKMWISSAEQAGMFYVMANVD 176
Cdd:cd01159 83 LAAFPPEAQEEVW-----------------GDGpdtllAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 177 PSLGYRGITCFIVDR------DTEglcagkkeDKLGLRASSTCPVTFENVKVPETNIL-----------GQLGQGYKYAI 239
Cdd:cd01159 146 DDDGGPLPRAFVVPRaeyeivDTW--------HVVGLRGTGSNTVVVDDVFVPEHRTLtagdmmagdgpGGSTPVYRMPL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 240 GMLNRgrIGIAAQMLGLAQGCFDQTLPYTKERVQ---FGKSIFDFQGMQHQIAQVATQLEAARLLTYNATR----LAETG 312
Cdd:cd01159 218 RQVFP--LSFAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRdlwaHALAG 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1394717047 313 KPF-IKEASMAKYYAAEVATLTTS---KCIEWMGGAGFTKDYPVEKYYRD 358
Cdd:cd01159 296 GPIdVEERARIRRDAAYAAKLSAEavdRLFHAAGGSALYTASPLQRIWRD 345
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
106-378 |
9.32e-10 |
|
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: 60.04 E-value: 9.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 106 GTEKQKRTYLP-RLAKDMVGSFCLSEAGSGSDAFSLKTRA--EKKGDYYIIN-----GSKMWISSAEQAGMF-YVMANVD 176
Cdd:cd01150 117 GTDEHQDYWLQgANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWWPGNLGKTATHaVVFAQLI 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 177 PSLGYRGITCFIV---DRDTE----GLCAGKKEDKLGLRASSTCPVTFENVKVPETNILGQLGQ---------------- 233
Cdd:cd01150 197 TPGKNHGLHAFIVpirDPKTHqplpGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDvspdgtyvspfkdpnk 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 234 GYKYAIGMLNRGRIGIAaqMLGLAQGCFDQTLP--YTKERVQFGK-------SIFDFQGMQHQIaqvATQLEAARLLTYN 304
Cdd:cd01150 277 RYGAMLGTRSGGRVGLI--YDAAMSLKKAATIAirYSAVRRQFGPkpsdpevQILDYQLQQYRL---FPQLAAAYAFHFA 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 305 ATRLAETGKPFIKEASMA---------------KYYAAEVATLTTSKCIEWMGGAGFTKDYPVEKYYRDCKIGTIYEGTS 369
Cdd:cd01150 352 AKSLVEMYHEIIKELLQGnsellaelhalsaglKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDN 431
|
....*....
gi 1394717047 370 NIQLSTIAK 378
Cdd:cd01150 432 TVLLQQTAN 440
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
76-384 |
1.24e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 59.87 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 76 VVEELAKVDAAVALISELQNTLINRLLIVHGTEKQKRTYLPRLAK-DMVGSFCLSEAGSGSDAFSLKTRA--EKKGDYYI 152
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNlDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 153 IN-----GSKMWISSAEQAGMF-YVMANVD-PSLGYRGIT-----CFIVD-RDTE------GLCAGKKEDKLGLRASSTC 213
Cdd:PLN02636 206 INtpndgAIKWWIGNAAVHGKFaTVFARLKlPTHDSKGVSdmgvhAFIVPiRDMKthqvlpGVEIRDCGHKVGLNGVDNG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 214 PVTFENVKVPETNILGQLGQ-----GYKYAIGMLNR-----------GRIGIAAQMLGLAQGCFDQTLPYTKERVQFGK- 276
Cdd:PLN02636 286 ALRFRSVRIPRDNLLNRFGDvsrdgKYTSSLPTINKrfaatlgelvgGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPp 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 277 -----SIFDFQGMQHQIAQVATQLEAARLLT-YNATRLAETGKPFIKE--------ASMAKYYAAEVATLTTSKCIEWMG 342
Cdd:PLN02636 366 kqpeiSILDYQSQQHKLMPMLASTYAFHFATeYLVERYSEMKKTHDDQlvadvhalSAGLKAYITSYTAKALSTCREACG 445
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1394717047 343 GAGFTKDYPVEKYYRDCKIGTIYEGTSNIQLSTIAKCIAQEY 384
Cdd:PLN02636 446 GHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQY 487
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
33-256 |
1.03e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 44.10 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 33 KKMDADgkiEESVLQGLFE---------LGLMGIDLGTEWGGTGSSFFSTILVVEEL-AKVDAavALISELQNT-LINRL 101
Cdd:PTZ00457 38 RKLDGD---EAENLQSLLEqirsndkilGNLYGARIATEYGGLGLGHTAHALIYEEVgTNCDS--KLLSTIQHSgFCTYL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394717047 102 LIVHGTEKQKRTYLPRLAKDMVGSFCLSEAGSGSDAFSLKTRAEKKGD-YYIINGSKMWIsSAEQAGMFYVMAN-VDPSL 179
Cdd:PTZ00457 113 LSTVGSKELKGKYLTAMSDGTIMMGWATEEGCGSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKtLTQTA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394717047 180 GYRGITcfIVDRDTEGLCAgkkEDKLGLRASSTCpVTFENvkVPETNILGQLGQGYKYAIGMLNRGRIGIAAQMLGL 256
Cdd:PTZ00457 192 AEEGAT--EVSRNSFFICA---KDAKGVSVNGDS-VVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGI 260
|
|
| |
