|
Name |
Accession |
Description |
Interval |
E-value |
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
67-439 |
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: 698.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 67 EEHDLFRQNVRRFFQEEVAPYHAQWEKAGEVSREVWEKAGEHGLLGVYTPEEHGGIGGDLLSAAIVWEEQMYSNCSGPGF 146
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 147 SLHSEIVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTFAKKDGTDWILNGSKVFITNGWMSDVVI 226
Cdd:cd01160 81 SLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 227 VVAVTDREAkTAAHGISLFLVDRGTKGYQKGRKLEKLGLKAQDTAELFFEDVRLPAEALLGQVNKGFYYLMNELPQERLL 306
Cdd:cd01160 161 VVARTGGEA-RGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 307 IAVMGLASCEFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGRAFIDSCLQLHSEKKLDSSTASMAKYWATD 386
Cdd:cd01160 240 IAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 41056265 387 LQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKELISRNIV 439
Cdd:cd01160 320 LQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
57-439 |
1.05e-154 |
|
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: 443.13 E-value: 1.05e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 57 MDIGtrriFSEEHDLFRQNVRRFFQEEVAPYHAQWEKAGEVSREVWEKAGEHGLLGVYTPEEHGGIGGDLLSAAIVWEEQ 136
Cdd:COG1960 1 MDFE----LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 137 MYSNCS-GPGFSLHSeIVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTFAKKDGTDWILNGSKVF 215
Cdd:COG1960 77 ARADASlALPVGVHN-GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 216 ITNGWMSDVVIVVAVTDREAKTaaHGISLFLVDRGTKGYQKGRKLEKLGLKAQDTAELFFEDVRLPAEALLGQVNKGFYY 295
Cdd:COG1960 156 ITNAPVADVILVLARTDPAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 296 LMNELPQERLLIAVMGLASCEFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGRAFIDSCLQLHSEKKLDSS 375
Cdd:COG1960 234 AMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAAL 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41056265 376 TASMAKYWATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKELISRNIV 439
Cdd:COG1960 314 EAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
67-438 |
4.03e-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: 349.64 E-value: 4.03e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 67 EEHDLFRQNVRRFFQEEVAPYHAQWEKAGEVSREVWEKAGEHGLLGVYTPEEHGGIGGDLLSAAIVWEE-QMYSNCSGPG 145
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEElAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 146 FSLHSEIVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTFAKKDGTDWILNGSKVFITNGWMSDVV 225
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 226 IVVAVTDREAKtaAHGISLFLVDRGTKGYQKGRKLEKLGLKAQDTAELFFEDVRLPAEALLGQVNKGFYYLMNELPQERL 305
Cdd:cd01158 161 IVFAVTDPSKG--YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 306 LIAVMGLASCEFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGRAFIDSCLQLHSEKKLDSSTASMAKYWAT 385
Cdd:cd01158 239 GIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFAS 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 41056265 386 DLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKELISRNI 438
Cdd:cd01158 319 EVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
65-440 |
6.18e-106 |
|
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: 318.59 E-value: 6.18e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 65 FSEEHDLFRQNVRRFFQEEVAPYHAQWEKAGEVSREVWEKAGEHGLLGVYTPEEHGGIGGDLLSAAIVWEEQMYSNCS-G 143
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 144 PGFSLHSEIVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTFAKKDGTDWILNGSKVFITNGWMSD 223
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 224 VVIVVAVTDREAKtaAHGISLFLVDRGTKGYQKGRKLEKLGLKAQDTAELFFEDVRLPAEALLGQVNKGFYYLMNELPQE 303
Cdd:cd01156 162 TLVVYAKTDPSAG--AHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 304 RLLIAVMGLASCEFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGRAFIDSCLQLHSEKKLDSSTASMAKYW 383
Cdd:cd01156 240 RLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILY 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 41056265 384 ATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKELISRNIVS 440
Cdd:cd01156 320 AAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
67-436 |
3.39e-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: 3.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 67 EEHDLFRQNVRRFFQEEVAPYHAQWEKAGEVSREVWEKAGEhgLLGVYTpeehggiggdllsaaivweeqmysncsgpgf 146
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGL--LLGAAL------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 147 slhseivmpyISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTFAKKDGTDWILNGSKVFITNGWMSDVVI 226
Cdd:cd00567 48 ----------LLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 227 VVAVTDREAKTAaHGISLFLVDRGTKGYQKGRKLEKLGLKAQDTAELFFEDVRLPAEALLGQVNKGFYYLMNELPQERLL 306
Cdd:cd00567 118 VLARTDEEGPGH-RGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 307 IAVMGLASCEFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGRAFI----DSCLQLHSEKKLDsstASMAKY 382
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLyraaWLLDQGPDEARLE---AAMAKL 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 41056265 383 WATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKELISR 436
Cdd:cd00567 274 FATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
66-441 |
2.38e-92 |
|
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: 283.95 E-value: 2.38e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 66 SEEHDLFRQNVRRFFQEEVAPYHAQWEKAGEVSREVWEKAGEHGLLGVYTPEEHGGIGGDLLSAAIVWEEQMYSNCSGPG 145
Cdd:cd01162 2 NEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 146 F-SLHSeIVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTFAKKDGTDWILNGSKVFITNGWMSDV 224
Cdd:cd01162 82 YiSIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 225 VIVVAVTDREAktaAHGISLFLVDRGTKGYQKGRKLEKLGLKAQDTAELFFEDVRLPAEALLGQVNKGFYYLMNELPQER 304
Cdd:cd01162 161 YVVMARTGGEG---PKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 305 LLIAVMGLASCEFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGRAFI-DSCLQLHSEKKLDSSTASMAKYW 383
Cdd:cd01162 238 LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVrRAASALDRGDPDAVKLCAMAKRF 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 41056265 384 ATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKELISRNIVSK 441
Cdd:cd01162 318 ATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
43-438 |
1.53e-78 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 249.41 E-value: 1.53e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 43 AAPFRPETSMAKTLMDIGTRRIFSEEHDLFRQNVRRFFQEEVAPYHAQWEKAGEVSREV--WEKAGEHGLLGVYTPEEHG 120
Cdd:PLN02519 4 SAAKARRRGLARRFSSSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 121 GIGGDLLSAAIVWEE-QMYSNCSGPGFSLHSEIVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTF 199
Cdd:PLN02519 84 GLGLGYLYHCIAMEEiSRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 200 AKKDGTDWILNGSKVFITNGWMSDVVIVVAVTDREAktAAHGISLFLVDRGTKGYQKGRKLEKLGLKAQDTAELFFEDVR 279
Cdd:PLN02519 164 AERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAA--GSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 280 LPAEALLGQVNKGFYYLMNELPQERLLIAVMGLASCEFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGRAF 359
Cdd:PLN02519 242 VPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSY 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41056265 360 IDSCLQLHSEKKLDSSTASMAKYWATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKELISRNI 438
Cdd:PLN02519 322 VYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
66-438 |
3.70e-77 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 244.96 E-value: 3.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 66 SEEHDLFRQNVRRFFQEEVAPYHAQWEKAGEVSREVWEKAGEHGLLGVyTPEEHGGIGGDLLSAAIVWEE--QMYSNCSG 143
Cdd:cd01151 14 TEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREveRVDSGYRS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 144 pGFSLHSEIVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTFAKKDGTDWILNGSKVFITNGWMSD 223
Cdd:cd01151 93 -FMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 224 VVIVVAVTDREAKtaahgISLFLVDRGTKGYQKGRKLEKLGLKAQDTAELFFEDVRLPAEALLGQVNkGFYYLMNELPQE 303
Cdd:cd01151 172 VFVVWARNDETGK-----IRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAE-GLRGPFKCLNNA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 304 RLLIAVMGLASCEFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGrafIDSCLQ---LHSEKKLDSSTASMA 380
Cdd:cd01151 246 RYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALG---LLACLRvgrLKDQGKATPEQISLL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 41056265 381 KYWATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKELISRNI 438
Cdd:cd01151 323 KRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAI 380
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
58-442 |
7.75e-77 |
|
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: 245.07 E-value: 7.75e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 58 DIGTRRIF----------SEEHDLFRQNVRRFFQEEVAPyhAQWEKAGEVSREVWEKAGEHGLLGVYTPEEHGGIGGDLL 127
Cdd:cd01161 10 DIVTKQVFpypsvlteeqTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 128 SAAIVWEEQMYSNCSGPGFSLHSEIVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTFAKK--DGT 205
Cdd:cd01161 88 QYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 206 DWILNGSKVFITNGWMSDVVIVVAVTDREAKTAA--HGISLFLVDRGTKGYQKGRKLEKLGLKAQDTAELFFEDVRLPAE 283
Cdd:cd01161 168 HYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSvkDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 284 ALLGQVNKGFYYLMNELPQERLLIAVMGLASCEFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGR--AFID 361
Cdd:cd01161 248 NVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATEsmAYMT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 362 SCL---QLHSEKKLDsstASMAKYWATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKELISRNI 438
Cdd:cd01161 328 SGNmdrGLKAEYQIE---AAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTG 404
|
....
gi 41056265 439 VSKK 442
Cdd:cd01161 405 LQHA 408
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
65-441 |
2.81e-74 |
|
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: 237.48 E-value: 2.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 65 FSEEHDLFRQNVRRFFQEEVAPYHAQWEKAGEVSREVWEKAGEHGLLGVYTPEEHGGIGGDLLSAAIVWEEQMYSnCSG- 143
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYG-CTGv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 144 -PGFSLHSEIVMP-YIShyGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTFAKKDGTDWILNGSKVFITNGWM 221
Cdd:cd01157 80 qTAIEANSLGQMPvIIS--GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 222 SDVVIVVAVTDREAKT-AAHGISLFLVDRGTKGYQKGRKLEKLGLKAQDTAELFFEDVRLPAEALLGQVNKGFYYLMNEL 300
Cdd:cd01157 158 ANWYFLLARSDPDPKCpASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 301 PQERLLIAVMGLASCEFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGR-AFIDSCLQLHSEKKlDSSTASM 379
Cdd:cd01157 238 DKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARlAYQRAAWEVDSGRR-NTYYASI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41056265 380 AKYWATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKELISRNIVSK 441
Cdd:cd01157 317 AKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
43-439 |
4.34e-73 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 235.22 E-value: 4.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 43 AAPFRPETSMAKTLMDIGTRrifSEEHDLFRQNVRRFFQEEVAPYHAQWEKAGEVSREVWEKAGEHGLLGVYTPEEHGGI 122
Cdd:PTZ00461 18 WTAAATMTSASRAFMDLYNP---TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 123 GGDLLSAAIVWEEqmYSNCSgPGFSL----HSEIVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKT 198
Cdd:PTZ00461 95 GMDAVAAVIIHHE--LSKYD-PGFCLaylaHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 199 FAKKDGT-DWILNGSKVFITNGWMSDVVIVVAVTDREaktaahgISLFLVDRGTKGYQKGRKLEKLGLKAQDTAELFFED 277
Cdd:PTZ00461 172 TAKKDSNgNYVLNGSKIWITNGTVADVFLIYAKVDGK-------ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 278 VRLPAEALLGQVNKGFYYLMNELPQERLLIAVMGLASCEFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGR 357
Cdd:PTZ00461 245 VVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 358 AFIDSCLQLHSEKKLDSSTASMAKYWATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKELISRN 437
Cdd:PTZ00461 325 ALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKD 404
|
..
gi 41056265 438 IV 439
Cdd:PTZ00461 405 LL 406
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
66-441 |
7.68e-61 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 202.65 E-value: 7.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 66 SEEHDL----FRQNVRRFFQEEvapYHAQWEKAGEVSREVWEKAGEHG--LLGVytPEEHGGIGGDLLSAAIVWEEqmYS 139
Cdd:PRK12341 6 TEEQELllasIRELITRNFPEE---YFRTCDENGTYPREFMRALADNGisMLGV--PEEFGGTPADYVTQMLVLEE--VS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 140 NCSGPGFSLHSEIVMPYISHYGSKAQIERYIPQ-MAAGKCIGAIAMTEPGAGSD-LQGAKTFAKKDGTdWILNGSKVFIT 217
Cdd:PRK12341 79 KCGAPAFLITNGQCIHSMRRFGSAEQLRKTAEStLETGDPAYALALTEPGAGSDnNSATTTYTRKNGK-VYLNGQKTFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 218 NGWMSDVVIVVAvTDREAKTAAHGISLFLVDRGTKGYqKGRKLEKLGLKAQDTAELFFEDVRLPAEALLGQVNKGFYYLM 297
Cdd:PRK12341 158 GAKEYPYMLVLA-RDPQPKDPKKAFTLWWVDSSKPGI-KINPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 298 NELPQERLLIA--VMGLASCEfmFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGRAFI-DSCLQLHSEKKLDS 374
Cdd:PRK12341 236 YNFEMERLINAarSLGFAECA--FEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVyKVAWQADNGQSLRT 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41056265 375 STAsMAKYWATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKELISRNIVSK 441
Cdd:PRK12341 314 SAA-LAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKD 379
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
72-441 |
2.34e-56 |
|
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: 190.64 E-value: 2.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 72 FRQNVRRFFQEEVAP-----YHAQWEKAGEVSREvWEKA-GEHGLLGVYTPEEHGGIGGDLLSAAIVWEEQMYSNCSGPG 145
Cdd:cd01152 6 FRAEVRAWLAAHLPPelreeSALGYREGREDRRR-WQRAlAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 146 FSLHSEIVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTFAKKDGTDWILNGSKVFITNGWMSDVV 225
Cdd:cd01152 85 NQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 226 IVVAVTDREAKTAAhGISLFLVDRGTKGYQKgRKLEKLgLKAQDTAELFFEDVRLPAEALLGQVNKGFYYLMNELPQERL 305
Cdd:cd01152 165 WLLVRTDPEAPKHR-GISILLVDMDSPGVTV-RPIRSI-NGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 306 LIAvmGLASCefMFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGRAFIDSCLQLHSEKKLDSSTASMAKYWAT 385
Cdd:cd01152 242 SIG--GSAAT--FFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGS 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41056265 386 DLQNRVATQCLQLHGGWGYMwEYPIAKAFADARVQ---------PIYGGTNEIMkelisRNIVSK 441
Cdd:cd01152 318 ELAQELAELALELLGTAALL-RDPAPGAELAGRWEadylrsratTIYGGTSEIQ-----RNIIAE 376
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
65-430 |
7.73e-47 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 165.77 E-value: 7.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 65 FSEEHDLFRQNVRRFF-QEEVAPYHAQWEKAGEVSrEVWEKA-GEHGLLGVYTPEEHGGIGGDLLSAAIVWEEqmYSNCS 142
Cdd:PRK03354 5 LNDEQELFVAGIRELMaSENWEAYFAECDRDSVYP-ERFVKAlADMGIDSLLIPEEHGGLDAGFVTLAAVWME--LGRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 143 GPGFSLHSeivMPY----ISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQG-AKTFAKKDGTDWiLNGSKVFIT 217
Cdd:PRK03354 82 APTYVLYQ---LPGgfntFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSlKTTYTRRNGKVY-LNGSKCFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 218 NGWMSDVVIVVAvtdREAKTAAHGI-SLFLVDRGTKGYQKGrKLEKLGLKAQDTAELFFEDVRLPAEALLGQVNKGFYYL 296
Cdd:PRK03354 158 SSAYTPYIVVMA---RDGASPDKPVyTEWFVDMSKPGIKVT-KLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 297 MNELPQERLLIAVM--GLASCEfmFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGRAFIDSCLQLHSEKKLDS 374
Cdd:PRK03354 234 KEEFDHERFLVALTnyGTAMCA--FEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITS 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 41056265 375 STASMAKYWATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIM 430
Cdd:PRK03354 312 GDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQ 367
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
107-439 |
6.17e-46 |
|
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: 163.71 E-value: 6.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 107 EHGLLGVYTPEEHGGIGgdlLSAAIVW--EEQMYSNCSGpgfslhseIVMPYISH--------YGSKAQIERYIPQMAAG 176
Cdd:cd01153 47 EAGWMALGVPEEYGGQG---LPITVYSalAEIFSRGDAP--------LMYASGTQgaaatllaHGTEAQREKWIPRLAEG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 177 KCIGAIAMTEPGAGSDLQGAKTFAKKDGT-DWILNGSKVFITNG--WMSD--VVIVVAVTDrEAKTAAHGISLFLVDR-- 249
Cdd:cd01153 116 EWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGehDMSEniVHLVLARSE-GAPPGVKGLSLFLVPKfl 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 250 --GTK-GYQKGRKLEKLGLKAQDTAELFFEDVRLPaeaLLGQVNKGFYYLMNELPQERLLIAVMGLASCEFMFEESRNYV 326
Cdd:cd01153 195 ddGERnGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 327 MQRKAFGR--------TIADLQVVQHKLAELKTEICVGRA-------FIDSCLQLHSEKkLDSSTAS--------MAKYW 383
Cdd:cd01153 272 KERKQGGDlikaapavTIIHHPDVRRSLMTQKAYAEGSRAldlytatVQDLAERKATEG-EDRKALSaladlltpVVKGF 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 41056265 384 ATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIM-KELISRNIV 439
Cdd:cd01153 351 GSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQaLDLIGRKIV 407
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
42-438 |
1.23e-45 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 163.10 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 42 TAAPFRPETSMAKTLMDIGTrrifSEEHDLfRQNVRRFFQEEVAPYHAQ-WEKAgEVSREVWEKAGEHGLLGvYTPEEHG 120
Cdd:PLN02526 11 PASIFPPSVSDYYQFDDLLT----PEEQAL-RKRVRECMEKEVAPIMTEyWEKA-EFPFHIIPKLGSLGIAG-GTIKGYG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 121 GIGGDLLSAAIVWEEQMYSNCSGPGFSL-HSEIVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTF 199
Cdd:PLN02526 84 CPGLSITASAIATAEVARVDASCSTFILvHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 200 AKKDGTDWILNGSKVFITNGWMSDVVIVVAvtdREAKTaaHGISLFLVDRGTKGYqKGRKLE-KLGLKAQDTAELFFEDV 278
Cdd:PLN02526 164 ATKVEGGWILNGQKRWIGNSTFADVLVIFA---RNTTT--NQINGFIVKKGAPGL-KATKIEnKIGLRMVQNGDIVLKDV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 279 RLPAEALLGQVNKgFYYLMNELPQERLLIAVMGLASCEFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEI----C 354
Cdd:PLN02526 238 FVPDEDRLPGVNS-FQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIqamfL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 355 VGRAFidsClQLHSEKKLDSSTASMAKYWATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADarVQPIYG--GTNEIMKE 432
Cdd:PLN02526 317 VGWRL---C-KLYESGKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCD--LEPIYTyeGTYDINAL 390
|
....*.
gi 41056265 433 LISRNI 438
Cdd:PLN02526 391 VTGREI 396
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
290-438 |
3.03e-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: 151.64 E-value: 3.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 290 NKGFYYLMNELPQERLLIAVMGLASCEFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELKTEICVGRAFIDSCLQLHSE 369
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41056265 370 KKLDSSTASMAKYWATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKELISRNI 438
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 ... |
66-177 |
2.28e-43 |
|
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: 147.99 E-value: 2.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 66 SEEHDLFRQNVRRFFQEEVAPYHAQWEKAGEVSREVWEKAGEHGLLGVYTPEEHGGIGGDLLSAAIVWEEQMYSNCS-GP 144
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASvAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 41056265 145 GFSLHSEIVMPYISHYGSKAQIERYIPQMAAGK 177
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
179-430 |
6.61e-36 |
|
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: 137.12 E-value: 6.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 179 IGAIAMTEPGAGSDLQGAKTFAKKDGTD-WILNGSKVFiTNGWMSDVVIVVAVTDrEAKTAAHGISLFLVDR----GTK- 252
Cdd:cd01154 148 LGGTWMTEKQGGSDLGANETTAERSGGGvYRLNGHKWF-ASAPLADAALVLARPE-GAPAGARGLSLFLVPRlledGTRn 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 253 GYQKGRKLEKLGLKAQDTAELFFEDvrlpAEA-LLGQVNKGFYYLMNELPQERLLIAVMGLASCEFMFEESRNYVMQRKA 331
Cdd:cd01154 226 GYRIRRLKDKLGTRSVATGEVEFDD----AEAyLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 332 FGRTIADLQVVQHKLAELKTEICVGRAFI-DSCLQLHSEKKLDSSTASMA-------KYWATDLQNRVATQCLQLHGGWG 403
Cdd:cd01154 302 FGKPLIDHPLMRRDLAEMEVDVEAATALTfRAARAFDRAAADKPVEAHMArlatpvaKLIACKRAAPVTSEAMEVFGGNG 381
|
250 260
....*....|....*....|....*..
gi 41056265 404 YMWEYPIAKAFADARVQPIYGGTNEIM 430
Cdd:cd01154 382 YLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
73-437 |
1.60e-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: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 73 RQNVRRFFQEEVAP----YHAQWEKAG-------EVSREVWEKAGEHGLLGVYTPEEHGGIGGDLLSAAIVWEEQMYS-- 139
Cdd:cd01155 7 RARVKAFMEEHVYPaeqeFLEYYAEGGdrwwtppPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRSff 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 140 -----NCSGPGFSlhseiVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPG-AGSDLQGAKTFAKKDGTDWILNGSK 213
Cdd:cd01155 87 apevfNCQAPDTG-----NMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 214 VFITNGWMSD--VVIVVAVTDREAKTAAHGISLFLVDRGTKGYQKGRKLEKLGlkAQDT----AELFFEDVRLPAEALLG 287
Cdd:cd01155 162 WWSSGAGDPRckIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFG--YDDAphghAEITFDNVRVPASNLIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 288 QVNKGFyylmnELPQERL-------LIAVMGLASC--EFMFEESRnyvmQRKAFGRTIADLQVVQHKLAELKTEICVGRA 358
Cdd:cd01155 240 GEGRGF-----EIAQGRLgpgrihhCMRLIGAAERalELMCQRAV----SREAFGKKLAQHGVVAHWIAKSRIEIEQARL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 359 FidsCLQL-HSEKKLDSSTA----SMAKYWATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKEL 433
Cdd:cd01155 311 L---VLKAaHMIDTVGNKAArkeiAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRS 387
|
....
gi 41056265 434 ISRN 437
Cdd:cd01155 388 IARM 391
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
181-276 |
6.45e-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: 111.60 E-value: 6.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 181 AIAMTEPGAGSDLQGAKTFA-KKDGTDWILNGSKVFITNGWMSDVVIVVAVTDREakTAAHGISLFLVDRGTKGYQKGRK 259
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGD--DRHGGISLFLVPKDAPGVSVRRI 78
|
90
....*....|....*..
gi 41056265 260 LEKLGLKAQDTAELFFE 276
Cdd:pfam02770 79 ETKLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
90-442 |
2.28e-22 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 99.94 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 90 QWEKAGEVS-----REVWEKAGEHGLLGVYTPEEHGGIGGDLlSAAIVWEEQMYSncSGPGFSLHSEI---VMPYISHYG 161
Cdd:PTZ00456 88 VLLKDGNVTtpkgfKEAYQALKAGGWTGISEPEEYGGQALPL-SVGFITRELMAT--ANWGFSMYPGLsigAANTLMAWG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 162 SKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTFAKK--DGTdWILNGSKVFITNG---WMSDVVIVVAVTDREAK 236
Cdd:PTZ00456 165 SEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPsaDGS-YKITGTKIFISAGdhdLTENIVHIVLARLPNSL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 237 TAAHGISLFLVDR------GTKGYQKGRK---LE-KLGLKAQDTAELFFEDvrlPAEALLGQVNKGFYYLMNELPQERLL 306
Cdd:PTZ00456 244 PTTKGLSLFLVPRhvvkpdGSLETAKNVKcigLEkKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 307 IAVMGLASCEFMFEESRNYVMQR-------------KAFGRTIADLQVVQHKL-AELKTEicVGRAF---IDSCLQLHSE 369
Cdd:PTZ00456 321 TALEGVCHAELAFQNALRYARERrsmralsgtkepeKPADRIICHANVRQNILfAKAVAE--GGRALlldVGRLLDIHAA 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 370 KKLDSSTASM----------AKYWATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMK-ELISRNI 438
Cdd:PTZ00456 399 AKDAATREALdheigfytpiAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQAlDFIGRKV 478
|
....
gi 41056265 439 VSKK 442
Cdd:PTZ00456 479 LSLK 482
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
132-429 |
7.55e-21 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 95.63 E-value: 7.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 132 VWEEQMYsNCSGPGFSlhseiVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPG-AGSDLQGAKTFAKKDGTDWILN 210
Cdd:PLN02876 510 VWAPQVF-NCGAPDTG-----NMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVIN 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 211 GSKvFITNGWMS---DVVIVVAVTDREAktAAHGI-SLFLVDRGTKGYQKGRKLEKLGLK--AQDTAELFFEDVRLPAEA 284
Cdd:PLN02876 584 GTK-WWTSGAMDprcRVLIVMGKTDFNA--PKHKQqSMILVDIQTPGVQIKRPLLVFGFDdaPHGHAEISFENVRVPAKN 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 285 LLGQVNKGFyylmnELPQERL----LIAVMGLASC-----EFMFEESrnyvMQRKAFGRTIADLQVVQHKLAELKTEICV 355
Cdd:PLN02876 661 ILLGEGRGF-----EIAQGRLgpgrLHHCMRLIGAaergmQLMVQRA----LSRKAFGKLIAQHGSFLSDLAKCRVELEQ 731
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41056265 356 GRAFIDSC---LQLHSEKKLDSSTAsMAKYWATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEI 429
Cdd:PLN02876 732 TRLLVLEAadqLDRLGNKKARGIIA-MAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
98-403 |
8.19e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 70.37 E-value: 8.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 98 SREVWEKAGEHGLLGVYTPEEHGG--------------IGGDLLSAAIVweeQMYSNCSGPGfslhsEIVMpyisHYGSK 163
Cdd:PRK13026 110 PPEVWDYLKKEGFFALIIPKEYGGkgfsayanstivskIATRSVSAAVT---VMVPNSLGPG-----ELLT----HYGTQ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 164 AQIERYIPQMAAGKCIGAIAMTEPGAGSDL-----QGAKTFAKKDGTDWI---LNGSKVFITNGWMSDVV-IVVAVTDRE 234
Cdd:PRK13026 178 EQKDYWLPRLADGTEIPCFALTGPEAGSDAgaipdTGIVCRGEFEGEEVLglrLTWDKRYITLAPVATVLgLAFKLRDPD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 235 A---KTAAHGISLFLVDRGTKGYQKGRKLEKLGLKAQDtAELFFEDVRLPAEALLG---QVNKGFYYLMNELPQER-LLI 307
Cdd:PRK13026 258 GllgDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMN-GTTRGKDVFIPLDWIIGgpdYAGRGWRMLVECLSAGRgISL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 308 AVMGLASCEFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELkteicVGRAF-IDSCLQLHS----EKKLDSSTASMAKY 382
Cdd:PRK13026 337 PALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARI-----AGNTYlLEAARRLTTtgldLGVKPSVVTAIAKY 411
|
330 340
....*....|....*....|.
gi 41056265 383 WATDLQNRVATQCLQLHGGWG 403
Cdd:PRK13026 412 HMTELARDVVNDAMDIHAGKG 432
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
45-441 |
9.08e-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: 70.05 E-value: 9.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 45 PFRPETSMA----KTLMDIGtrrIFSEEHDLFRQNVRR------FFQEEVAPYHAQWEKAGEVSREVWEKAGEHGL-LGV 113
Cdd:cd01150 2 DLDKERASAtfdwKALTHIL---EGGEENLRRKREVERelesdpLFQRELPSKHLSREELYEELKRKAKTDVERMGeLMA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 114 YTPEEHGGIGGDLLsaaivweeqMYSNCSGPGFSLHSEIVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDL 193
Cdd:cd01150 79 DDPEKMLALTNSLG---------GYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 194 QGAKTFAKKDGT--DWILN-----GSKVFITN-GWMSDVVIVVAVTDREAKTaaHGISLFLV---DRGT----KGYQKGR 258
Cdd:cd01150 150 QGLETTATYDPLtqEFVINtpdftATKWWPGNlGKTATHAVVFAQLITPGKN--HGLHAFIVpirDPKThqplPGVTVGD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 259 KLEKLGLKAQDTAELFFEDVRLPAEALL---GQV-------------NKGFYYLMNELPQERLLIAVMGLASCEFMFEES 322
Cdd:cd01150 228 IGPKMGLNGVDNGFLQFRNVRIPRENLLnrfGDVspdgtyvspfkdpNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 323 RNYVMQRKAFGRT-------IADLQVVQHKL-AELKTEIC---VGRAFID---SCLQLHSEKKLDSST-----ASMAKYW 383
Cdd:cd01150 308 IRYSAVRRQFGPKpsdpevqILDYQLQQYRLfPQLAAAYAfhfAAKSLVEmyhEIIKELLQGNSELLAelhalSAGLKAV 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 41056265 384 ATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNEIMKELISRNIVSK 441
Cdd:cd01150 388 ATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKK 445
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
100-403 |
3.34e-08 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 55.98 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 100 EVWEKAGEHGLLGVYTPEEHGGIG-----------------GDLlsAAIVweeqMYSNCSGPGfslhsEIVMpyisHYGS 162
Cdd:PRK09463 113 EVWQFIKEHGFFGMIIPKEYGGLEfsayahsrvlqklasrsGTL--AVTV----MVPNSLGPG-----ELLL----HYGT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 163 KAQIERYIPQMAAGKCIGAIAMTEPGAGSD--------------LQGAKTFAKKdgtdwiLNGSKVFITNGWMSDVV-IV 227
Cdd:PRK09463 178 DEQKDHYLPRLARGEEIPCFALTSPEAGSDagsipdtgvvckgeWQGEEVLGMR------LTWNKRYITLAPIATVLgLA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 228 VAVTDRE---AKTAAHGISLFLVDRGTKGYQKGRKLEKLGlkaqdtaELFF------EDVRLPAEALLG---QVNKGFYY 295
Cdd:PRK09463 252 FKLYDPDgllGDKEDLGITCALIPTDTPGVEIGRRHFPLN-------VPFQngptrgKDVFIPLDYIIGgpkMAGQGWRM 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 296 LMNELPQERlLIAVMGLASC--EFMFEESRNYVMQRKAFGRTIADLQVVQHKLAELkteicVGRAFIDSCLQLHSEKKLD 373
Cdd:PRK09463 325 LMECLSVGR-GISLPSNSTGgaKLAALATGAYARIRRQFKLPIGKFEGIEEPLARI-----AGNAYLMDAARTLTTAAVD 398
|
330 340 350
....*....|....*....|....*....|....*
gi 41056265 374 -----SSTASMAKYWATDLQNRVATQCLQLHGGWG 403
Cdd:PRK09463 399 lgekpSVLSAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
82-290 |
4.83e-08 |
|
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: 54.64 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 82 EEVAPYHAQWEKAGEVSREVWEKAGEHGLLGVYTPEEHGGIGGDLLSAAIVWEE--QMYSNCsGPGFSLHSEIVMPyISH 159
Cdd:cd01163 8 ARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRElaAADSNI-AQALRAHFGFVEA-LLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 160 YGSKAQIERYIPQMAAGKCIGAiAMTEPGaGSDLQGAKTFAKKDGTDWILNGSKVFITNGWMSDVVIVVAVTDREAKTAA 239
Cdd:cd01163 86 AGPEQFRKRWFGRVLNGWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKLVFA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 41056265 240 hgislfLVDRGTKGYQKGRKLEKLGLKAQDTAELFFEDVRLPAEALLGQVN 290
Cdd:cd01163 164 ------AVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPN 208
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
147-286 |
1.07e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 54.08 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 147 SLHSEIVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTFAKKD--GTDWILNGSKVFITNGW---- 220
Cdd:PTZ00460 96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDkqTNEFVIHTPSVEAVKFWpgel 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41056265 221 --MSDVVIVVAVTDREAKTaaHGISLFLV---DRGT----KGYQKGRKLEKLGLKAQDTAELFFEDVRLPAEALL 286
Cdd:PTZ00460 176 gfLCNFALVYAKLIVNGKN--KGVHPFMVrirDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLL 248
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
308-428 |
1.95e-07 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 49.65 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 308 AVMGLAscEFMFEESRNYVMQRK--AFGRTIADLQVVQHKLAELKTEI-----CVGRAFIDSCLQLHSEKKLDSST---A 377
Cdd:pfam08028 5 AALGAA--RAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIdaarlLLERAAARIEAAAAAGKPVTPALraeA 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 41056265 378 SMAKYWATDLQNRVATQCLQLHGGWGYMWEYPIAKAFADARVQPIYGGTNE 428
Cdd:pfam08028 83 RRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
144-303 |
1.77e-04 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 44.06 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 144 PGFS-LHSEIVMPYISHYGSKAQIERYIPQMAAGKCIGAIAMTEPGAGSDLQGAKTFAKKD-GTDWILNGSKVFITNGW- 220
Cdd:PLN02443 96 PGYTdLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDpKTDEFVIHSPTLTSSKWw 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056265 221 ------MSDVVIVVA--VTDREaktaAHGISLFLVD-RGTKGYQK---------GRKLEKLGLKAQDTAELFFEDVRLPA 282
Cdd:PLN02443 176 pgglgkVSTHAVVYArlITNGK----DHGIHGFIVQlRSLDDHSPlpgvtvgdiGMKFGNGAYNTMDNGFLRFDHVRIPR 251
|
170 180
....*....|....*....|....
gi 41056265 283 EALL---GQVNKGFYYLMNELPQE 303
Cdd:PLN02443 252 DQMLmrlSKVTREGKYVQSDVPRQ 275
|
|
| |
