|
Name |
Accession |
Description |
Interval |
E-value |
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
55-427 |
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: 703.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 55 PEHDIFRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYSNCSGPGF 134
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 135 SIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVI 214
Cdd:cd01160 81 SLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 215 VVAVTNHEApSPAHGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLL 294
Cdd:cd01160 161 VVARTGGEA-RGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 295 IADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWASE 374
Cdd:cd01160 240 IAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 4501857 375 LQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIV 427
Cdd:cd01160 320 LQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
53-427 |
8.18e-151 |
|
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: 432.73 E-value: 8.18e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 53 FSPEHDIFRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYSNCS-G 131
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASlA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 132 PGFSIHSGiVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGSLSD 211
Cdd:COG1960 85 LPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVAD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 212 VVIVVAVTNHEAPspAHGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQE 291
Cdd:COG1960 164 VILVLARTDPAAG--HRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 292 RLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYW 371
Cdd:COG1960 242 RLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLF 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 4501857 372 ASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIV 427
Cdd:COG1960 322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
55-426 |
4.82e-118 |
|
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: 349.26 E-value: 4.82e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 55 PEHDIFRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYSNCS-GPG 133
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASvAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 134 FSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGSLSDVV 213
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 214 IVVAVTNHEAPspAHGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERL 293
Cdd:cd01158 161 IVFAVTDPSKG--YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 294 LIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWAS 373
Cdd:cd01158 239 GIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFAS 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 4501857 374 ELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREI 426
Cdd:cd01158 319 EVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
55-424 |
2.57e-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: 314.99 E-value: 2.57e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 55 PEHDIFRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGllgvniaehlggiggdlySAAIVWEeqaysncsgpgf 134
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLL------------------GAALLLA------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 135 sihsgivmsyitnHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVI 214
Cdd:cd00567 51 -------------YGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 215 VVAVTNhEAPSPAHGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLL 294
Cdd:cd00567 118 VLARTD-EEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 295 IADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDN-CLQLHEAKRLDSATACMAKYWAS 373
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRaAWLLDQGPDEARLEAAMAKLFAT 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 4501857 374 ELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAR 424
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
53-427 |
3.75e-105 |
|
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: 316.28 E-value: 3.75e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 53 FSPEHDIFRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYSNCS-G 131
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 132 PGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGSLSD 211
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 212 VVIVVAVTNHEAPspAHGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQE 291
Cdd:cd01156 162 TLVVYAKTDPSAG--AHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 292 RLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYW 371
Cdd:cd01156 240 RLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILY 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 4501857 372 ASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIV 427
Cdd:cd01156 320 AAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELF 375
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
56-426 |
3.44e-96 |
|
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: 293.20 E-value: 3.44e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 56 EHDIFRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYSNCSGPGF- 134
Cdd:cd01162 4 EQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 135 SIHSgIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVI 214
Cdd:cd01162 84 SIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVYV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 215 VVAVTNHEAPSpahGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLL 294
Cdd:cd01162 163 VMARTGGEGPK---GISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 295 IADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATAC-MAKYWAS 373
Cdd:cd01162 240 IASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCaMAKRFAT 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 4501857 374 ELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREI 426
Cdd:cd01162 320 DECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARAL 372
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
56-423 |
2.33e-75 |
|
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: 240.83 E-value: 2.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 56 EHDIFRKSVRKFFQEEVIPHHSEWEkaGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYSNCSGPGFS 135
Cdd:cd01161 30 ELNMLVGPVEKFFEEVNDPAKNDQL--EKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFSVTLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 136 IHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKK--DGSDWILNGSKVFISNGSLSDVV 213
Cdd:cd01161 108 AHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWITNGGIADIF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 214 IVVAVTNHEAP--SPAHGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQE 291
Cdd:cd01161 188 TVFAKTEVKDAtgSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 292 RLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTR--AFVDNCLQLHEAKRLDSATACMAK 369
Cdd:cd01161 268 RFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATEsmAYMTSGNMDRGLKAEYQIEAAISK 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 4501857 370 YWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIA 423
Cdd:cd01161 348 VFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIA 401
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
60-426 |
3.03e-75 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 240.55 E-value: 3.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 60 FRKSVRKFFQEEVIPHHSEWEKAGEVSREV--WEKAGKQGLLGVNIAEHLGGIG-GDLYSAAIVWEEQAYSNCSGPGFSI 136
Cdd:PLN02519 33 FKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYGGLGlGYLYHCIAMEEISRASGSVGLSYGA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 137 HSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVV 216
Cdd:PLN02519 113 HSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 217 AVTNHEAPSpaHGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLLIA 296
Cdd:PLN02519 193 AKTDVAAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 297 DVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWASELQ 376
Cdd:PLN02519 271 AGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERA 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 4501857 377 NSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREI 426
Cdd:PLN02519 351 TQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
60-427 |
1.94e-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: 1.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 60 FRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYSnCSGPGFSIHS- 138
Cdd:cd01157 8 FQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYG-CTGVQTAIEAn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 139 --GIVMSYITnhGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVV 216
Cdd:cd01157 87 slGQMPVIIS--GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 217 AVTNHEAPSPA-HGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLLI 295
Cdd:cd01157 165 ARSDPDPKCPAsKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 296 ADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATACMAKYWASEL 375
Cdd:cd01157 245 AAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADI 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 4501857 376 QNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIV 427
Cdd:cd01157 325 ANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
54-426 |
9.24e-70 |
|
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: 225.70 E-value: 9.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 54 SPEHDIFRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHlGGIGGDLYSAAIVWEE--QAYSNCSG 131
Cdd:cd01151 14 TEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGY-GCAGLSSVAYGLIAREveRVDSGYRS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 132 pGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGSLSD 211
Cdd:cd01151 93 -FMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 212 VVIVVAVTNHEApspahGISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENkGFYYIMKELPQE 291
Cdd:cd01151 172 VFVVWARNDETG-----KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAE-GLRGPFKCLNNA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 292 RLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHIcvtRAFVDNCLQ---LHEAKRLDSATACMA 368
Cdd:cd01151 246 RYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEI---ALGLLACLRvgrLKDQGKATPEQISLL 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4501857 369 KYWASelqnSVAYDCV----QLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREI 426
Cdd:cd01151 323 KRNNC----GKALEIArtarEMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAI 380
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
54-427 |
1.09e-69 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 226.36 E-value: 1.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 54 SPEHDIFRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEqaYSNCSgPG 133
Cdd:PTZ00461 38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHE--LSKYD-PG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 134 FSI----HSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGS-DWILNGSKVFISNGS 208
Cdd:PTZ00461 115 FCLaylaHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 209 LSDVVIVVAVTNHEapspahgISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKEL 288
Cdd:PTZ00461 195 VADVFLIYAKVDGK-------ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 289 PQERLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFV---------DNClqlheaKR 359
Cdd:PTZ00461 268 ELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVysvshnvhpGNK------NR 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4501857 360 LDSATacmAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIV 427
Cdd:PTZ00461 342 LGSDA---AKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLL 406
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
54-427 |
9.09e-65 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 212.28 E-value: 9.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 54 SPEHDIFRKSVRKFFQEEViPHH--SEWEKAGEVSREVWEKAGKQG--LLGVniAEHLGGIGGDLYSAAIVWEEqaYSNC 129
Cdd:PRK12341 6 TEEQELLLASIRELITRNF-PEEyfRTCDENGTYPREFMRALADNGisMLGV--PEEFGGTPADYVTQMLVLEE--VSKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 130 SGPGFSIHSGIVMSYITNHGSEEQIKH-FIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGS 208
Cdd:PRK12341 81 GAPAFLITNGQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 209 LSDVVIVVAvTNHEAPSPAHGISLFLVENGMKGfIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKEL 288
Cdd:PRK12341 161 EYPYMLVLA-RDPQPKDPKKAFTLWWVDSSKPG-IKINPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 289 PQERLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFV-------DNclqlHEAKRLD 361
Cdd:PRK12341 239 EMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVykvawqaDN----GQSLRTS 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4501857 362 SAtacMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIV 427
Cdd:PRK12341 315 AA---LAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQIL 377
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
97-427 |
3.68e-52 |
|
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: 180.28 E-value: 3.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 97 GLLGVNIAEHLGGIG--GDLYSAAivwEEQAYSNCSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTE 174
Cdd:cd01153 49 GWMALGVPEEYGGQGlpITVYSAL---AEIFSRGDAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 175 PGAGSDLQGIKTNA--KKDGSdWILNGSKVFISNG----SLSDVVIVVAVTNhEAPSPAHGISLFLV----ENGMKGFIK 244
Cdd:cd01153 126 PDAGSDLGALRTKAvyQADGS-WRINGVKRFISAGehdmSENIVHLVLARSE-GAPPGVKGLSLFLVpkflDDGERNGVT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 245 GRKL-HKMGLKAQDTAELFFEDIRlpaSALLGEENKGFYYIMKELPQERLLIADVAISASEFMFEETRNYVKQRKAFGK- 322
Cdd:cd01153 204 VARIeEKMGLHGSPTCELVFDNAK---GELIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDl 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 323 -------TVAHLQTVQHKLAELKTHICVTRAFVDNC---LQLHEAK-----------RLDSATACMAKYWASELQNSVAY 381
Cdd:cd01153 281 ikaapavTIIHHPDVRRSLMTQKAYAEGSRALDLYTatvQDLAERKategedrkalsALADLLTPVVKGFGSEAALEAVS 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 4501857 382 DCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIM-KELIAREIV 427
Cdd:cd01153 361 DAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQaLDLIGRKIV 407
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
55-426 |
3.20e-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: 176.77 E-value: 3.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 55 PEHDIFRKSVRKFFQEEVIP-----HHSEWEKAGEVSREvWEKA-GKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYSN 128
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPelreeSALGYREGREDRRR-WQRAlAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 129 CSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGS 208
Cdd:cd01152 80 APVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 209 LSDVVIVVAVTNHEAPSPAhGISLFLVENGMKGfIKGRKLHK-MGlkAQDTAELFFEDIRLPASALLGEENKGFYYIMKE 287
Cdd:cd01152 160 YADWAWLLVRTDPEAPKHR-GISILLVDMDSPG-VTVRPIRSiNG--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 288 LPQERLLIADVAISAsefmFEETRNYVK--QRKAFGKTVAHLqtVQHKLAELKTHICVTRAFV-DNCLQLHEAKRLDsAT 364
Cdd:cd01152 236 LNFERVSIGGSAATF----FELLLARLLllTRDGRPLIDDPL--VRQRLARLEAEAEALRLLVfRLASALAAGKPPG-AE 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 365 ACMAKYWASELQNSVAYDCVQLHGGWG---YMWEYPIAKA-----YVDARVQPIYGGTNEIMKELIAREI 426
Cdd:cd01152 309 ASIAKLFGSELAQELAELALELLGTAAllrDPAPGAELAGrweadYLRSRATTIYGGTSEIQRNIIAERL 378
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
53-418 |
5.24e-45 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 160.38 E-value: 5.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 53 FSPEHDIFRKSVRKFFQEEviphhsEWEKA-GEVSR-----EVWEKA-GKQGLLGVNIAEHLGGIGGDLYSAAIVWEEqa 125
Cdd:PRK03354 5 LNDEQELFVAGIRELMASE------NWEAYfAECDRdsvypERFVKAlADMGIDSLLIPEEHGGLDAGFVTLAAVWME-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 126 YSNCSGPGFSIH---SGIvmSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKV 202
Cdd:PRK03354 77 LGRLGAPTYVLYqlpGGF--NTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 203 FISNGSLSDVVIVVAvtnHEAPSPAHGI-SLFLVENGMKGfIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGF 281
Cdd:PRK03354 155 FITSSAYTPYIVVMA---RDGASPDKPVyTEWFVDMSKPG-IKVTKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 282 YYIMKELPQERLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLD 361
Cdd:PRK03354 231 NRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 4501857 362 SATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIM 418
Cdd:PRK03354 311 SGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQ 367
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
52-426 |
1.86e-44 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 159.63 E-value: 1.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 52 IFSPEHDIFRKSVRKFFQEEVIPHHSE-WEKAgEVSREVWEKAGKQGLLGVNIAEHlGGIGGDLYSAAIVWEEQAYSNCS 130
Cdd:PLN02526 28 LLTPEEQALRKRVRECMEKEVAPIMTEyWEKA-EFPFHIIPKLGSLGIAGGTIKGY-GCPGLSITASAIATAEVARVDAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 131 GPGFS-IHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGSDWILNGSKVFISNGSL 209
Cdd:PLN02526 106 CSTFIlVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 210 SDVVIVVA---VTNHeapspahgISLFLVENGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKgFYYIMK 286
Cdd:PLN02526 186 ADVLVIFArntTTNQ--------INGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNS-FQDTNK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 287 ELPQERLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDSATAC 366
Cdd:PLN02526 257 VLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHAS 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4501857 367 MAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDarVQPIYG--GTNEIMKELIAREI 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 |
7.69e-44 |
|
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: 150.10 E-value: 7.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 278 NKGFYYIMKELPQERLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEA 357
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4501857 358 KRLDSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREI 426
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
152-418 |
1.26e-39 |
|
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: 146.75 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 152 EQIKHFIPQMTAGKC----IGAIAMTEPGAGSDLQGIKTNAKKDGSD-WILNGSKVFISNgSLSDVVIVVAVTnHEAPSP 226
Cdd:cd01154 129 EELKQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSGGGvYRLNGHKWFASA-PLADAALVLARP-EGAPAG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 227 AHGISLFLV----ENGMKGFIKGRKL-HKMGLKAQDTAELFFEDirlpASA-LLGEENKGFYYIMKELPQERLliaDVAI 300
Cdd:cd01154 207 ARGLSLFLVprllEDGTRNGYRIRRLkDKLGTRSVATGEVEFDD----AEAyLIGDEGKGIYYILEMLNISRL---DNAV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 301 SASEFM---FEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFV-DNCLQLHEAKRLDSATACMA-------K 369
Cdd:cd01154 280 AALGIMrraLSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTfRAARAFDRAAADKPVEAHMArlatpvaK 359
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 4501857 370 YWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIM 418
Cdd:cd01154 360 LIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
54-165 |
6.11e-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: 6.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 54 SPEHDIFRKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYSNCS-GP 132
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASvAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 4501857 133 GFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGK 165
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
61-424 |
9.65e-36 |
|
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: 135.60 E-value: 9.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 61 RKSVRKFFQEEVIPHHSE-----------WEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYS-- 127
Cdd:cd01155 7 RARVKAFMEEHVYPAEQEfleyyaeggdrWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRSff 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 128 -----NCSGPgfsiHSGiVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPG-AGSDLQGIKTNAKKDGSDWILNGSK 201
Cdd:cd01155 87 apevfNCQAP----DTG-NMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 202 VFISNGSLSD--VVIVVAVTNHEAPSPAHGISLFLVENGMKGFIKGRKLHKMGlkAQDT----AELFFEDIRLPASALLG 275
Cdd:cd01155 162 WWSSGAGDPRckIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFG--YDDAphghAEITFDNVRVPASNLIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 276 EENKGFYYIMKELPQERLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVdnclqLH 355
Cdd:cd01155 240 GEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLV-----LK 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4501857 356 EAKRLD---SATA----CMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAR 424
Cdd:cd01155 315 AAHMIDtvgNKAArkeiAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
169-264 |
1.08e-31 |
|
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: 116.23 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 169 AIAMTEPGAGSDLQGIKTNA-KKDGSDWILNGSKVFISNGSLSDVVIVVAVTnhEAPSPAHGISLFLVENGMKGFIKGRK 247
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLART--GGDDRHGGISLFLVPKDAPGVSVRRI 78
|
90
....*....|....*..
gi 4501857 248 LHKMGLKAQDTAELFFE 264
Cdd:pfam02770 79 ETKLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
75-427 |
2.21e-23 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 102.64 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 75 HHSEWEKAGEVS-----REVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEEQAYSNcsgPGFSIHSGI---VMSYIT 146
Cdd:PTZ00456 85 EGCVLLKDGNVTtpkgfKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATAN---WGFSMYPGLsigAANTLM 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 147 NHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKK--DGSdWILNGSKVFISNGS---LSDVVIVVAVTNH 221
Cdd:PTZ00456 162 AWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPsaDGS-YKITGTKIFISAGDhdlTENIVHIVLARLP 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 222 EAPSPAHGISLFLV------ENG----MKGFIKGRKLHKMGLKAQDTAELFFEDirlPASALLGEENKGFYYIMKELPQE 291
Cdd:PTZ00456 241 NSLPTTKGLSLFLVprhvvkPDGsletAKNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 292 RLLIADVAISASEFMFEETRNYVKQRKAF------------GKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQL----H 355
Cdd:PTZ00456 318 RVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNILFAKAVAEGGRALLLDVGRLldihA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 356 EAKRLDSATAC---------MAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMK-ELIARE 425
Cdd:PTZ00456 398 AAKDAATREALdheigfytpIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQAlDFIGRK 477
|
..
gi 4501857 426 IV 427
Cdd:PTZ00456 478 VL 479
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
120-424 |
1.52e-19 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 91.40 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 120 VWEEQAYsNCSGPgfsiHSGiVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPG-AGSDLQGIKTNAKKDGSDWILN 198
Cdd:PLN02876 510 VWAPQVF-NCGAP----DTG-NMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVIN 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 199 GSKVFISnGSLS---DVVIVVAVTNHEAPSPAHGiSLFLVENGMKGFIKGRKLHKMGLK--AQDTAELFFEDIRLPASAL 273
Cdd:PLN02876 584 GTKWWTS-GAMDprcRVLIVMGKTDFNAPKHKQQ-SMILVDIQTPGVQIKRPLLVFGFDdaPHGHAEISFENVRVPAKNI 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 274 LGEENKGFYYIMKELPQERLLIADVAISASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNC-- 351
Cdd:PLN02876 662 LLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAad 741
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4501857 352 -LQLHEAKRLDSATAcMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAR 424
Cdd:PLN02876 742 qLDRLGNKKARGIIA-MAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAK 814
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
38-427 |
5.13e-13 |
|
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: 70.82 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 38 TPSAKKLTDIGIRrifSPEHDIFRKSVRKFFQEEviPHHSEWEKAGEVSRE-VWEKAGKQGLLGVNIAEHLGGIGGDLYS 116
Cdd:cd01150 11 TFDWKALTHILEG---GEENLRRKREVERELESD--PLFQRELPSKHLSREeLYEELKRKAKTDVERMGELMADDPEKML 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 117 AAIVWEEQAYSNCSGPgFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKDGS--D 194
Cdd:cd01150 86 ALTNSLGGYDLSLGAK-LGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLtqE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 195 WILN-----GSKVFISN-GSLSDVVIVVAvtNHEAPSPAHGISLFLVE-------NGMKGFIKGRKLHKMGLKAQDTAEL 261
Cdd:cd01150 165 FVINtpdftATKWWPGNlGKTATHAVVFA--QLITPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNGFL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 262 FFEDIRLPASALLgeeNK-------GFYYIMKELPQERL-------------LIADVAISASEFMFEETRnYVKQRKAFG 321
Cdd:cd01150 243 QFRNVRIPRENLL---NRfgdvspdGTYVSPFKDPNKRYgamlgtrsggrvgLIYDAAMSLKKAATIAIR-YSAVRRQFG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 322 KT-------VAHLQTVQHKL-AELKTHIC---VTRAFVDN---CLQLHEAKRLDS-----ATACMAKYWASELQNSVAYD 382
Cdd:cd01150 319 PKpsdpevqILDYQLQQYRLfPQLAAAYAfhfAAKSLVEMyheIIKELLQGNSELlaelhALSAGLKAVATWTAAQGIQE 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 4501857 383 CVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIAREIV 427
Cdd:cd01150 399 CREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLL 443
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
132-424 |
1.77e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 59.85 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 132 PGFS-IHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKD--GSDWILNGSKVFISN-- 206
Cdd:PLN02443 96 PGYTdLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDpkTDEFVIHSPTLTSSKww 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 207 ----GSLSDVVIVVA--VTNHEapspAHGISLFLVE-----------NGMKGFIkGRKLHKMGLKAQDTAELFFEDIRLP 269
Cdd:PLN02443 176 pgglGKVSTHAVVYArlITNGK----DHGIHGFIVQlrslddhsplpGVTVGDI-GMKFGNGAYNTMDNGFLRFDHVRIP 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 270 ASALL------GEENKgfyYIMKELPQERL----------LIADVAISASEFMFEETRnYVKQRKAFGK-------TVAH 326
Cdd:PLN02443 251 RDQMLmrlskvTREGK---YVQSDVPRQLVygtmvyvrqtIVADASTALSRAVCIATR-YSAVRRQFGSqdggpetQVID 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 327 LQTVQHKLAELkthICVTRAF-------------VDNCLQLHEAKRLDSATACMAKYWAseLQNSVAYD----CVQLHGG 389
Cdd:PLN02443 327 YKTQQSRLFPL---LASAYAFrfvgewlkwlytdVTQRLEANDFSTLPEAHACTAGLKS--LTTSATADgieeCRKLCGG 401
|
330 340 350
....*....|....*....|....*....|....*...
gi 4501857 390 WGYMWEYPIAK---AYVDARVqpiYGGTNEIMKELIAR 424
Cdd:PLN02443 402 HGYLCSSGLPElfaVYVPACT---YEGDNVVLLLQVAR 436
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
295-416 |
3.41e-08 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 51.96 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 295 IADVAISASEFMFEETRNYVKQRK--AFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRLDS--------AT 364
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGkpvtpalrAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 4501857 365 ACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNE 416
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
77-232 |
2.14e-07 |
|
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: 52.71 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 77 SEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIVWEE--QAYSNCsGPGFSIHSGIVMSYITNhGSEEQI 154
Cdd:cd01163 15 AERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRElaAADSNI-AQALRAHFGFVEALLLA-GPEQFR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 155 KHFIPQMTAGKCIGAiAMTEPGaGSDLQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVVAVTNHEA------PSPAH 228
Cdd:cd01163 93 KRWFGRVLNGWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKlvfaavPTDRP 170
|
....
gi 4501857 229 GISL 232
Cdd:cd01163 171 GITV 174
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
78-391 |
9.71e-07 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 51.11 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 78 EWE---KAGEVSREVWEKAGKQGLLGVNIAEHLGGIGgdlYSAA----IVWEEQAYS----------NCSGPGfsihsgi 140
Cdd:PRK13026 99 DWDivqNRKDLPPEVWDYLKKEGFFALIIPKEYGGKG---FSAYanstIVSKIATRSvsaavtvmvpNSLGPG------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 141 vmSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDL-----QGIKTNAKKDGSDWI---LNGSKVFISNGSLSDv 212
Cdd:PRK13026 169 --ELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAgaipdTGIVCRGEFEGEEVLglrLTWDKRYITLAPVAT- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 213 VIVVAVTNHEapsPAH--------GISLFLVENGMKGFIKGRKLHKMGLKAQDtAELFFEDIRLPASALLGEEN---KGF 281
Cdd:PRK13026 246 VLGLAFKLRD---PDGllgdkkelGITCALIPTDHPGVEIGRRHNPLGMAFMN-GTTRGKDVFIPLDWIIGGPDyagRGW 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 282 YYIMKELPQERlliadvAIS-------ASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAEL--KTHIC-VTRAFVDNC 351
Cdd:PRK13026 322 RMLVECLSAGR------GISlpalgtaSGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIagNTYLLeAARRLTTTG 395
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 4501857 352 LQLHEAKRLDSAtacMAKYWASELQNSVAYDCVQLHGGWG 391
Cdd:PRK13026 396 LDLGVKPSVVTA---IAKYHMTELARDVVNDAMDIHAGKG 432
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
135-274 |
1.90e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 50.23 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 135 SIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSDLQGIKTNAKKD--GSDWILNGSKV---------- 202
Cdd:PTZ00460 96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDkqTNEFVIHTPSVeavkfwpgel 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 203 -FISNGSLSDVVIVVAVTNheapspaHGISLFLVE-------NGMKGFIKGRKLHKMGLKAQDTAELFFEDIRLPASALL 274
Cdd:PTZ00460 176 gFLCNFALVYAKLIVNGKN-------KGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLL 248
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
98-291 |
1.08e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 47.57 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 98 LLGVNIAEHLGGIGGDLYSAAIVWEEQAySNCSGPGFSI--HSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAmTEP 175
Cdd:PTZ00457 65 LYGARIATEYGGLGLGHTAHALIYEEVG-TNCDSKLLSTiqHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 176 GAGSDLQGIKTNAK-KDGSDWILNGSK-VFISNGSLSDVVIVVAVTN---HEAPSPAHGISLFLVENGMKGF-IKGRKLH 249
Cdd:PTZ00457 143 GCGSDISMNTTKASlTDDGSYVLTGQKrCEFAASATHFLVLAKTLTQtaaEEGATEVSRNSFFICAKDAKGVsVNGDSVV 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 4501857 250 -----------KMGLKAQDTAELFFEDIRLPASALLGeenkgfyyIMKELPQE 291
Cdd:PTZ00457 223 fentpaadvvgVVGEGFKDAMITLFTEQYLYAASLLG--------IMKRVVQE 267
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
164-418 |
2.73e-04 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 43.20 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 164 GKCIGaIAMTEPGAGSDLQGIKTNAKK-DGSDWILNGSKVFISNGSlSDVVIVVAVTNHeapspahGISLFLVE----NG 238
Cdd:PRK11561 177 GLLIG-MGMTEKQGGSDVLSNTTRAERlADGSYRLVGHKWFFSVPQ-SDAHLVLAQAKG-------GLSCFFVPrflpDG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 239 MKGFIKGRKLH-KMGLKAQDTAELFFEDirlpASA-LLGEENKGFYYIMKELPQERLliaDVAISASEFM---FEETRNY 313
Cdd:PRK11561 248 QRNAIRLERLKdKLGNRSNASSEVEFQD----AIGwLLGEEGEGIRLILKMGGMTRF---DCALGSHGLMrraFSVAIYH 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501857 314 VKQRKAFGKTVAHLQTVQHKLA----ELKTHIC----VTRAFvDNCLQLHEA--KRLDSATacmAKYWASELQNSVAYDC 383
Cdd:PRK11561 321 AHQRQVFGKPLIEQPLMRQVLSrmalQLEGQTAllfrLARAW-DRRADAKEAlwARLFTPA---AKFVICKRGIPFVAEA 396
|
250 260 270
....*....|....*....|....*....|....*
gi 4501857 384 VQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIM 418
Cdd:PRK11561 397 MEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIM 431
|
|
| |
