|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-381 |
0e+00 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 785.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 1 MDFSLTEEQELLLASIRELITTNFPEEYFRTCDQNGTYPREFMRALADNGISMLGVPEEFGGIPADYVTQMLALMEVSKC 80
Cdd:PRK12341 1 MDFSLTEEQELLLASIRELITRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 81 GAPAFLITNGQCIHSMRRFGSAEQLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYINGQKTFITGAK 160
Cdd:PRK12341 81 GAPAFLITNGQCIHSMRRFGSAEQLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 161 EYPYMLVLARDPQPKDPKKAFTLWWVDSSKPGIKINPLHKIGWHMLSTCEVYLDNVEVEESDMVGEEGMGFLNVMYNFEM 240
Cdd:PRK12341 161 EYPYMLVLARDPQPKDPKKAFTLWWVDSSKPGIKINPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 241 ERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQSLRTSAALAKL 320
Cdd:PRK12341 241 ERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAKL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38704005 321 YCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYVAGRQILKDYQ 381
Cdd:PRK12341 321 YCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDYQ 381
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
1-381 |
7.97e-157 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 446.20 E-value: 7.97e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 1 MDFSLTEEQELLLASIRELITTNFPEEYFRTCDQNGTYPREFMRALADNGISMLGVPEEFGGIPADYVTQMLALMEVSKC 80
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELMASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 81 GAPAFLITN-GQCIHSMRRFGSAEQLRKTAeSTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYINGQKTFITGA 159
Cdd:PRK03354 81 GAPTYVLYQlPGGFNTFLREGTQEQIDKIM-AFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 160 KEYPYMLVLARDPQPKDpKKAFTLWWVDSSKPGIKINPLHKIGWHMLSTCEVYLDNVEVEESDMVGEEGMGFLNVMYNFE 239
Cdd:PRK03354 160 AYTPYIVVMARDGASPD-KPVYTEWFVDMSKPGIKVTKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 240 MERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQSLRTSAALAK 319
Cdd:PRK03354 239 HERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCK 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38704005 320 LYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYVAGRQILKDYQ 381
Cdd:PRK03354 319 YFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-380 |
1.25e-127 |
|
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: 371.87 E-value: 1.25e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 1 MDFSLTEEQELLLASIRELITTNFPEeYFRTCDQNGTYPREFMRALADNGISMLGVPEEFGGIPADYVTQMLALMEVSKC 80
Cdd:COG1960 1 MDFELTEEQRALRDEVREFAEEEIAP-EAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 81 GAP---AFLITNGqCIHSMRRFGSAEQ----LRKTAestleTGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYINGQK 153
Cdd:COG1960 80 DASlalPVGVHNG-AAEALLRFGTEEQkeryLPRLA-----SGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 154 TFITGAKEYPYMLVLARDPqPKDPKKAFTLWWVDSSKPGIKINP-LHKIGWHMLSTCEVYLDNVEVEESDMVGEEGMGFL 232
Cdd:COG1960 154 TFITNAPVADVILVLARTD-PAAGHRGISLFLVPKDTPGVTVGRiEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 233 NVMYNFEMERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQSLR 312
Cdd:COG1960 233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAA 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38704005 313 TSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYVAGRQILKDY 380
Cdd:COG1960 313 LEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRP 380
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
7-374 |
4.37e-100 |
|
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: 299.97 E-value: 4.37e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 7 EEQELLLASIRELITtNFPEEYFRTCDQNGTYPREFMRALADNGISMLgvpeefggipadyvtqmlalmevskcgapafl 86
Cdd:cd00567 1 EEQRELRDSAREFAA-EELEPYARERRETPEEPWELLAELGLLLGAAL-------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 87 itngqcihsMRRFGSAEQLRKTAEStLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYINGQKTFITGAKEYPYML 166
Cdd:cd00567 48 ---------LLAYGTEEQKERYLPP-LASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 167 VLARDPQPKDPKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDMVGEEGMGFLNVMYNFEMERLIN 245
Cdd:cd00567 118 VLARTDEEGPGHRGISAFLVPADTPGVTVGRIWdKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 246 AARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQS-LRTSAALAKLYCAR 324
Cdd:cd00567 198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKLFATE 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 38704005 325 TAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYVAGR 374
Cdd:cd00567 278 AAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
7-378 |
1.73e-89 |
|
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: 274.15 E-value: 1.73e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 7 EEQELLLASIRElittnFPEEYF----RTCDQNGTYPREFMRALADNGISMLGVPEEFGGIPADYVTQMLALMEVSKCGA 82
Cdd:cd01158 1 EEHQMIRKTVRD-----FAEKEIaplaAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 83 PAFLI---TNGQCIHSMRRFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYINGQKTFITGA 159
Cdd:cd01158 76 SVAVIvsvHNSLGANPIIKFGTEEQ-KKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 160 KEYPYMLVLAR-DPQPKdpKKAFTLWWVDSSKPGIKIN-PLHKIGWHMLSTCEVYLDNVEVEESDMVGEEGMGFLNVMYN 237
Cdd:cd01158 155 GEADFYIVFAVtDPSKG--YRGITAFIVERDTPGLSVGkKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 238 FEMERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQSLRTSAAL 317
Cdd:cd01158 233 LDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAM 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38704005 318 AKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYVAGRQILK 378
Cdd:cd01158 313 AKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
7-377 |
6.16e-79 |
|
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: 247.41 E-value: 6.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 7 EEQELLLASIRELittnFPEE---YFRTCDQNGTYPREFMRALADNGISMLGVPEEFGGIPADYVTQMLALMEV--SKCG 81
Cdd:cd01160 1 EEHDAFRDVVRRF----FAKEvapFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELarAGGS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 82 APAFLITNGQCIHSMRRFGSAEQLRKTAESTLeTGDPAYALALTEPGAGSDNNSATTTyTRKNGKVYI-NGQKTFITGAK 160
Cdd:cd01160 77 GPGLSLHTDIVSPYITRAGSPEQKERVLPQMV-AGKKIGAIAMTEPGAGSDLQGIRTT-ARKDGDHYVlNGSKTFITNGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 161 EYPYMLVLARDPQPKDPKKAFTLWWVDSSKPG-IKINPLHKIGWHMLSTCEVYLDNVEVEESDMVGEEGMGFLNVMYNFE 239
Cdd:cd01160 155 LADVVIVVARTGGEARGAGGISLFLVERGTPGfSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 240 MERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQSLRTSAALAK 319
Cdd:cd01160 235 QERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAK 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 38704005 320 LYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYVAGRQIL 377
Cdd:cd01160 315 YWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
5-378 |
1.57e-74 |
|
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: 236.15 E-value: 1.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 5 LTEEQELLLASIRELITTNFpEEYFRTCDQNGTYPREFMRALADNGISMLGVPEEFGGIPADYVTQMLALMEVSKcGAPA 84
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEI-APLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISR-ASGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 85 FLITNGQ----CIHSMRRFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYINGQKTFITGAK 160
Cdd:cd01156 80 VALSYGAhsnlCINQIYRNGSAAQ-KEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 161 EYPYMLVLARDpQPKDPKKAFTLWWVDSSKPGIKINP-LHKIGWHMLSTCEVYLDNVEVEESDMVGEEGMGFLNVMYNFE 239
Cdd:cd01156 159 DADTLVVYAKT-DPSAGAHGITAFIVEKGMPGFSRAQkLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 240 MERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQSLRTSAALAK 319
Cdd:cd01156 238 YERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVI 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 38704005 320 LYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYVAGRQILK 378
Cdd:cd01156 318 LYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
33-377 |
1.50e-54 |
|
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: 184.18 E-value: 1.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 33 DQNGTYPREFMRALADNGISMLGVPEEFGG-----IPADYVTQMLALMEVSkcgAPAFLITNGQCIHSMRRFGSAEQlRK 107
Cdd:cd01162 28 DQKKHFPVDVLRKAAELGFGGIYIRDDVGGsglsrLDASIIFEALSTGCVS---TAAYISIHNMCAWMIDSFGNDEQ-RE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 108 TAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYINGQKTFITGAKEYPYMLVLARdpQPKDPKKAFTLWWVD 187
Cdd:cd01162 104 RFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVVMAR--TGGEGPKGISCFVVE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 188 SSKPGIKIN-PLHKIGWHMLSTCEVYLDNVEVEESDMVGEEGMGFLNVMYNFEMERLINAARSTGFAECAFEDAARYANQ 266
Cdd:cd01162 182 KGTPGLSFGaNEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 267 RIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQSLRTS-AALAKLYCARTAMEVIDDAIQIMGGLGYTDE 345
Cdd:cd01162 262 RKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKlCAMAKRFATDECFDVANQALQLHGGYGYLKD 341
|
330 340 350
....*....|....*....|....*....|..
gi 38704005 346 ARVSRFWRDVRCERIGGGTDEIMIYVAGRQIL 377
Cdd:cd01162 342 YPVEQYVRDLRVHQILEGTNEIMRLIIARALL 373
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
1-380 |
3.14e-54 |
|
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: 184.21 E-value: 3.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 1 MDFSLTEEQELLLASIRELIT-TNFPeeyfRTCDQNGTYPREFMRALADNGISMLGVPEEFGGIPADYvTQMLALMEvsK 79
Cdd:cd01161 23 LTEEQTEELNMLVGPVEKFFEeVNDP----AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNN-TQYARLAE--I 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 80 CGAPA-FLITNGqcIHS------MRRFGSAEQLRKTAEStLETGDPAYALALTEPGAGSDNNSATTTYTRK-NGKVY-IN 150
Cdd:cd01161 96 VGMDLgFSVTLG--AHQsigfkgILLFGTEAQKEKYLPK-LASGEWIAAFALTEPSSGSDAASIRTTAVLSeDGKHYvLN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 151 GQKTFITGAKEYPYMLVLARDPQpKDP----KKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDMVG 225
Cdd:cd01161 173 GSKIWITNGGIADIFTVFAKTEV-KDAtgsvKDKITAFIVERSFGGVTNGPPEkKMGIKGSNTAEVYFEDVKIPVENVLG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 226 EEGMGFLNVMYNFEMERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQA 305
Cdd:cd01161 252 EVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNM 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38704005 306 DQHQSLRTS--AALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM-IYVAGrQILKDY 380
Cdd:cd01161 332 DRGLKAEYQieAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILrLFIAL-TGLQHA 408
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
26-366 |
3.10e-52 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 178.98 E-value: 3.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 26 EEYFRTCDQNGTYPREFMRALADNGISMLGVPEEFGGIPADYVTQMLALMEVSKCGaPAFLItnGQCIHSM---RRF--- 99
Cdd:PTZ00461 57 DKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYD-PGFCL--AYLAHSMlfvNNFyys 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 100 GSAEQLRKTAESTLeTGDPAYALALTEPGAGSDNNSATTTYTR-KNGKVYINGQKTFITGAKEYPYMLVLARdpqpKDPK 178
Cdd:PTZ00461 134 ASPAQRARWLPKVL-TGEHVGAMGMSEPGAGTDVLGMRTTAKKdSNGNYVLNGSKIWITNGTVADVFLIYAK----VDGK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 179 kaFTLWWVDSSKPGIKINP-LHKIGWHMLSTCEVYLDNVEVEESDMVGEEGMGFLNVMYNFEMERLINAARSTGFAECAF 257
Cdd:PTZ00461 209 --ITAFVVERGTKGFTQGPkIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 258 EDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQSLRTSAALAKLYCARTAMEVIDDAIQIM 337
Cdd:PTZ00461 287 ELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKKVADSAIQVM 366
|
330 340
....*....|....*....|....*....
gi 38704005 338 GGLGYTDEARVSRFWRDVRCERIGGGTDE 366
Cdd:PTZ00461 367 GGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
2-379 |
4.21e-51 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 175.84 E-value: 4.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 2 DFSLTEEQELLLASIRELITTNFPEeYFRTCDQNGTYPRE--FMRALADNGISMLGVPEEFGGIPADYVTQMLALMEVSK 79
Cdd:PLN02519 23 SLLFDDTQLQFKESVQQFAQENIAP-HAAAIDATNSFPKDvnLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 80 CGAPAFLITNGQ---CIHSMRRFGSAEQLRKTAeSTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYINGQKTFI 156
Cdd:PLN02519 102 ASGSVGLSYGAHsnlCINQLVRNGTPAQKEKYL-PKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWC 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 157 TGAKEYPYMLVLARDpQPKDPKKAFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDMVGEEGMGFLNVM 235
Cdd:PLN02519 181 TNGPVAQTLVVYAKT-DVAAGSKGITAFIIEKGMPGFSTaQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 236 YNFEMERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQSLRTSA 315
Cdd:PLN02519 260 SGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDC 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38704005 316 ALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYVAGRQILKD 379
Cdd:PLN02519 340 AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
7-377 |
1.21e-50 |
|
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: 173.93 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 7 EEQELLLASIRELITTNFPEEyfrtcDQNGTYPREFMRALADNGISMLGVPEEFGGIPADYVTQMLALMEVS-KC-GAPA 84
Cdd:cd01157 7 EFQETARKFAREEIIPVAAEY-----DKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAyGCtGVQT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 85 FLITNGQCIHSMRRFGSAEQLRKTAESTLEtgDPAY-ALALTEPGAGSDNNSATTTYTRKNGKVYINGQKTFITGAKEYP 163
Cdd:cd01157 82 AIEANSLGQMPVIISGNDEQKKKYLGRMTE--EPLMcAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 164 YMLVLAR-DPQPKDP-KKAFTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDMVGEEGMGFLNVMYNFEM 240
Cdd:cd01157 160 WYFLLARsDPDPKCPaSKAFTGFIVEADTPGIQPGRKELnMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 241 ERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQSLRTSAALAKL 320
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 38704005 321 YCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYVAGRQIL 377
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
228-376 |
5.49e-50 |
|
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: 165.12 E-value: 5.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 228 GMGFLNVMYNFEMERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQ 307
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38704005 308 HQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYVAGRQI 376
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
7-377 |
4.35e-47 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 164.83 E-value: 4.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 7 EEQELLLASIRELITTN----FPEEYFRTCDQNGTYPREFMRALADNGISMLGVPEEFGGIPADYVTQMLALMEVSKCGA 82
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHlppeLREESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 83 P--AFLITNGQCIHSMRRFGSAEQLRKTAESTLeTGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYINGQKTFITGAK 160
Cdd:cd01152 81 PvpFNQIGIDLAGPTILAYGTDEQKRRFLPPIL-SGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 161 EYPYMLVLARDPqPKDPK-KAFTLWWVDSSKPGIKINPLHKIGWHMlSTCEVYLDNVEVEESDMVGEEGMGFLNVMYNFE 239
Cdd:cd01152 160 YADWAWLLVRTD-PEAPKhRGISILLVDMDSPGVTVRPIRSINGGE-FFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 240 MERLINAarstGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQSLRTSAALAK 319
Cdd:cd01152 238 FERVSIG----GSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAK 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38704005 320 LYCARTAMEVIDDAIQIMG--GLGYTDE--ARVSRFWRDV----RCERIGGGTDEIMIYVAGRQIL 377
Cdd:cd01152 314 LFGSELAQELAELALELLGtaALLRDPApgAELAGRWEADylrsRATTIYGGTSEIQRNIIAERLL 379
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
20-376 |
6.67e-47 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 164.87 E-value: 6.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 20 ITTNFPEEYFRTCDQNGT--------YPREF---MRALADNGISMLGVPEEFGGIPADYVTQ-MLALMEVSKCGAPAFLI 87
Cdd:cd01153 8 LAENVLAPLNADGDREGPvfddgrvvVPPPFkeaLDAFAEAGWMALGVPEEYGGQGLPITVYsALAEIFSRGDAPLMYAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 88 TNGQCIHSMRRFGSAEQLRKTAESTLEtGDPAYALALTEPGAGSD-NNSATTTYTRKNGKVYINGQKTFITGAKEYPYM- 165
Cdd:cd01153 88 GTQGAAATLLAHGTEAQREKWIPRLAE-GEWTGTMCLTEPDAGSDlGALRTKAVYQADGSWRINGVKRFISAGEHDMSEn 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 166 ---LVLARDPQPKDPKKAFTLWWVDSSKPGIKINPL------HKIGWHMLSTCEVYLDNVEVEesdMVGEEGMGFLNVMY 236
Cdd:cd01153 167 ivhLVLARSEGAPPGVKGLSLFLVPKFLDDGERNGVtvarieEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 237 NFEMERLINAARSTGFAECAFEDAARYANQRIAFGKP--------IGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQH 308
Cdd:cd01153 244 MMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLikaapavtIIHHPDVRRSLMTQKAYAEGSRALDLYTATVQDLA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 309 Q-------SLRTSAALA-------KLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIY-VAG 373
Cdd:cd01153 324 ErkategeDRKALSALAdlltpvvKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALdLIG 403
|
...
gi 38704005 374 RQI 376
Cdd:cd01153 404 RKI 406
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
76-378 |
3.20e-42 |
|
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: 152.16 E-value: 3.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 76 EVSKCGAPAflITNGQCIHsmrRFGSAEQLRKTAESTLEtGDPAYALALTEPG-AGSDNNSATTTYTRKNGKVYINGQKT 154
Cdd:cd01155 89 EVFNCQAPD--TGNMEVLH---RYGSEEQKKQWLEPLLD-GKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKW 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 155 FITGAKEyP---YMLVLAR-DPQPKDPKKAFTLWWVDSSKPGIKI-NPLHKIGW------HmlstCEVYLDNVEVEESDM 223
Cdd:cd01155 163 WSSGAGD-PrckIAIVMGRtDPDGAPRHRQQSMILVPMDTPGVTIiRPLSVFGYddaphgH----AEITFDNVRVPASNL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 224 VGEEGMGFLNVMYNFEMERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAW 303
Cdd:cd01155 238 ILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAH 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38704005 304 QADQHQS--LRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYVAGRQILK 378
Cdd:cd01155 318 MIDTVGNkaARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
2-376 |
3.60e-40 |
|
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: 146.35 E-value: 3.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 2 DFSLTEEQELLLASIRELITTN-FP--EEYFRtcdqNGTYPREFMRALADNGisMLG-VPEEFGGIPADYVTQMLALMEV 77
Cdd:cd01151 10 DDLLTEEERAIRDTAREFCQEElAPrvLEAYR----EEKFDRKIIEEMGELG--LLGaTIKGYGCAGLSSVAYGLIAREV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 78 SKCGA---PAFLITNGQCIHSMRRFGSAEQLRKTAEStLETGDPAYALALTEPGAGSDNNSATTTyTRKNGKVY-INGQK 153
Cdd:cd01151 84 ERVDSgyrSFMSVQSSLVMLPIYDFGSEEQKQKYLPK-LASGELIGCFGLTEPNHGSDPGGMETR-ARKDGGGYkLNGSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 154 TFITGAKEYPYMLVLARDpQPKDPKKAFTlwwVDSSKPGIKINPL-HKIGWHMLSTCEVYLDNVEVEESDMV-GEEGMG- 230
Cdd:cd01151 162 TWITNSPIADVFVVWARN-DETGKIRGFI---LERGMKGLSAPKIqGKFSLRASITGEIVMDNVFVPEENLLpGAEGLRg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 231 ---FLNVmynfemERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQ 307
Cdd:cd01151 238 pfkCLNN------ARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQ 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38704005 308 HQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYVAGRQI 376
Cdd:cd01151 312 GKATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAI 380
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
40-368 |
3.85e-34 |
|
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: 130.57 E-value: 3.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 40 REFMRALADNGIsMLGVPEEFGGIPADYVTQMLALMEVSKCGAPAFLITNGQCIHSMRRFGSA---EQLRKTAESTLETG 116
Cdd:cd01154 68 HALMRRLIEEGV-INIEDGPAGEGRRHVHFAAGYLLSDAAAGLLCPLTMTDAAVYALRKYGPEelkQYLPGLLSDRYKTG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 117 DPAyALALTEPGAGSDNNSATTTYTRKNGKVY-INGQKTFITGAKEyPYMLVLARDPQPKDPKKAFTLWWV-----DSSK 190
Cdd:cd01154 147 LLG-GTWMTEKQGGSDLGANETTAERSGGGVYrLNGHKWFASAPLA-DAALVLARPEGAPAGARGLSLFLVprlleDGTR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 191 PGIKINPL-HKIGWHMLSTCEVYLDNVEVEesdMVGEEGMGFLNVMYNFEMERLINAARSTGFAECAFEDAARYANQRIA 269
Cdd:cd01154 225 NGYRIRRLkDKLGTRSVATGEVEFDDAEAY---LIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 270 FGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQS--------LRTSAALAKLYCARTAMEVIDDAIQIMGGLG 341
Cdd:cd01154 302 FGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAAdkpveahmARLATPVAKLIACKRAAPVTSEAMEVFGGNG 381
|
330 340
....*....|....*....|....*..
gi 38704005 342 YTDEARVSRFWRDVRCERIGGGTDEIM 368
Cdd:cd01154 382 YLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
121-214 |
1.39e-24 |
|
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: 96.20 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 121 ALALTEPGAGSDNNS-ATTTYTRKNGKVYINGQKTFITGAKEYPYMLVLARDPQPkDPKKAFTLWWVDSSKPGIKINPL- 198
Cdd:pfam02770 1 AFALTEPGAGSDVASlKTTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGD-DRHGGISLFLVPKDAPGVSVRRIe 79
|
90
....*....|....*.
gi 38704005 199 HKIGWHMLSTCEVYLD 214
Cdd:pfam02770 80 TKLGVRGLPTGELVFD 95
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
76-367 |
9.86e-23 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 100.25 E-value: 9.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 76 EVSKCGAPafliTNGQcIHSMRRFGSAEQLRKTAESTLEtGDPAYALALTEPGAGSDNNSATTTYTRKNGKVY-INGQKT 154
Cdd:PLN02876 514 QVFNCGAP----DTGN-MEVLLRYGNKEQQLEWLIPLLE-GKIRSGFAMTEPQVASSDATNIECSIRRQGDSYvINGTKW 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 155 FITGAKEyP--YMLVLARDPQPKDPK-KAFTLWWVDSSKPGIKI-NPLHKIGW----HmlSTCEVYLDNVEVEESDMVGE 226
Cdd:PLN02876 588 WTSGAMD-PrcRVLIVMGKTDFNAPKhKQQSMILVDIQTPGVQIkRPLLVFGFddapH--GHAEISFENVRVPAKNILLG 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 227 EGMGFLNVMYNFEMERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQAD 306
Cdd:PLN02876 665 EGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLD 744
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38704005 307 QH--QSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI 367
Cdd:PLN02876 745 RLgnKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
6-107 |
2.32e-21 |
|
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: 88.29 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 6 TEEQELLLASIRELITTNFPEeYFRTCDQNGTYPREFMRALADNGISMLGVPEEFGGIPADYVTQMLALMEVSKCGAP-- 83
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAP-HAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASva 79
|
90 100
....*....|....*....|....*
gi 38704005 84 -AFLITNGQCIHSMRRFGSAEQLRK 107
Cdd:pfam02771 80 lALSVHSSLGAPPILRFGTEEQKER 104
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
72-376 |
6.20e-20 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 90.68 E-value: 6.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 72 LALMEVSKCGAPA---FLITNGQCIHSMRRFGSAEQLRKTAEStLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVY 148
Cdd:PLN02526 94 IATAEVARVDASCstfILVHSSLAMLTIALCGSEAQKQKYLPS-LAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 149 INGQKTFITGAKEYPYMLVLARDPQPKDpkkaFTLWWVDSSKPGIKINPL-HKIGWHMLSTCEVYLDNVEVEESDMVgeE 227
Cdd:PLN02526 173 LNGQKRWIGNSTFADVLVIFARNTTTNQ----INGFIVKKGAPGLKATKIeNKIGLRMVQNGDIVLKDVFVPDEDRL--P 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 228 GM-GFLNVMYNFEMERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMaikIDNMRNMVLkVAWQ-A 305
Cdd:PLN02526 247 GVnSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRM---LGNIQAMFL-VGWRlC 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38704005 306 DQHQSLRTS---AALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYVAGRQI 376
Cdd:PLN02526 323 KLYESGKMTpghASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
246-366 |
4.53e-17 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 77.00 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 246 AARSTGFAECAFEDAARYANQRI--AFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQH--------QSLRTSA 315
Cdd:pfam08028 3 AAAALGAARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAaaagkpvtPALRAEA 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 38704005 316 ALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDE 366
Cdd:pfam08028 83 RRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
33-356 |
1.04e-15 |
|
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: 77.75 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 33 DQNGTYPREFMRALADNGISMLGVPEEFGGIPADYVTQMLALMEVSKCG---APAFLITNGQcIHSMRRFGSaEQLRKTA 109
Cdd:cd01163 18 DRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADsniAQALRAHFGF-VEALLLAGP-EQFRKRW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 110 ESTLETGDpAYALALTEPGAGSDNNSATTTyTRKNGKVYINGQKTFITGAKEYPYMLVLARDPQPKDpkkafTLWWVDSS 189
Cdd:cd01163 96 FGRVLNGW-IFGNAVSERGSVRPGTFLTAT-VRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKL-----VFAAVPTD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 190 KPGIK-INPLHKIGWHMLSTCEVYLDNVEVEESDMVGEEGMGFLNvMYNFEMERLINAARSTGFAECAFEDAARYANQRi 268
Cdd:cd01163 169 RPGITvVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRG-TLLTAIYQLVLAAVLAGIARAALDDAVAYVRSR- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 269 afGKPIGH--------NQMIQEKLALMAIKIDNMRNMVLKVAWQADQ--------------HQSLRTSAalAKLYCARTA 326
Cdd:cd01163 247 --TRPWIHsgaesardDPYVQQVVGDLAARLHAAEALVLQAARALDAaaaagtaltaeargEAALAVAA--AKVVVTRLA 322
|
330 340 350
....*....|....*....|....*....|
gi 38704005 327 MEVIDDAIQIMGGLGYTDEARVSRFWRDVR 356
Cdd:cd01163 323 LDATSRLFEVGGASATAREHNLDRHWRNAR 352
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
122-368 |
4.80e-14 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 73.25 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 122 LALTEPGAGSDNNSATTTYTRKNGKVY-INGQKTFITGAKEYPYmLVLArdpQPKDPKKAFTL--WWVDSSKPGIKINPL 198
Cdd:PRK11561 182 MGMTEKQGGSDVLSNTTRAERLADGSYrLVGHKWFFSVPQSDAH-LVLA---QAKGGLSCFFVprFLPDGQRNAIRLERL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 199 H-KIGWHMLSTCEVYLDNVEveeSDMVGEEGMGFLNVMYNFEMERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHN 277
Cdd:PRK11561 258 KdKLGNRSNASSEVEFQDAI---GWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQ 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 278 QMIQEKLALMAIKIDNMRNMVLKV--AW--QADQHQSL--RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRF 351
Cdd:PRK11561 335 PLMRQVLSRMALQLEGQTALLFRLarAWdrRADAKEALwaRLFTPAAKFVICKRGIPFVAEAMEVLGGIGYCEESELPRL 414
|
250
....*....|....*..
gi 38704005 352 WRDVRCERIGGGTDEIM 368
Cdd:PRK11561 415 YREMPVNSIWEGSGNIM 431
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
33-378 |
1.79e-12 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 68.74 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 33 DQNGTYPREFMRA---LADNGISMLGVPEEFGGIPADYvTQMLALMEVSKCGAPAFLITNGQCIHSMRRF---GSAEQ-- 104
Cdd:PTZ00456 92 DGNVTTPKGFKEAyqaLKAGGWTGISEPEEYGGQALPL-SVGFITRELMATANWGFSMYPGLSIGAANTLmawGSEEQke 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 105 --LRKTAEstletGDPAYALALTEPGAGSDNNSATTTYTRK-NGKVYINGQKTFITGAK----EYPYMLVLARDPQPKDP 177
Cdd:PTZ00456 171 qyLTKLVS-----GEWSGTMCLTEPQCGTDLGQVKTKAEPSaDGSYKITGTKIFISAGDhdltENIVHIVLARLPNSLPT 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 178 KKAFTLWWV-------DSS---KPGIKINPLH-KIGWHMLSTCEVYLDNvevEESDMVGEEGMGFlnvmynFEMERLINA 246
Cdd:PTZ00456 246 TKGLSLFLVprhvvkpDGSletAKNVKCIGLEkKMGIKGSSTCQLSFEN---SVGYLIGEPNAGM------KQMFTFMNT 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 247 AR------STGFAECAFEDAARYANQRIAF------------GKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQH 308
Cdd:PTZ00456 317 ARvgtaleGVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIH 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 309 QSLRTSAA-------------LAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM-IYVAGR 374
Cdd:PTZ00456 397 AAAKDAATrealdheigfytpIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQaLDFIGR 476
|
....
gi 38704005 375 QILK 378
Cdd:PTZ00456 477 KVLS 480
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
33-356 |
1.18e-09 |
|
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: 59.28 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 33 DQNGTYPREFMRALADNGISMLGVPEEFGGIPADYVTQMLALMEVSK-CGAPAFlITNGQCIHSmrRFGSAeqLRKTAES 111
Cdd:cd01159 18 ERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEaCGSAAW-VASIVATHS--RMLAA--FPPEAQE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 112 TLETGDPAYALALT-EPGAgsdnnsattTYTRKNGKVYINGQKTFITGAKEYPYMLV---LARDPQPKDPKkAFTLwwvd 187
Cdd:cd01159 93 EVWGDGPDTLLAGSyAPGG---------RAERVDGGYRVSGTWPFASGCDHADWILVgaiVEDDDGGPLPR-AFVV---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 188 sSKPGIKINPLhkigWHMLSTC-----EVYLDNVEVEES------DMVGEEGMGFLNVMYNFEMERLI---NAARSTGFA 253
Cdd:cd01159 159 -PRAEYEIVDT----WHVVGLRgtgsnTVVVDDVFVPEHrtltagDMMAGDGPGGSTPVYRMPLRQVFplsFAAVSLGAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 254 ECAFEDAARYANQRI---AFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQ--------SLRTSAALAKLYC 322
Cdd:cd01159 234 EGALAEFLELAGKRVrqyGAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHAlaggpidvEERARIRRDAAYA 313
|
330 340 350
....*....|....*....|....*....|....
gi 38704005 323 ARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVR 356
Cdd:cd01159 314 AKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIH 347
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
247-341 |
6.05e-06 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 48.27 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 247 ARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIK---IDNMRNMVLKVawqADQHQSLRTSAALAKLYCA 323
Cdd:PRK09463 339 SNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTLTTAA---VDLGEKPSVLSAIAKYHLT 415
|
90
....*....|....*...
gi 38704005 324 RTAMEVIDDAIQIMGGLG 341
Cdd:PRK09463 416 ERGRQVINDAMDIHGGKG 433
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
247-341 |
5.88e-03 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 38.79 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704005 247 ARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIK---IDNMRNMVLKvawQADQHQSLRTSAALAKLYCA 323
Cdd:PRK13026 338 ALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNtylLEAARRLTTT---GLDLGVKPSVVTAIAKYHMT 414
|
90
....*....|....*...
gi 38704005 324 RTAMEVIDDAIQIMGGLG 341
Cdd:PRK13026 415 ELARDVVNDAMDIHAGKG 432
|
|
| |
