|
Name |
Accession |
Description |
Interval |
E-value |
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
56-427 |
0e+00 |
|
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: 685.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 56 EHDIFRESVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNCTGPGFS 135
Cdd:cd01160 2 EHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 136 LHSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDLVIV 215
Cdd:cd01160 82 LHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 216 VAVTNREARsPAHGISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKGFYYLMQELPQERLLI 295
Cdd:cd01160 162 VARTGGEAR-GAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 296 AELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDSCLQLHETKRLDSGSASMAKYWASEL 375
Cdd:cd01160 241 AAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATEL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 31982520 376 QNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIV 427
Cdd:cd01160 321 QNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
53-427 |
1.39e-149 |
|
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: 429.65 E-value: 1.39e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 53 FSSEHDIFRESVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNC-TG 131
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAsLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 132 PGFSLHsDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSD 211
Cdd:COG1960 85 LPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVAD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 212 LVIVVAVTNREARspAHGISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKGFYYLMQELPQE 291
Cdd:COG1960 164 VILVLARTDPAAG--HRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 292 RLLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDSCLQLHETKRLDSGSASMAKYW 371
Cdd:COG1960 242 RLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLF 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 31982520 372 ASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIV 427
Cdd:COG1960 322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
55-426 |
5.98e-119 |
|
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: 351.57 E-value: 5.98e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 55 SEHDIFRESVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQA-YSNCTGPG 133
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAkVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 134 FSLHSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDLV 213
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 214 IVVAVTNREARspAHGISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKGFYYLMQELPQERL 293
Cdd:cd01158 161 IVFAVTDPSKG--YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 294 LIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDSCLQLHETKRLDSGSASMAKYWAS 373
Cdd:cd01158 239 GIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFAS 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 31982520 374 ELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQI 426
Cdd:cd01158 319 EVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
56-424 |
8.77e-105 |
|
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: 313.45 E-value: 8.77e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 56 EHDIFRESVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGllginiaekhggiggdllstavtweeqaysnctgpgfs 135
Cdd:cd00567 2 EQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLL-------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 136 lhsdiVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDLVIV 215
Cdd:cd00567 44 -----GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 216 VAVTNrEARSPAHGISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKGFYYLMQELPQERLLI 295
Cdd:cd00567 119 LARTD-EEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 296 AELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDS-CLQLHETKRLDSGSASMAKYWASE 374
Cdd:cd00567 198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRaAWLLDQGPDEARLEAAMAKLFATE 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 31982520 375 LQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAR 424
Cdd:cd00567 278 AAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
53-428 |
2.39e-104 |
|
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: 314.35 E-value: 2.39e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 53 FSSEHDIFRESVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAY-SNCTG 131
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRaSGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 132 PGFSLHSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSD 211
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 212 LVIVVAVTNREARspAHGISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKGFYYLMQELPQE 291
Cdd:cd01156 162 TLVVYAKTDPSAG--AHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 292 RLLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDSCLQLHETKRLDSGSASMAKYW 371
Cdd:cd01156 240 RLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILY 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 31982520 372 ASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIVS 428
Cdd:cd01156 320 AAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
54-426 |
5.90e-93 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 285.11 E-value: 5.90e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 54 SSEHDIFRESVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNCTGPG 133
Cdd:cd01162 2 NEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 134 F-SLHsDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDL 212
Cdd:cd01162 82 YiSIH-NMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 213 VIVVAVTNREArspAHGISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKGFYYLMQELPQER 292
Cdd:cd01162 161 YVVMARTGGEG---PKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 293 LLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVdsclqLHETKRLDSGSA------S 366
Cdd:cd01162 238 LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMV-----RRAASALDRGDPdavklcA 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 367 MAKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQI 426
Cdd:cd01162 313 MAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARAL 372
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
60-430 |
8.73e-78 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 247.10 E-value: 8.73e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 60 FRESVRKFFQEEVIPHHTEWEKAGEVSREV--WEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEE-QAYSNCTGPGFSL 136
Cdd:PLN02519 33 FKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEiSRASGSVGLSYGA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 137 HSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDLVIVV 216
Cdd:PLN02519 113 HSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 217 AVTNREARSpaHGISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKGFYYLMQELPQERLLIA 296
Cdd:PLN02519 193 AKTDVAAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 297 ELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDSCLQLHETKRLDSGSASMAKYWASELQ 376
Cdd:PLN02519 271 AGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERA 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 31982520 377 NSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIVSDS 430
Cdd:PLN02519 351 TQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKEE 404
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
43-429 |
1.71e-74 |
|
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: 238.52 E-value: 1.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 43 KLTDIGIRRIF----------SSEHDIFRESVRKFFQEEVIPHHTEWEkaGEVSREVWEKAGKQGLLGINIAEKHGGIGG 112
Cdd:cd01161 7 FLGDIVTKQVFpypsvlteeqTEELNMLVGPVEKFFEEVNDPAKNDQL--EKIPRKTLTQLKELGLFGLQVPEEYGGLGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 113 DLLSTAVTWEEQAYSNCTGPGFSLHSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRS- 191
Cdd:cd01161 85 NNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSe 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 192 -GSDWILNGSKVFITNGWLSDLVIVVAVT--NREARSPAHGISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRL 268
Cdd:cd01161 165 dGKHYVLNGSKIWITNGGIADIFTVFAKTevKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 269 PANALLGEENKGFYYLMQELPQERLLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELkthicVTRAFV 348
Cdd:cd01161 245 PVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANM-----AILQYA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 349 DSCLQLHETKRLDSGS-------ASMAKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKEL 421
Cdd:cd01161 320 TESMAYMTSGNMDRGLkaeyqieAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLF 399
|
....*...
gi 31982520 422 IARQIVSD 429
Cdd:cd01161 400 IALTGLQH 407
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
53-427 |
1.44e-72 |
|
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: 232.48 E-value: 1.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 53 FSSEHDIFRESVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSnCTGP 132
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYG-CTGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 133 GFSLHSDIV--MPYIANyGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLS 210
Cdd:cd01157 80 QTAIEANSLgqMPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 211 DLVIVVAVTNREARSPA-HGISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKGFYYLMQELP 289
Cdd:cd01157 159 NWYFLLARSDPDPKCPAsKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 290 QERLLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDSCLQLHETKRLDSGSASMAK 369
Cdd:cd01157 239 KTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 31982520 370 YWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIV 427
Cdd:cd01157 319 AFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
54-426 |
3.19e-69 |
|
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: 224.16 E-value: 3.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 54 SSEHDIFRESVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGLLGINIaEKHGGIGgdLLSTA---VTWE-EQAYSNC 129
Cdd:cd01151 14 TEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATI-KGYGCAG--LSSVAyglIAREvERVDSGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 130 TGpGFSLHSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWL 209
Cdd:cd01151 91 RS-FMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 210 SDLVIVVAVTNREArspahGISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENkGFYYLMQELP 289
Cdd:cd01151 170 ADVFVVWARNDETG-----KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAE-GLRGPFKCLN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 290 QERLLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHIcvtRAFVDSCLQ---LHETKRLDSGSAS 366
Cdd:cd01151 244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEI---ALGLLACLRvgrLKDQGKATPEQIS 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31982520 367 MAKYWASelqnSVAYECV----QLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQI 426
Cdd:cd01151 321 LLKRNNC----GKALEIArtarEMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAI 380
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
20-427 |
3.45e-69 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 224.82 E-value: 3.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 20 RPLPSARCSHSGA-EARLETPSAKKLTDIGIRRIFSSEHDIFRESVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGL 98
Cdd:PTZ00461 3 RVLQSSLGRRSATcGWTAAATMTSASRAFMDLYNPTPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 99 LGINIAEKHGGIGGDLLSTAVTWEEqaYSNCTgPGFSL----HSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTE 174
Cdd:PTZ00461 83 MGVTVPEADGGAGMDAVAAVIIHHE--LSKYD-PGFCLaylaHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 175 PGAGSDLQGVRTNAKR-SGSDWILNGSKVFITNGWLSDLVIVVAVTNREarspahgISLFLVENGMKGFIKGRKLHKMGM 253
Cdd:PTZ00461 160 PGAGTDVLGMRTTAKKdSNGNYVLNGSKIWITNGTVADVFLIYAKVDGK-------ITAFVVERGTKGFTQGPKIDKCGM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 254 KAQDTAELFFEDVRLPANALLGEENKGFYYLMQELPQERLLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHK 333
Cdd:PTZ00461 233 RASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 334 LAELKTHICVTRAFVDSCLQ-LHETKRLDSGSASmAKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYG 412
Cdd:PTZ00461 313 IAEGYADTEAAKALVYSVSHnVHPGNKNRLGSDA-AKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGG 391
|
410
....*....|....*
gi 31982520 413 GTNEIMKELIARQIV 427
Cdd:PTZ00461 392 GTIEAHHKNITKDLL 406
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
54-429 |
3.61e-63 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 208.43 E-value: 3.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 54 SSEHDIFRESVRKFFQEEViPHH--TEWEKAGEVSREVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEqaYSNCTG 131
Cdd:PRK12341 6 TEEQELLLASIRELITRNF-PEEyfRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEE--VSKCGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 132 PGFSLHSDIVMPYIANYGTKEQIEK-FIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLS 210
Cdd:PRK12341 83 PAFLITNGQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 211 DLVIVVAvTNREARSPAHGISLFLVENGMKGfIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKGFYYLMQELPQ 290
Cdd:PRK12341 163 PYMLVLA-RDPQPKDPKKAFTLWWVDSSKPG-IKINPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 291 ERLLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDSC---LQLHETKRLDSgsaSM 367
Cdd:PRK12341 241 ERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVawqADNGQSLRTSA---AL 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31982520 368 AKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIVSD 429
Cdd:PRK12341 318 AKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKD 379
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
60-426 |
1.55e-51 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 177.54 E-value: 1.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 60 FRESVRKFFQEEVIP-----HHTEWEKAGEVSREvWEKA-GKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNCTGPG 133
Cdd:cd01152 6 FRAEVRAWLAAHLPPelreeSALGYREGREDRRR-WQRAlAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 134 FSLHSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDLV 213
Cdd:cd01152 85 NQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 214 IVVAVTNREArsPAH-GISLFLVENGMKGFIkgRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKGFYYLMQELPQER 292
Cdd:cd01152 165 WLLVRTDPEA--PKHrGISILLVDMDSPGVT--VRPIRSINGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 293 LLIAELAISACEFMFEetrnYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFV-DSCLQLHETKRLDSGsASMAKYW 371
Cdd:cd01152 241 VSIGGSAATFFELLLA----RLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVfRLASALAAGKPPGAE-ASIAKLF 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31982520 372 ASELQNSVAYECVQLHGGWG---YMWEYPIAKA-----YVDARVQPIYGGTNEIMKELIARQI 426
Cdd:cd01152 316 GSELAQELAELALELLGTAAllrDPAPGAELAGrweadYLRSRATTIYGGTSEIQRNIIAERL 378
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
97-427 |
3.93e-49 |
|
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: 172.19 E-value: 3.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 97 GLLGINIAEKHGGIGgdlLSTAVTW--EEQAYSNCTGPGFSLHSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTE 174
Cdd:cd01153 49 GWMALGVPEEYGGQG---LPITVYSalAEIFSRGDAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 175 PGAGSDLQGVRTNA-KRSGSDWILNGSKVFITNG-WLSDLVIVVAVTNR--EARSPAHGISLFLV----ENGMKGFIKGR 246
Cdd:cd01153 126 PDAGSDLGALRTKAvYQADGSWRINGVKRFISAGeHDMSENIVHLVLARseGAPPGVKGLSLFLVpkflDDGERNGVTVA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 247 KL-HKMGMKAQDTAELFFEDVRLPanaLLGEENKGFYYLMQELPQERLLIAELAISACEFMFEETRNYVKQRKAFGK--- 322
Cdd:cd01153 206 RIeEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDlik 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 323 -----TVAHIQTVQHKLAELKTHICVTRAFVDSCL------QLHETKRLDSGSAS--------MAKYWASELQNSVAYEC 383
Cdd:cd01153 283 aapavTIIHHPDVRRSLMTQKAYAEGSRALDLYTAtvqdlaERKATEGEDRKALSaladlltpVVKGFGSEAALEAVSDA 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 31982520 384 VQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIM-KELIARQIV 427
Cdd:cd01153 363 IQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQaLDLIGRKIV 407
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
53-429 |
4.96e-49 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 171.17 E-value: 4.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 53 FSSEHDIFRESVRKFFQEEviphhtEWEK------AGEVSREVWEKA-GKQGLLGINIAEKHGGIGGDLLSTAVTWEEqa 125
Cdd:PRK03354 5 LNDEQELFVAGIRELMASE------NWEAyfaecdRDSVYPERFVKAlADMGIDSLLIPEEHGGLDAGFVTLAAVWME-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 126 YSNCTGPGFSLHSdivMPY----IANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSK 201
Cdd:PRK03354 77 LGRLGAPTYVLYQ---LPGgfntFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 202 VFITNGWLSDLVIVVAvtnREARSPAHGI-SLFLVENGMKGfIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKG 280
Cdd:PRK03354 154 CFITSSAYTPYIVVMA---RDGASPDKPVyTEWFVDMSKPG-IKVTKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 281 FYYLMQELPQERLLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDSCLQLHETKRL 360
Cdd:PRK03354 230 FNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTI 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31982520 361 DSGSASMAKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIVSD 429
Cdd:PRK03354 310 TSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
52-426 |
5.43e-43 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 155.78 E-value: 5.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 52 IFSSEHDIFRESVRKFFQEEVIPHHTE-WEKAgEVSREVWEKAGKQGLLGINIaEKHGGIGGDLLSTAVTWEEQAYSNCT 130
Cdd:PLN02526 28 LLTPEEQALRKRVRECMEKEVAPIMTEyWEKA-EFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVARVDAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 131 GPGFSL-HSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWL 209
Cdd:PLN02526 106 CSTFILvHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 210 SDLVIVVA---VTNRearspahgISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKgFYYLMQ 286
Cdd:PLN02526 186 ADVLVIFArntTTNQ--------INGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNS-FQDTNK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 287 ELPQERLLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDSCLQLHETKRLDSGSAS 366
Cdd:PLN02526 257 VLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHAS 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31982520 367 MAKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDarVQPIYG--GTNEIMKELIARQI 426
Cdd:PLN02526 337 LGKAWITKKARETVALGRELLGGNGILADFLVAKAFCD--LEPIYTyeGTYDINALVTGREI 396
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
278-426 |
9.90e-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: 147.40 E-value: 9.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 278 NKGFYYLMQELPQERLLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDSCLQLHET 357
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31982520 358 KRLDSGSASMAKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQI 426
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
54-165 |
5.22e-39 |
|
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: 136.05 E-value: 5.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 54 SSEHDIFRESVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNC-TGP 132
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADAsVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 31982520 133 GFSLHSDIVMPYIANYGTKEQIEKFIPQMTAGK 165
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
61-425 |
1.56e-34 |
|
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: 132.51 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 61 RESVRKFFQEEVIPHHTE-----------WEKAGEVSREVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYS-- 127
Cdd:cd01155 7 RARVKAFMEEHVYPAEQEfleyyaeggdrWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRSff 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 128 -----NCTGPgfslhsDI-VMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPG-AGSDLQGVRTNAKRSGSDWILNGS 200
Cdd:cd01155 87 apevfNCQAP------DTgNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 201 KVFITNGwlSD----LVIVVAVTNREARSPAHGISLFLVENGMKGFIKGRKLHKMGMkaQDT----AELFFEDVRLPANA 272
Cdd:cd01155 161 KWWSSGA--GDprckIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGY--DDAphghAEITFDNVRVPASN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 273 LLGEENKGFyylmqELPQERLLIAEL-----AISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAF 347
Cdd:cd01155 237 LILGEGRGF-----EIAQGRLGPGRIhhcmrLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 348 VdsclqLHETKRLDSGSA-------SMAKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKE 420
Cdd:cd01155 312 V-----LKAAHMIDTVGNkaarkeiAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLR 386
|
....*
gi 31982520 421 LIARQ 425
Cdd:cd01155 387 SIARM 391
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
167-418 |
1.67e-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: 132.88 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 167 IGAIAMTEPGAGSDLQGVRTNAKRSGSD-WILNGSKVFiTNGWLSDLVIVVAVTnREARSPAHGISLFLV----ENGMKG 241
Cdd:cd01154 148 LGGTWMTEKQGGSDLGANETTAERSGGGvYRLNGHKWF-ASAPLADAALVLARP-EGAPAGARGLSLFLVprllEDGTRN 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 242 FIKGRKL-HKMGMKAQDTAELFFEDvrlpANA-LLGEENKGFYYLMQELPQERLLIAELAISACEFMFEETRNYVKQRKA 319
Cdd:cd01154 226 GYRIRRLkDKLGTRSVATGEVEFDD----AEAyLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 320 FGKTVAHIQTVQHKLAELKTHICVTRAFV-DSCLQLHETKRLDSGSASMA-------KYWASELQNSVAYECVQLHGGWG 391
Cdd:cd01154 302 FGKPLIDHPLMRRDLAEMEVDVEAATALTfRAARAFDRAAADKPVEAHMArlatpvaKLIACKRAAPVTSEAMEVFGGNG 381
|
250 260
....*....|....*....|....*..
gi 31982520 392 YMWEYPIAKAYVDARVQPIYGGTNEIM 418
Cdd:cd01154 382 YLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
169-264 |
9.69e-30 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 110.83 E-value: 9.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 169 AIAMTEPGAGSDLQGVRTNA-KRSGSDWILNGSKVFITNGWLSDLVIVVAVTnrEARSPAHGISLFLVENGMKGFIKGRK 247
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLART--GGDDRHGGISLFLVPKDAPGVSVRRI 78
|
90
....*....|....*..
gi 31982520 248 LHKMGMKAQDTAELFFE 264
Cdd:pfam02770 79 ETKLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
75-428 |
3.01e-21 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 96.09 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 75 HHTEWEKAGEVS-----REVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNctgPGFSLHSDI---VMPYIA 146
Cdd:PTZ00456 85 EGCVLLKDGNVTtpkgfKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATAN---WGFSMYPGLsigAANTLM 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 147 NYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGS-DWILNGSKVFITNGwLSDLV--IVVAVTNREA 223
Cdd:PTZ00456 162 AWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAG-DHDLTenIVHIVLARLP 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 224 RSPA--HGISLFLV------ENG----MKGFIKGRKLHKMGMKAQDTAELFFEDvrlPANALLGEENKGFYYLMQELPQE 291
Cdd:PTZ00456 241 NSLPttKGLSLFLVprhvvkPDGsletAKNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 292 RLLIAELAISACEFMFEETRNYVKQRKAF------------GKTVAHIQTVQHKLAELKTHICVTRAF---VDSCLQLHE 356
Cdd:PTZ00456 318 RVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNILFAKAVAEGGRALlldVGRLLDIHA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 357 TKRLDSGSASM----------AKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMK-ELIARQ 425
Cdd:PTZ00456 398 AAKDAATREALdheigfytpiAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQAlDFIGRK 477
|
...
gi 31982520 426 IVS 428
Cdd:PTZ00456 478 VLS 480
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
121-424 |
1.67e-19 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 91.01 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 121 WEEQAYsNCTGPGFSlhsdiVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPG-AGSDLQGVRTNAKRSGSDWILNG 199
Cdd:PLN02876 511 WAPQVF-NCGAPDTG-----NMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVING 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 200 SKvFITNGWLS---DLVIVVAVTNREArsPAHG-ISLFLVENGMKGFIKGRKLHKMGMK--AQDTAELFFEDVRLPA-NA 272
Cdd:PLN02876 585 TK-WWTSGAMDprcRVLIVMGKTDFNA--PKHKqQSMILVDIQTPGVQIKRPLLVFGFDdaPHGHAEISFENVRVPAkNI 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 273 LLGeENKGFyylmqELPQERLLIAEL-----AISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAF 347
Cdd:PLN02876 662 LLG-EGRGF-----EIAQGRLGPGRLhhcmrLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLL 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 348 VDSC---LQLHETKRLdSGSASMAKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAR 424
Cdd:PLN02876 736 VLEAadqLDRLGNKKA-RGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAK 814
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
38-428 |
1.02e-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: 70.05 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 38 TPSAKKLTDI------GIRRIfsseHDIFRE-SVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGL-LGINIAEKHGG 109
Cdd:cd01150 11 TFDWKALTHIleggeeNLRRK----REVERElESDPLFQRELPSKHLSREELYEELKRKAKTDVERMGeLMADDPEKMLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 110 IGGDLLStavtweeqaYSNCTGPGFSLHSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAK 189
Cdd:cd01150 87 LTNSLGG---------YDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 190 --RSGSDWILN-----GSKVFITN-GWLSDLVIVVAVTNREARSpaHGISLFLVE-------NGMKGFIKGRKLHKMGMK 254
Cdd:cd01150 158 ydPLTQEFVINtpdftATKWWPGNlGKTATHAVVFAQLITPGKN--HGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 255 AQDTAELFFEDVRLPANALLG----------------EENKGFYYLMQELPQERLLIAELAI-SACEFMFEETRnYVKQR 317
Cdd:cd01150 236 GVDNGFLQFRNVRIPRENLLNrfgdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLIYDAAmSLKKAATIAIR-YSAVR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 318 KAFGKT-------VAHIQTVQHKL-AELKTHIC---VTRAFVDsclQLHET-KRLDSG-----------SASMaKYWASE 374
Cdd:cd01150 315 RQFGPKpsdpevqILDYQLQQYRLfPQLAAAYAfhfAAKSLVE---MYHEIiKELLQGnsellaelhalSAGL-KAVATW 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 31982520 375 LQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIVS 428
Cdd:cd01150 391 TAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLK 444
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
78-391 |
2.83e-09 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 59.20 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 78 EWE---KAGEVSREVWEKAGKQGLLGINIAEKHGG--------------IGGDLLSTAVTweeQAYSNCTGPGfslhsdi 140
Cdd:PRK13026 99 DWDivqNRKDLPPEVWDYLKKEGFFALIIPKEYGGkgfsayanstivskIATRSVSAAVT---VMVPNSLGPG------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 141 vmPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDL-----QGVRTNAKRSGSDWI---LNGSKVFITNGWLSDl 212
Cdd:PRK13026 169 --ELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAgaipdTGIVCRGEFEGEEVLglrLTWDKRYITLAPVAT- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 213 VIVVAVtnrEARSPAH--------GISLFLVENGMKGFIKGRKLHKMGMKAQDtAELFFEDVRLPANALLGEEN---KGF 281
Cdd:PRK13026 246 VLGLAF---KLRDPDGllgdkkelGITCALIPTDHPGVEIGRRHNPLGMAFMN-GTTRGKDVFIPLDWIIGGPDyagRGW 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 282 YYLMQELPQER-LLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAEL--KTHIC-VTRAFVDSCLQLHET 357
Cdd:PRK13026 322 RMLVECLSAGRgISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIagNTYLLeAARRLTTTGLDLGVK 401
|
330 340 350
....*....|....*....|....*....|....
gi 31982520 358 KrldSGSASMAKYWASELQNSVAYECVQLHGGWG 391
Cdd:PRK13026 402 P---SVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
135-274 |
8.76e-09 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 57.55 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 135 SLHSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNA--KRSGSDWILNGSKVFITNGW---- 208
Cdd:PTZ00460 96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHTPSVEAVKFWpgel 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31982520 209 --LSDLVIVVAVTNREARSpaHGISLFLVE-------NGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALL 274
Cdd:PTZ00460 176 gfLCNFALVYAKLIVNGKN--KGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLL 248
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
295-416 |
2.99e-07 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 49.27 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 295 IAELAISACEFMFEETRNYVKQRK--AFGKTVAHIQTVQHKLAELKTHICVTRAFVDSCLQLHETKRLDS--------GS 364
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGkpvtpalrAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 31982520 365 ASMAKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNE 416
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
132-274 |
9.19e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 50.99 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 132 PGFS-LHSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAK--RSGSDWILNGSKVFITNGW 208
Cdd:PLN02443 96 PGYTdLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATfdPKTDEFVIHSPTLTSSKWW 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 209 ------LSDLVIVVA--VTNREarspAHGISLFLV-----ENGMKgfIKGRKLHKMGMK-------AQDTAELFFEDVRL 268
Cdd:PLN02443 176 pgglgkVSTHAVVYArlITNGK----DHGIHGFIVqlrslDDHSP--LPGVTVGDIGMKfgngaynTMDNGFLRFDHVRI 249
|
....*.
gi 31982520 269 PANALL 274
Cdd:PLN02443 250 PRDQML 255
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
59-275 |
4.58e-05 |
|
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: 45.39 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 59 IFRESVRKFFQEEViphhtEWEKAGEVSREVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEE--QAYSNcTGPGFSL 136
Cdd:cd01163 2 RARPLAARIAEGAA-----ERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRElaAADSN-IAQALRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 137 HSDIVMPyIANYGTKEQIEKFIPQMTAGKCIGAiAMTEpgAGSDLQGVRTNAKRSGSD-WILNGSKVFITNGWLSDLVIV 215
Cdd:cd01163 76 HFGFVEA-LLLAGPEQFRKRWFGRVLNGWIFGN-AVSE--RGSVRPGTFLTATVRDGGgYVLNGKKFYSTGALFSDWVTV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982520 216 VAVTNREA------RSPAHGISLFLVENGmkgfikgrklhkMGMKAQDTAELFFEDVRLPANALLG 275
Cdd:cd01163 152 SALDEEGKlvfaavPTDRPGITVVDDWDG------------FGQRLTASGTVTFDNVRVEPDEVLP 205
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
88-180 |
2.27e-03 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 40.18 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 88 EVWEKAGKQGLLGINIAEKHGGIG-----------------GDLLSTA-VTweeqaysNCTGPG-FSLHsdivmpyianY 148
Cdd:PRK09463 113 EVWQFIKEHGFFGMIIPKEYGGLEfsayahsrvlqklasrsGTLAVTVmVP-------NSLGPGeLLLH----------Y 175
|
90 100 110
....*....|....*....|....*....|..
gi 31982520 149 GTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSD 180
Cdd:PRK09463 176 GTDEQKDHYLPRLARGEEIPCFALTSPEAGSD 207
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
145-274 |
3.06e-03 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 39.84 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 145 IANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAK--RSGSDWILNGSKVFITNGWLSDLVIVVAVTNRE 222
Cdd:PLN02636 152 VINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATfdPLTDEFVINTPNDGAIKWWIGNAAVHGKFATVF 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982520 223 AR--SPAHGISLfLVENGMKGFIKG-RKL---------------HKMGMKAQDTAELFFEDVRLPANALL 274
Cdd:PLN02636 232 ARlkLPTHDSKG-VSDMGVHAFIVPiRDMkthqvlpgveirdcgHKVGLNGVDNGALRFRSVRIPRDNLL 300
|
|
| |
