|
Name |
Accession |
Description |
Interval |
E-value |
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
38-415 |
0e+00 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 766.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 38 GLTEEQIQLRQTVQRFFQEKLAPYADEIDKKNEFPqmREFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSA 117
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFP--RDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 118 AIGLSYGAHSNLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGDHYVLNGNKFWITNGS 197
Cdd:cd01156 79 SVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 198 DADVLIVYAKTDPEAVARGITAFIVEKGMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVLGPLNKGVYVLMSGLDL 277
Cdd:cd01156 159 DADTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 278 ERLVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGHFSAKDCAGVIL 357
Cdd:cd01156 239 ERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVIL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 41393139 358 YCAENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRIIIGRSSNA 415
Cdd:cd01156 319 YAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
39-411 |
0e+00 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 621.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 39 LTEEQIQLRQTVQRFFQEKLAPYADEIDKKNEFPQMREFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSAA 118
Cdd:PLN02519 26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 119 IGLSYGAHSNLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGDHYVLNGNKFWITNGSD 198
Cdd:PLN02519 106 VGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 199 ADVLIVYAKTDPEAVARGITAFIVEKGMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVLGPLNKGVYVLMSGLDLE 278
Cdd:PLN02519 186 AQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 279 RLVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGHFSAKDCAGVILY 358
Cdd:PLN02519 266 RLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILC 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 41393139 359 CAENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRIIIGR 411
Cdd:PLN02519 346 AAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR 398
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
39-412 |
1.56e-165 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 469.71 E-value: 1.56e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 39 LTEEQIQLRQTVQRFFQEKLAPYADEIDKKNEFPqmREFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSAA 118
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFP--RELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 119 IGLSYGAHsNLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGDHYVLNGNKFWITNGSD 198
Cdd:COG1960 83 LALPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 199 ADVLIVYAKTDPEAVARGITAFIVEKGMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVLGPLNKGVYVLMSGLDLE 278
Cdd:COG1960 162 ADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 279 RLVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGHFSAKDCAGVILY 358
Cdd:COG1960 242 RLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLF 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 41393139 359 CAENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRIIIGRS 412
Cdd:COG1960 322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARR 375
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
41-412 |
4.58e-151 |
|
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: 432.46 E-value: 4.58e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 41 EEQIQLRQTVQRFFQEKLAPYADEIDKKNEFPqmREFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSAAIG 120
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFP--REVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 121 LSYGAHSNLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGDHYVLNGNKFWITNGSDAD 200
Cdd:cd01158 79 VIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 201 VLIVYAKTDPEAVARGITAFIVEKGMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVLGPLNKGVYVLMSGLDLERL 280
Cdd:cd01158 159 FYIVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 281 VLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGHFSAKDCAGVILYCA 360
Cdd:cd01158 239 GIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFAS 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 41393139 361 ENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRIIIGRS 412
Cdd:cd01158 319 EVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKH 370
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
41-411 |
8.54e-124 |
|
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: 361.60 E-value: 8.54e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 41 EEQIQLRQTVQRFFQEKLAPYADEIDKKNEFPqmREFWKEMGDLGllgvtapvefggtglgyldhviimeeisrvsaaig 120
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEP--WELLAELGLLL----------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 121 lsygahsnlCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGDHYVLNGNKFWITNGSDAD 200
Cdd:cd00567 44 ---------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDAD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 201 VLIVYAKTDPEAV-ARGITAFIVEKGMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVLGPLNKGVYVLMSGLDLER 279
Cdd:cd00567 115 LFIVLARTDEEGPgHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 280 LVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGHFSA-KDCAGVILY 358
Cdd:cd00567 195 LLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEArLEAAMAKLF 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 41393139 359 CAENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRIIIGR 411
Cdd:cd00567 275 ATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
41-412 |
8.45e-112 |
|
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: 332.54 E-value: 8.45e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 41 EEQIQLRQTVQRFFQEKLAPYADEIDKKNEFPqmREFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRvSAAIG 120
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVP--REVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELAR-AGGSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 121 LSYGAHSNLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGDHYVLNGNKFWITNGSDAD 200
Cdd:cd01160 78 PGLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 201 VLIVYAKTDPEAV-ARGITAFIVEKGMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVLGPLNKGVYVLMSGLDLER 279
Cdd:cd01160 158 VVIVVARTGGEARgAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 280 LVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGHFSAKDCAGVILYC 359
Cdd:cd01160 238 LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 41393139 360 AENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRIIIGRS 412
Cdd:cd01160 318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
40-403 |
1.50e-103 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 313.03 E-value: 1.50e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 40 TEEQIQLRQTVQRFFQEKLAPYADEIDKKNEFPqmREFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSAAI 119
Cdd:PTZ00461 38 TPEHAALRETVAKFSREVVDKHAREDDINMHFN--RDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 120 GLSYGAHSNLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGD-HYVLNGNKFWITNGSD 198
Cdd:PTZ00461 116 CLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 199 ADVLIVYAKTDPEavargITAFIVEKGMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVLGPLNKGVYVLMSGLDLE 278
Cdd:PTZ00461 196 ADVFLIYAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 279 RLVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGHFSAKDCAGVILY 358
Cdd:PTZ00461 271 RVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLF 350
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 41393139 359 CAENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSE 403
Cdd:PTZ00461 351 ATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
39-412 |
6.04e-102 |
|
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: 307.45 E-value: 6.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 39 LTEEQIQLRQTVQRFFQEKLAPYADEIDKKNEFPQmrEFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSAA 118
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPV--DVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 119 IGlSYGAHSNLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGDHYVLNGNKFWITNGSD 198
Cdd:cd01162 79 TA-AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 199 ADVLIVYAKTDPEAvARGITAFIVEKGMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVLGPLNKGVYVLMSGLDLE 278
Cdd:cd01162 158 SDVYVVMARTGGEG-PKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 279 RLVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGHFSA-KDCAGVIL 357
Cdd:cd01162 237 RLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAvKLCAMAKR 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 41393139 358 YCAENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRIIIGRS 412
Cdd:cd01162 317 FATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARA 371
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
31-409 |
8.58e-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: 298.23 E-value: 8.58e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 31 PVDDIVN-GLTEEQIQLRQTVQRFFQEKLAPYA-DEIDKKNefpqmREFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVII 108
Cdd:cd01161 18 PYPSVLTeEQTEELNMLVGPVEKFFEEVNDPAKnDQLEKIP-----RKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 109 MEEISRvSAAIGLSYGAHSNLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQ--GDHYVL 186
Cdd:cd01161 93 AEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 187 NGNKFWITNGSDADVLIVYAKTDPE----AVARGITAFIVEKGMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVLG 262
Cdd:cd01161 172 NGSKIWITNGGIADIFTVFAKTEVKdatgSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 263 PLNKGVYVLMSGLDLERLVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARAC 342
Cdd:cd01161 252 EVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNM 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41393139 343 DKGHFS--AKDCAGVILYCAENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRIII 409
Cdd:cd01161 332 DRGLKAeyQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
39-411 |
7.72e-85 |
|
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: 264.22 E-value: 7.72e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 39 LTEEQIQLRQTVQRFFQEKLAPYADEIDKKNEFPqmREFWKEMGDLGLLGVTaPVEFGGTGLGYLDHVIIMEEISRVSAA 118
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFD--RKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDSG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 119 IGLSYGAHSNLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGDHYVLNGNKFWITNGSD 198
Cdd:cd01151 90 YRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 199 ADVLIVYAKTDPEAVARGitaFIVEKGMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVLgPLNKGVYVLMSGLDLE 278
Cdd:cd01151 170 ADVFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 279 RLVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGhfsaKDCAGVILY 358
Cdd:cd01151 246 RYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQG----KATPEQISL 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 359 CAENATQVALD----GIQCLGGNGYINDYPMGRFLRDAK---LYEigaGTSEIRRIIIGR 411
Cdd:cd01151 322 LKRNNCGKALEiartAREMLGGNGISDEYHIIRHMVNLEsvnTYE---GTHDIHALILGR 378
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
39-411 |
4.17e-82 |
|
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: 256.74 E-value: 4.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 39 LTEEQIQLRQTVQRFFQEKLAPYADEIDKKNEFPQmrEFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSAA 118
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPW--PLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 119 IGLSYGAHSnLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGDHYVLNGNKFWITNGSD 198
Cdd:cd01157 79 VQTAIEANS-LGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 199 ADVLIVYAKTDPEAVA---RGITAFIVEKGMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVLGPLNKGVYVLMSGL 275
Cdd:cd01157 158 ANWYFLLARSDPDPKCpasKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 276 DLERLVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGHFSAKDCAGV 355
Cdd:cd01157 238 DKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 41393139 356 ILYCAENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRIIIGR 411
Cdd:cd01157 318 KAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISR 373
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
39-411 |
4.41e-74 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 236.16 E-value: 4.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 39 LTEEQ----IQLRQTVQRFFQEKlapYADEIDKKNEFPQmrEFWKEMGD--LGLLGVtaPVEFGGTGLGYLDHVIIMEEI 112
Cdd:PRK12341 5 LTEEQelllASIRELITRNFPEE---YFRTCDENGTYPR--EFMRALADngISMLGV--PEEFGGTPADYVTQMLVLEEV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 113 SRVSAAIglsYGAHSNLCVNQMVRHGNQKQKEKYMPKLL-TGEHVGALAMSESNSGSDVVSMKLTA-KKQGDHYvLNGNK 190
Cdd:PRK12341 78 SKCGAPA---FLITNGQCIHSMRRFGSAEQLRKTAESTLeTGDPAYALALTEPGAGSDNNSATTTYtRKNGKVY-LNGQK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 191 FWITNGSDADVLIVYAK-TDPEAVARGITAFIVEKGMPGFSsAQKLDKLGMRGSSTCELVFEDCKIPEENVLGPLNKGVY 269
Cdd:PRK12341 154 TFITGAKEYPYMLVLARdPQPKDPKKAFTLWWVDSSKPGIK-INPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 270 VLMSGLDLERLVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGHFSA 349
Cdd:PRK12341 233 NVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLR 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41393139 350 KDCAGVILYCAENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRIIIGR 411
Cdd:PRK12341 313 TSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGR 374
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
39-412 |
2.88e-60 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 200.44 E-value: 2.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 39 LTEEQIQLRQTVQRFF-QEKLAPYADEIDKKNEFPQmrEFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSA 117
Cdd:PRK03354 5 LNDEQELFVAGIRELMaSENWEAYFAECDRDSVYPE--RFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 118 AIGLSYGAHSNLcvNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGDHYVLNGNKFWITNGS 197
Cdd:PRK03354 83 PTYVLYQLPGGF--NTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 198 DADVLIVYAKTDPEAVARGITAFIVEKGMPGFSsAQKLDKLGMRGSSTCELVFEDCKIPEENVLGPLNKGVYVLMSGLDL 277
Cdd:PRK03354 161 YTPYIVVMARDGASPDKPVYTEWFVDMSKPGIK-VTKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 278 ERLVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGHFSAKDCAGVIL 357
Cdd:PRK03354 240 ERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKY 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 41393139 358 YCAENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRIIIGRS 412
Cdd:PRK03354 320 FCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRA 374
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
40-154 |
1.12e-51 |
|
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: 169.18 E-value: 1.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 40 TEEQIQLRQTVQRFFQEKLAPYADEIDKKNEFPqmREFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSAAI 119
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFP--RELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASV 78
|
90 100 110
....*....|....*....|....*....|....*
gi 41393139 120 GLSYGAHSNLCVNQMVRHGNQKQKEKYMPKLLTGE 154
Cdd:pfam02771 79 ALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
39-411 |
1.99e-49 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 172.73 E-value: 1.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 39 LTEEQIQLRQTVQRFFQEKLAPYADEIDKKNEFPqmREFWKEMGDLGLLGVTAPvEFGGTGLGYLDHVIIMEEISRVSAA 118
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFP--FHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 119 IGLSYGAHSNLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGDHYVLNGNKFWITNGSD 198
Cdd:PLN02526 106 CSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 199 ADVLIVYAKTdpeAVARGITAFIVEKGMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVLGPLNKgVYVLMSGLDLE 278
Cdd:PLN02526 186 ADVLVIFARN---TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNS-FQDTNKVLAVS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 279 RLVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGHFSAKDCAGVILY 358
Cdd:PLN02526 262 RVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAW 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 41393139 359 CAENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRIIIGR 411
Cdd:PLN02526 342 ITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGR 394
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
49-411 |
9.94e-48 |
|
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: 167.95 E-value: 9.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 49 TVQRFFQEKLAPYADEID--------KKNEFPQ-MREFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSAAI 119
Cdd:cd01153 4 EVARLAENVLAPLNADGDregpvfddGRVVVPPpFKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 120 GLSYGAHSnlCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGD-HYVLNGNKFWITNG-- 196
Cdd:cd01153 84 MYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGeh 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 197 --SDADVLIVYAKT-DPEAVARGITAFIVEK-----GMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPeenVLGPLNKGV 268
Cdd:cd01153 162 dmSENIVHLVLARSeGAPPGVKGLSLFLVPKflddgERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 269 YVLMSGLDLERLVLASGPVGIMQAVLDHAIPYLHVREAFGQ--------KIGHFQLMQGKMADMYTRLSSCRQ-YLYnVA 339
Cdd:cd01153 239 AQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDlikaapavTIIHHPDVRRSLMTQKAYAEGSRAlDLY-TA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 340 RACDKGHFSAKD---------CAGVIL-----YCAENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIR 405
Cdd:cd01153 318 TVQDLAERKATEgedrkalsaLADLLTpvvkgFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQ 397
|
....*..
gi 41393139 406 RI-IIGR 411
Cdd:cd01153 398 ALdLIGR 404
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
41-412 |
7.47e-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: 7.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 41 EEQIQLRQTVQRFFQEKLAP---YADEIDKKNEFPQMREFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRvSA 117
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPelrEESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAA-AG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 118 AIGLSYGAHSNLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGDHYVLNGNKFWITNGS 197
Cdd:cd01152 80 APVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 198 DADVLIVYAKTDPEAVA-RGITAFIVEKGMPGFsSAQKLDKLgMRGSSTCELVFEDCKIPEENVLGPLNKGVYVLMSGLD 276
Cdd:cd01152 160 YADWAWLLVRTDPEAPKhRGISILLVDMDSPGV-TVRPIRSI-NGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 277 LERLVLASGPVGIMQAVLDHAIpyLHVREAFGqkiGHF-QLMQGKMADMYTRLSSCRQYLYNVARACDKGHFSAKDCAGV 355
Cdd:cd01152 238 FERVSIGGSAATFFELLLARLL--LLTRDGRP---LIDdPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIA 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41393139 356 ILYCAENATQVALDGIQCLGGNGYI-NDYPM----GRFLRD---AKLYEIGAGTSEIRRIIIGRS 412
Cdd:cd01152 313 KLFGSELAQELAELALELLGTAALLrDPAPGaelaGRWEADylrSRATTIYGGTSEIQRNIIAER 377
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
265-412 |
2.45e-43 |
|
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: 148.56 E-value: 2.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 265 NKGVYVLMSGLDLERLVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDK 344
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41393139 345 GHFSAKDCAGVILYCAENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRIIIGRS 412
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARR 148
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
144-404 |
7.68e-37 |
|
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: 139.04 E-value: 7.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 144 EKYMPKLLTGEH----VGALAMSESNSGSDVVSMKLTAKKQ-GDHYVLNGNKfWITNGSDADVLIVYAKT-DPEAVARGI 217
Cdd:cd01154 132 KQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSgGGVYRLNGHK-WFASAPLADAALVLARPeGAPAGARGL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 218 TAFIVEKGMP-----GFSSAQKLDKLGMRGSSTCELVFEDCkipEENVLGPLNKGVYVLMSGLDLERLVLASGPVGIMQA 292
Cdd:cd01154 211 SLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 293 VLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDK-GHFSAKDCAGVIL-------YCAENAT 364
Cdd:cd01154 288 ALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRaAADKPVEAHMARLatpvaklIACKRAA 367
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 41393139 365 QVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEI 404
Cdd:cd01154 368 PVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNI 407
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
158-251 |
9.51e-33 |
|
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: 118.92 E-value: 9.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 158 ALAMSESNSGSDVVSMK-LTAKKQGDHYVLNGNKFWITNGSDADVLIVYAKTDPEAVARGITAFIVEKGMPGFSSAQKLD 236
Cdd:pfam02770 1 AFALTEPGAGSDVASLKtTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 41393139 237 KLGMRGSSTCELVFE 251
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
72-411 |
1.58e-26 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 111.88 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 72 PQMREFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSAAI----GLSYGAhsnlcVNQMVRHGNQKQKEKYM 147
Cdd:PTZ00456 99 KGFKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFsmypGLSIGA-----ANTLMAWGSEEQKEQYL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 148 PKLLTGEHVGALAMSESNSGSDVVSMKLTAKKQGD-HYVLNGNKFWITNG----SDADVLIVYAKTdPEAVA--RGITAF 220
Cdd:PTZ00456 174 TKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGdhdlTENIVHIVLARL-PNSLPttKGLSLF 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 221 IVEKGMP---GFSSAQK------LD-KLGMRGSSTCELVFEDCKipeENVLGPLNKGVYVLMSGLDLERLVLASGPVGIM 290
Cdd:PTZ00456 253 LVPRHVVkpdGSLETAKnvkcigLEkKMGIKGSSTCQLSFENSV---GYLIGEPNAGMKQMFTFMNTARVGTALEGVCHA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 291 QAVLDHAIPYLHVR------------EAFGQKIGHFqlmqgkmADMYTRLSSC-------RQYLYNVARACDKgHFSAKD 351
Cdd:PTZ00456 330 ELAFQNALRYARERrsmralsgtkepEKPADRIICH-------ANVRQNILFAkavaeggRALLLDVGRLLDI-HAAAKD 401
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41393139 352 CAG-------------VILYC-AENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRI-IIGR 411
Cdd:PTZ00456 402 AATrealdheigfytpIAKGClTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGR 476
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
44-411 |
2.71e-23 |
|
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: 100.54 E-value: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 44 IQLRQTVQRFFQEKLAP--------YADEIDKKNEFPQMREFWKEMG-DLGLLGVTAPVEFGGTGLGYLDHVIIMEEISR 114
Cdd:cd01155 4 QELRARVKAFMEEHVYPaeqefleyYAEGGDRWWTPPPIIEKLKAKAkAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 115 -VSAAIGLSYGA--HSNLCVnqMVRHGNQKQKEKYMPKLLTGEHVGALAMSESN-SGSDVVSMKLTAKKQGDHYVLNGNK 190
Cdd:cd01155 84 sFFAPEVFNCQApdTGNMEV--LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 191 FWITNGSDAD--VLIVYAKTDPEAVARGI--TAFIVEKGMPGFSSAQKLDKLGMRGS--STCELVFEDCKIPEENVLGPL 264
Cdd:cd01155 162 WWSSGAGDPRckIAIVMGRTDPDGAPRHRqqSMILVPMDTPGVTIIRPLSVFGYDDAphGHAEITFDNVRVPASNLILGE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 265 NKGVYVLMSGLDLERLVLASGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDK 344
Cdd:cd01155 242 GRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDT 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41393139 345 ghFSAKDCAGVILYCAENATQVALD----GIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEIRRIIIGR 411
Cdd:cd01155 322 --VGNKAARKEIAMIKVAAPRMALKiidrAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
51-300 |
1.82e-19 |
|
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: 89.30 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 51 QRF--FQEKLAPYADEIDKKNEFPqmREFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSAAIGLSYGAHSN 128
Cdd:cd01163 1 ARArpLAARIAEGAAERDRQRGLP--YEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 129 LcVNQMVRHGNQKQKEKYMPKLLTGEHVGAlAMSESNSGSDVVSMKLTAkKQGDHYVLNGNKFWITNGSDADVLIVYAkT 208
Cdd:cd01163 79 F-VEALLLAGPEQFRKRWFGRVLNGWIFGN-AVSERGSVRPGTFLTATV-RDGGGYVLNGKKFYSTGALFSDWVTVSA-L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 209 DPEAVArgiTAFIVEKGMPGFSSAQKLDKLGMR--GSSTceLVFEDCKIPEENVLG---PLNKGVYVLMsgldLERLVLA 283
Cdd:cd01163 155 DEEGKL---VFAAVPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLPrpnAPDRGTLLTA----IYQLVLA 225
|
250
....*....|....*..
gi 41393139 284 SGPVGIMQAVLDHAIPY 300
Cdd:cd01163 226 AVLAGIARAALDDAVAY 242
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
134-404 |
1.10e-14 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 75.99 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 134 MVRHGNQKQKEKYMPKLLTGEHVGALAMSESN-SGSDVVSMKLTAKKQGDHYVLNGNKFWITNGSD--ADVLIVYAKTDP 210
Cdd:PLN02876 529 LLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDprCRVLIVMGKTDF 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 211 EAVARGITAFI-VEKGMPGFSSAQKLDKLGMRGS--STCELVFEDCKIPEENVLGPLNKGVYVLMSGLDLERLVLASGPV 287
Cdd:PLN02876 609 NAPKHKQQSMIlVDIQTPGVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLI 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 288 GI----MQAVLDHAIPylhvREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDK-GHFSAKDCAGVILYCAEN 362
Cdd:PLN02876 689 GAaergMQLMVQRALS----RKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRlGNKKARGIIAMAKVAAPN 764
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 41393139 363 ATQVALD-GIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEI 404
Cdd:PLN02876 765 MALKVLDmAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
138-404 |
2.13e-12 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 68.62 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 138 GNQKQKekympkLLTGehvgaLAMSESNSGSDVVSMKLTAKK-QGDHYVLNGNK-FWITNGSDADVLIVYAKTdpeavar 215
Cdd:PRK11561 172 GGQKRG------LLIG-----MGMTEKQGGSDVLSNTTRAERlADGSYRLVGHKwFFSVPQSDAHLVLAQAKG------- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 216 GITAFIVEKGMP-GFSSAQKL----DKLGMRGSSTCELVFEDCKipeENVLGPLNKGV-YVL-MSGLdlERLVLASGPVG 288
Cdd:PRK11561 234 GLSCFFVPRFLPdGQRNAIRLerlkDKLGNRSNASSEVEFQDAI---GWLLGEEGEGIrLILkMGGM--TRFDCALGSHG 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 289 IMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGHfSAKDCAGVILY--------CA 360
Cdd:PRK11561 309 LMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRA-DAKEALWARLFtpaakfviCK 387
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 41393139 361 ENATQVAlDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSEI 404
Cdd:PRK11561 388 RGIPFVA-EAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNI 430
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
108-339 |
6.63e-12 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 67.19 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 108 IMEEISRVSAAIGLSYGAHSNLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAK--KQGDHYV 185
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATfdPLTDEFV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 186 LN-----GNKFWITNGS-DADVLIVYAKT-----DPEAVA-RGITAFIV-------EKGMPGFSSAQKLDKLGMRGSSTC 246
Cdd:PLN02636 206 INtpndgAIKWWIGNAAvHGKFATVFARLklpthDSKGVSdMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 247 ELVFEDCKIPEENVLG----------------PLNKGVYVLMSGLDLERLVLASGPVGIMQAVLDHAIPYLHVREAFGQ- 309
Cdd:PLN02636 286 ALRFRSVRIPRDNLLNrfgdvsrdgkytsslpTINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPp 365
|
250 260 270
....*....|....*....|....*....|....*
gi 41393139 310 -----KIGHFQLMQGKMADMytrLSScrQYLYNVA 339
Cdd:PLN02636 366 kqpeiSILDYQSQQHKLMPM---LAS--TYAFHFA 395
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
103-310 |
9.15e-12 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 66.97 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 103 LDHVIIMEEISRVSAAIGLSYGAHSNLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAK--KQ 180
Cdd:cd01150 82 EKMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATydPL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 181 GDHYVLN-----GNKFWITN-GSDADVLIVYAKTDPEAVARGITAFIVE-------KGMPGFSSAQKLDKLGMRGSSTCE 247
Cdd:cd01150 162 TQEFVINtpdftATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNGF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 248 LVFEDCKIPEENVlgpLNK-------GVYV------------LMSGLDLERLVLASGPVGIMQAVLDHAIPYLHVREAFG 308
Cdd:cd01150 242 LQFRNVRIPRENL---LNRfgdvspdGTYVspfkdpnkrygaMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFG 318
|
..
gi 41393139 309 QK 310
Cdd:cd01150 319 PK 320
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
76-324 |
3.65e-10 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 61.90 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 76 EFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSAAIGLSYGAHSNLCVNQMVRH-GNQKQKEKYMPKLLTGE 154
Cdd:PRK13026 112 EVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLGPGELLTHyGTQEQKDYWLPRLADGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 155 HVGALAMSESNSGSDVVSMKLTA-----KKQGDHYV---LNGNKFWITNGSDADVL-IVYAKTDPEA-----VARGITAF 220
Cdd:PRK13026 192 EIPCFALTGPEAGSDAGAIPDTGivcrgEFEGEEVLglrLTWDKRYITLAPVATVLgLAFKLRDPDGllgdkKELGITCA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 221 IVEKGMPGFSSAQKLDKLGMR---GSSTCELVFedckIPEENVL-GPLN--KGVYVLMS------GLDLERLVLASGPVG 288
Cdd:PRK13026 272 LIPTDHPGVEIGRRHNPLGMAfmnGTTRGKDVF----IPLDWIIgGPDYagRGWRMLVEclsagrGISLPALGTASGHMA 347
|
250 260 270
....*....|....*....|....*....|....*.
gi 41393139 289 IMQAVldhaiPYLHVREAFGQKIGHFQLMQGKMADM 324
Cdd:PRK13026 348 TRTTG-----AYAYVRRQFGMPIGQFEGVQEALARI 378
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
73-294 |
4.22e-10 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 61.44 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 73 QMREFWKEMGDLGllGVTAPVEFGGTGLGYLDHVIIMEEISRVSAAIGLSYGAHSNLCVNQMVRHGNQKQKEKYMPKLLT 152
Cdd:PTZ00457 54 QIRSNDKILGNLY--GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 153 GEHVGALAMSESNsGSDvVSMKLTAKKQGDH--YVLNGNKFWItNGSDADVLIVYAKT--------DPEAVARgITAFIV 222
Cdd:PTZ00457 132 GTIMMGWATEEGC-GSD-ISMNTTKASLTDDgsYVLTGQKRCE-FAASATHFLVLAKTltqtaaeeGATEVSR-NSFFIC 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41393139 223 EKGMPGFSsaqkldklgMRGSStceLVFEDckIPEENVLGPLNKGVYVLMSGLDLERLVLASGPVGIMQAVL 294
Cdd:PTZ00457 208 AKDAKGVS---------VNGDS---VVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVV 265
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
138-261 |
3.10e-08 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 55.62 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 138 GNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTA--KKQGDHYVLN-----GNKFWITN-GSDADVLIVYAKTD 209
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLI 189
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 41393139 210 PEAVARGITAFIVE-------KGMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVL 261
Cdd:PTZ00460 190 VNGKNKGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLL 248
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
76-378 |
8.25e-07 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 51.36 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 76 EFWKEMGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSAAiglsygahsnLCVNQMV-----------RHGNQKQKE 144
Cdd:PRK09463 113 EVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGT----------LAVTVMVpnslgpgelllHYGTDEQKD 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 145 KYMPKLLTGEHVGALAMSESNSGSDVVSMKLTA-----KKQGDHYV---LNGNKFWITNGSDADVLIVYAKT-DPE---- 211
Cdd:PRK09463 183 HYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGvvckgEWQGEEVLgmrLTWNKRYITLAPIATVLGLAFKLyDPDgllg 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 212 -AVARGITAFIVEKGMPGFSSAQKLDKLG---MRGSSTCELVFedckIPEENVLG---PLNKGVYVLMSGLDLERLV-LA 283
Cdd:PRK09463 263 dKEDLGITCALIPTDTPGVEIGRRHFPLNvpfQNGPTRGKDVF----IPLDYIIGgpkMAGQGWRMLMECLSVGRGIsLP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 284 SGPVGIMQAVLDHAIPYLHVREAFGQKIGHFQLMQGKMADM--YTrlsscrqYLYNVAR-----ACDKGHFSAKDCAGVI 356
Cdd:PRK09463 339 SNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIagNA-------YLMDAARtlttaAVDLGEKPSVLSAIAK 411
|
330 340
....*....|....*....|..
gi 41393139 357 LYCAENATQVALDGIQCLGGNG 378
Cdd:PRK09463 412 YHLTERGRQVINDAMDIHGGKG 433
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
287-403 |
1.93e-06 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 46.96 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 287 VGIMQAVLDHAIPYL--HVREAFGQKIGHFQLMQGKMADMYTRLSSCRQYLY-NVARACDKGHfSAKDCAGVI------- 356
Cdd:pfam08028 7 LGAARAALAEFTERArgRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLErAAARIEAAAA-AGKPVTPALraearra 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 41393139 357 -LYCAENATQVALDGIQCLGGNGYINDYPMGRFLRDAKLYEIGAGTSE 403
Cdd:pfam08028 86 aAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
56-392 |
1.31e-05 |
|
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: 46.96 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 56 EKLAPYADEI-DKKNEFPQMREFWKE----MGDLGLLGVTAPVEFGGTGLGYLDHVIIMEEISRVSAAIG---LSYGAHS 127
Cdd:cd01159 1 ARAEDLAPLIrERAPEAERARRLPDEvvraLREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAwvaSIVATHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 128 NlcvnQMVRHGNQKQKEKYmpklltGEHVGALAmsesnsgSDVVSMKLTAKKQGDHYVLNGNKFWITnGSD-ADVLIVYA 206
Cdd:cd01159 81 R----MLAAFPPEAQEEVW------GDGPDTLL-------AGSYAPGGRAERVDGGYRVSGTWPFAS-GCDhADWILVGA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 207 KTDPEAVARGITAFIVEKGmpGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVL--GPLNKGVYVLmSGLDLER----- 279
Cdd:cd01159 143 IVEDDDGGPLPRAFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtaGDMMAGDGPG-GSTPVYRmplrq 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 280 ---LVLASGPVGIMQAVLDHAIPYLHVR---EAFGQKIGHFQLMQGKMADMYTRLSSCRQYLYNVARACDKGHFSAK--- 350
Cdd:cd01159 220 vfpLSFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGGpid 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 41393139 351 ---------DCAGVILYCAENATQVALdgiqCLGGNGYINDYPMGRFLRDA 392
Cdd:cd01159 300 veerarirrDAAYAAKLSAEAVDRLFH----AAGGSALYTASPLQRIWRDI 346
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
116-307 |
1.42e-04 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 43.99 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 116 SAAIGLsyGAHSNLCVNQMVRHGNQKQKEKYMPKLLTGEHVGALAMSESNSGSDV--VSMKLTAKKQGDHYVLN-----G 188
Cdd:PLN02312 148 SLAIKL--GVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVrgIETVTTYDPKTEEFVINtpcesA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 189 NKFWITNGSD-ADVLIVYAKTDPEAVARGITAFIVE------KGMPGFSSAQKLDKLGMRGSSTCELVFEDCKIPEENVL 261
Cdd:PLN02312 226 QKYWIGGAANhATHTIVFSQLHINGKNEGVHAFIAQirdqdgNICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLL 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41393139 262 GP----LNKGVYV------------LMSGLDLERLVLASGPVGIMQAVLDHAIPYLHVREAF 307
Cdd:PLN02312 306 NSvadvSPDGKYVsaikdpdqrfgaFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
138-312 |
2.75e-03 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 39.82 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 138 GNQKQKEKYMPKLLTGEHVGALAMSESNSGSDVVSMKLTAK--KQGDHYVLN-----GNKFWITN-GSDADVLIVYAKTD 209
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATfdPKTDEFVIHsptltSSKWWPGGlGKVSTHAVVYARLI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393139 210 PEAVARGITAFIVE-------KGMPGFSSAQKLDKLGMRGSSTCE---LVFEDCKIPEENVLGPLNK----GVYVlmsGL 275
Cdd:PLN02443 194 TNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSKvtreGKYV---QS 270
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 41393139 276 DLERLVLASGPVGIMQAVLDHAIPYLH-----------VREAFGQKIG 312
Cdd:PLN02443 271 DVPRQLVYGTMVYVRQTIVADASTALSravciatrysaVRRQFGSQDG 318
|
|
| |
