|
Name |
Accession |
Description |
Interval |
E-value |
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
9-381 |
0e+00 |
|
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: 676.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 9 LNEDQRAIQEMARDFSRDKIAPFALEWDEKEHFPVDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEALASGCPAVS 88
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 89 AFISIHNMASWMIDRFGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGTDFVLNGTKQFISGAGTSDL 168
Cdd:cd01162 81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 169 YLVMARTGGDGAAGVSCFLVPKDAPGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMIGDEGQGFKIAMMGLDGGRLNI 248
Cdd:cd01162 161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 249 GACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDAKAHDATRWCAMAKRFATD 328
Cdd:cd01162 241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 522082706 329 TGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDLL 381
Cdd:cd01162 321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALL 373
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
7-384 |
1.89e-167 |
|
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: 473.17 E-value: 1.89e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 7 FDLNEDQRAIQEMARDFSRDKIAPFALEWDEKEHFPVDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEALASGCPA 86
Cdd:COG1960 3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 87 VSAFISIHNMASWMIDRFGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGTDFVLNGTKQFISGAGTS 166
Cdd:COG1960 83 LALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 167 DLYLVMARTGGD-GAAGVSCFLVPKDAPGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMIGDEGQGFKIAMMGLDGGR 245
Cdd:COG1960 163 DVILVLARTDPAaGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 246 LNIGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDAkAHDATRWCAMAKRF 325
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDA-GEDAALEAAMAKLF 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 522082706 326 ATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDLLKGG 384
Cdd:COG1960 322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRP 380
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
11-382 |
1.11e-156 |
|
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: 445.56 E-value: 1.11e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 11 EDQRAIQEMARDFSRDKIAPFALEWDEKEHFPVDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEALASGCPAVSAF 90
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 91 ISIHN-MASWMIDRFGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGTDFVLNGTKQFISGAGTSDLY 169
Cdd:cd01158 81 VSVHNsLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 170 LVMARTGGD-GAAGVSCFLVPKDAPGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMIGDEGQGFKIAMMGLDGGRLNI 248
Cdd:cd01158 161 IVFAVTDPSkGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 249 GACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDAKaHDATRWCAMAKRFATD 328
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNG-EPFIKEAAMAKLFASE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 522082706 329 TGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDLLK 382
Cdd:cd01158 320 VAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
11-378 |
6.72e-128 |
|
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: 370.85 E-value: 6.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 11 EDQRAIQEMARDFSRDKIAPFALEWDEKEHFPVDVMREAAALgmggiyvrddvggtglgrldaalifealasgcpavsaf 90
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLL-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 91 isihnMASWMIDRFGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGTDFVLNGTKQFISGAGTSDLYL 170
Cdd:cd00567 43 -----LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 171 VMARTGGDGAA--GVSCFLVPKDAPGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMIGDEGQGFKIAMMGLDGGRLNI 248
Cdd:cd00567 118 VLARTDEEGPGhrGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 249 GACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDAKAHDATRWCAMAKRFATD 328
Cdd:cd00567 198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATE 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 522082706 329 TGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISR 378
Cdd:cd00567 278 AAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
11-381 |
7.30e-112 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 331.77 E-value: 7.30e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 11 EDQRAIQEMARDFSRDKIAPFALEWDEKEHFPVDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEALA-SGCpaVSA 89
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELArAGG--SGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 90 FISIHN-MASWMIDRFGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGTDFVLNGTKQFISGAGTSDL 168
Cdd:cd01160 79 GLSLHTdIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 169 YLVMARTGGD--GAAGVSCFLVPKDAPGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMIGDEGQGFKIAMMGLDGGRL 246
Cdd:cd01160 159 VIVVARTGGEarGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 247 NIGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDAKAHDATRWCaMAKRFA 326
Cdd:cd01160 239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEAS-MAKYWA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 522082706 327 TDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDLL 381
Cdd:cd01160 318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
9-381 |
1.96e-110 |
|
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: 328.39 E-value: 1.96e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 9 LNEDQRAIQEMARDFSRDKIAPFALEWDEKEHFPVDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEALASGCPAVS 88
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 89 AFISIHNMASWMIDRFGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGTDFVLNGTKQFISGAGTSDL 168
Cdd:cd01157 81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 169 YLVMARTGGDGAAGVS----CFLVPKDAPGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMIGDEGQGFKIAMMGLDGG 244
Cdd:cd01157 161 YFLLARSDPDPKCPASkaftGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 245 RLNIGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDAKAHDaTRWCAMAKR 324
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRN-TYYASIAKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 522082706 325 FATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDLL 381
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
8-382 |
3.45e-108 |
|
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: 322.44 E-value: 3.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 8 DLNEDQRAIQEMARDFSRDKIAPFALEWDEKEHFPVDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEALASGCPAV 87
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 88 SAFISIH-NMASWMIDRFGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGTDFVLNGTKQFISGAGTS 166
Cdd:cd01156 81 ALSYGAHsNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 167 DLYLVMARTGGD-GAAGVSCFLVPKDAPGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMIGDEGQGFKIAMMGLDGGR 245
Cdd:cd01156 161 DTLVVYAKTDPSaGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 246 LNIGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDaKAHDATRWCAMAKRF 325
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACD-RGNMDPKDAAGVILY 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 522082706 326 ATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDLLK 382
Cdd:cd01156 320 AAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
8-382 |
2.52e-100 |
|
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: 303.62 E-value: 2.52e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 8 DLNEDQRAIQEMARDFSRDKIAPFALewDEKEHFPVDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEALASGCpAV 87
Cdd:cd01161 26 EQTEELNMLVGPVEKFFEEVNDPAKN--DQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDL-GF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 88 SAFISIH-NMASWMIDRFGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVK--DGTDFVLNGTKQFISGAG 164
Cdd:cd01161 103 SVTLGAHqSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWITNGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 165 TSDLYLVMART-----GGDGAAGVSCFLVPKDAPGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMIGDEGQGFKIAMM 239
Cdd:cd01161 183 IADIFTVFAKTevkdaTGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 240 GLDGGRLNIGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDAKA-HDATRW 318
Cdd:cd01161 263 ILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLkAEYQIE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522082706 319 CAMAKRFATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDLLK 382
Cdd:cd01161 343 AAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQ 406
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
9-378 |
7.15e-78 |
|
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: 7.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 9 LNEDQRAIQEMARDFSRDKIAPFALEWDEKEHFPVDVMREAAALGMGGIYVRDdVGGTGLGRLDAALIFEALASGCPAVS 88
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKG-YGCAGLSSVAYGLIAREVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 89 AFISIH-NMASWMIDRFGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGTDFVLNGTKQFISGAGTSD 167
Cdd:cd01151 92 SFMSVQsSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 168 LYLVMARTGGDGaaGVSCFLVPKDAPGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMIgDEGQGFKIAMMGLDGGRLN 247
Cdd:cd01151 172 VFVVWARNDETG--KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNARYG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 248 IGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAArTLLYKAACKLDAKAHDATRWCAMAKRFAT 327
Cdd:cd01151 249 IAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALG-LLACLRVGRLKDQGKATPEQISLLKRNNC 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 522082706 328 DTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISR 378
Cdd:cd01151 328 GKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
9-382 |
1.09e-70 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 227.07 E-value: 1.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 9 LNEDQRAIQEMARDFSRDKIAPFALEWDEKEHFP--VDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEALASGCPA 86
Cdd:PLN02519 26 FDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 87 VSAFISIH-NMASWMIDRFGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGTDFVLNGTKQFISGAGT 165
Cdd:PLN02519 106 VGLSYGAHsNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 166 SDLYLVMARTG-GDGAAGVSCFLVPKDAPGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMIGDEGQGFKIAMMGLDGG 244
Cdd:PLN02519 186 AQTLVVYAKTDvAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 245 RLNIGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDAKAHDaTRWCAMAKR 324
Cdd:PLN02519 266 RLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVD-RKDCAGVIL 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 522082706 325 FATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDLLK 382
Cdd:PLN02519 345 CAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
7-382 |
5.38e-70 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 224.61 E-value: 5.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 7 FDLNEDQRAIQE-----MARDFSRDKIApfalEWDEKEHFPVDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEALA 81
Cdd:PRK12341 3 FSLTEEQELLLAsirelITRNFPEEYFR----TCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 82 -SGCPA--VSAFISIHNMAswmidRFGTEAQRQKWLPSMMSMDLIAsYCL--TEPSAGSDAAALKTKAVKDGTDFVLNGT 156
Cdd:PRK12341 79 kCGAPAflITNGQCIHSMR-----RFGSAEQLRKTAESTLETGDPA-YALalTEPGAGSDNNSATTTYTRKNGKVYLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 157 KQFISGAGTSDLYLVMAR--TGGDGAAGVSCFLVPKDAPGVSFGANEKkMGWKAQPTRTVILEDVRIPAENMIGDEGQGF 234
Cdd:PRK12341 153 KTFITGAKEYPYMLVLARdpQPKDPKKAFTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 235 KIAMMGLDGGRLNIGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDakAHD 314
Cdd:PRK12341 232 LNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQAD--NGQ 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522082706 315 ATRW-CAMAKRFATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDLLK 382
Cdd:PRK12341 310 SLRTsAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILK 378
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
1-383 |
5.14e-61 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 202.09 E-value: 5.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 1 MSQFDLFDLNEDQRAIQEMARDFSRDKIAPFALEWDEKEHFPVDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEAL 80
Cdd:PTZ00461 29 RAFMDLYNPTPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 81 ASGCPAVSAFISIHNMAswMIDRF---GTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGT-DFVLNGT 156
Cdd:PTZ00461 109 SKYDPGFCLAYLAHSML--FVNNFyysASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 157 KQFISGAGTSDLYLVMARTGGDgaagVSCFLVPKDAPGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMIGDEGQGFKI 236
Cdd:PTZ00461 187 KIWITNGTVADVFLIYAKVDGK----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 237 AMMGLDGGRLNIGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDAKAHDAT 316
Cdd:PTZ00461 263 MMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRL 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522082706 317 RWCAmAKRFATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDLLKG 383
Cdd:PTZ00461 343 GSDA-AKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKG 408
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
36-371 |
4.02e-59 |
|
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: 197.23 E-value: 4.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 36 DEKEHFP------VDVMREAAALGMGgiyVRDDVGGTGLGRLDAALIFEALASGC-PAVSAFISIHNMASwmIDRFGTEA 108
Cdd:cd01153 29 DGRVVVPppfkeaLDAFAEAGWMALG---VPEEYGGQGLPITVYSALAEIFSRGDaPLMYASGTQGAAAT--LLAHGTEA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 109 QRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGT-DFVLNGTKQFISgAGTSDL-----YLVMARTGG--DGA 180
Cdd:cd01153 104 QREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFIS-AGEHDMsenivHLVLARSEGapPGV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 181 AGVSCFLVPK-----DAPGVSFGANEKKMGWKAQPTRTVILEDVRIPaenMIGDEGQGFKIAMMGLDGGRLNIGACSLGG 255
Cdd:cd01153 183 KGLSLFLVPKflddgERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 256 AQAALDKAVTYMGERKAFGKNLAQFQA----LQFKVADMLTE----LEAARTL-LYKA----------ACKLDAKAHDA- 315
Cdd:cd01153 260 AEAAYLNALAYAKERKQGGDLIKAAPAvtiiHHPDVRRSLMTqkayAEGSRALdLYTAtvqdlaerkaTEGEDRKALSAl 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 522082706 316 TRW-CAMAKRFATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEI 371
Cdd:cd01153 340 ADLlTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
12-382 |
1.71e-54 |
|
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: 184.52 E-value: 1.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 12 DQRAIQEMARDFSRDKIAPFALEwDEKEhfpvdvmrEAAALGMGGIYVRDDVGGTGLGRLDAALIFEALASGCPAVSAF- 90
Cdd:cd01155 22 EQEFLEYYAEGGDRWWTPPPIIE-KLKA--------KAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRSFFAPEVFn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 91 ---ISIHNMAswMIDRFGTEAQRQKWLPSMMSMDLIASYCLTEPS-AGSDAAALKTKAVKDGTDFVLNGTKQFISGAGTS 166
Cdd:cd01155 93 cqaPDTGNME--VLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGDP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 167 D--LYLVMARTGGDGAAG---VSCFLVPKDAPGVSFGANEKKMGWKAQPT--RTVILEDVRIPAENMIGDEGQGFKIAMM 239
Cdd:cd01155 171 RckIAIVMGRTDPDGAPRhrqQSMILVPMDTPGVTIIRPLSVFGYDDAPHghAEITFDNVRVPASNLILGEGRGFEIAQG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 240 GLDGGRLNIGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDAKAHDATR-W 318
Cdd:cd01155 251 RLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAARkE 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522082706 319 CAMAKRFATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDLLK 382
Cdd:cd01155 331 IAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
7-382 |
4.06e-51 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 175.40 E-value: 4.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 7 FDLNEDQRAIQEMARDF--SRDKIAPFAlEWDEKEHFPVDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEALAS-G 83
Cdd:PRK03354 3 FNLNDEQELFVAGIRELmaSENWEAYFA-ECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 84 CPAVSAFISIHNMASWMidRFGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGTDFVLNGTKQFISGA 163
Cdd:PRK03354 82 APTYVLYQLPGGFNTFL--REGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 164 GTSDLYLVMARTGGDGAAGV-SCFLVPKDAPGVSFGANEKkMGWKAQPTRTVILEDVRIPAENMIGDEGQGFKIAMMGLD 242
Cdd:PRK03354 160 AYTPYIVVMARDGASPDKPVyTEWFVDMSKPGIKVTKLEK-LGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 243 GGRLNIGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDAKAHDATRwCAMA 322
Cdd:PRK03354 239 HERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGD-AAMC 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 323 KRFATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDLLK 382
Cdd:PRK03354 318 KYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLK 377
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
231-378 |
4.38e-49 |
|
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: 162.81 E-value: 4.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 231 GQGFKIAMMGLDGGRLNIGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDA 310
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522082706 311 KAHDATRwCAMAKRFATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISR 378
Cdd:pfam00441 81 GGPDGAE-ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
29-381 |
5.09e-47 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 164.44 E-value: 5.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 29 APFALEWDEKEHFPVDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEALASGCPAVSAFISIHNMASWMIDRFGTEA 108
Cdd:cd01152 24 EESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILAYGTDE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 109 QRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGTDFVLNGTKQFISGAGTSDLYLVMARTGGDGA--AGVSCF 186
Cdd:cd01152 104 QKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEAPkhRGISIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 187 LVPKDAPGVSFGANEKKMGwkAQPTRTVILEDVRIPAENMIGDEGQGFKIAMMGLDGGRLNIGacslGGAQAALDKAVTY 266
Cdd:cd01152 184 LVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIG----GSAATFFELLLAR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 267 MGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDA-KAHDATrwCAMAKRFATDTGFSVANEALQIHGGYG 345
Cdd:cd01152 258 LLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAgKPPGAE--ASIAKLFGSELAQELAELALELLGTAA 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 522082706 346 YLADYG--------VEKIVRDLRVHQILEGTNEIMRLIISRDLL 381
Cdd:cd01152 336 LLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIAERLL 379
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
3-380 |
8.15e-46 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 162.33 E-value: 8.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 3 QFDLFDLNEDQrAIQEMARDFSRDKIAPFALEWDEKEHFPVDVMREAAALGMGGIYVRDdVGGTGLGRLDAALIFEALAS 82
Cdd:PLN02526 24 QFDDLLTPEEQ-ALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIKG-YGCPGLSITASAIATAEVAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 83 GCPAVSAFISIHN-MASWMIDRFGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGTDFVLNGTKQFIS 161
Cdd:PLN02526 102 VDASCSTFILVHSsLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 162 GAGTSDLYLVMARTGGDGAagVSCFLVPKDAPGVSFGANEKKMGWKAQPTRTVILEDV------RIPAENMIGDEGQGFK 235
Cdd:PLN02526 182 NSTFADVLVIFARNTTTNQ--INGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVfvpdedRLPGVNSFQDTNKVLA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 236 IAmmgldggRLNIGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAArTLLYKAACKLDAKAHDA 315
Cdd:PLN02526 260 VS-------RVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAM-FLVGWRLCKLYESGKMT 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522082706 316 TRWCAMAKRFATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDL 380
Cdd:PLN02526 332 PGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
10-121 |
1.10e-42 |
|
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: 144.91 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 10 NEDQRAIQEMARDFSRDKIAPFALEWDEKEHFPVDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEALASGCPAVSA 89
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 522082706 90 FISIHN-MASWMIDRFGTEAQRQKWLPSMMSMD 121
Cdd:pfam02771 81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
82-382 |
1.47e-42 |
|
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: 153.68 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 82 SGCPavsafISIHNMASWMIDRFGTEAQRQkWLPSM----MSMDLIASYCLTEPSAGSDAAALKTKAVKDGTDF-VLNGT 156
Cdd:cd01154 109 LLCP-----LTMTDAAVYALRKYGPEELKQ-YLPGLlsdrYKTGLLGGTWMTEKQGGSDLGANETTAERSGGGVyRLNGH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 157 KQFISGAgTSDLYLVMARTGG--DGAAGVSCFLVPKDAP-----GVSFGANEKKMGWKAQPTRTVILEDvripAEN-MIG 228
Cdd:cd01154 183 KWFASAP-LADAALVLARPEGapAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDD----AEAyLIG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 229 DEGQGFKIAMMGLDGGRLNIGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKL 308
Cdd:cd01154 258 DEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAF 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 309 DAKAHDATRWCAMA-------KRFATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDLL 381
Cdd:cd01154 338 DRAAADKPVEAHMArlatpvaKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVLV 417
|
.
gi 522082706 382 K 382
Cdd:cd01154 418 K 418
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
125-217 |
2.57e-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: 114.30 E-value: 2.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 125 SYCLTEPSAGSDAAALKTKAVK-DGTDFVLNGTKQFISGAGTSDLYLVMARTGG-DGAAGVSCFLVPKDAPGVSFGANEK 202
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADgDGGGWVLNGTKWWITNAGIADLFLVLARTGGdDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 522082706 203 KMGWKAQPTRTVILE 217
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
53-382 |
3.75e-28 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 116.12 E-value: 3.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 53 GMGGIYVRDDVGGTGLGRLDAALIFEALASGCPAVSAF--ISIHNMASWMIdrFGTEAQRQKWLPSMMSMDLIASYCLTE 130
Cdd:PTZ00456 112 GWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYpgLSIGAANTLMA--WGSEEQKEQYLTKLVSGEWSGTMCLTE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 131 PSAGSDAAALKTKAVK--DGTdFVLNGTKQFISgAGTSDL-----YLVMARTGGD--GAAGVSCFLVPKDAP-------- 193
Cdd:PTZ00456 190 PQCGTDLGQVKTKAEPsaDGS-YKITGTKIFIS-AGDHDLtenivHIVLARLPNSlpTTKGLSLFLVPRHVVkpdgslet 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 194 --GVSFGANEKKMGWKAQPTRTVILEDvriPAENMIGDEGQGFKIAMMGLDGGRLNIGACSLGGAQAALDKAVTYMGERK 271
Cdd:PTZ00456 268 akNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERR 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 272 AFgKNLAQFQALQfKVADMLTE--------------LEAARTLLYKAACKLD--AKAHDATRWCAM----------AKRF 325
Cdd:PTZ00456 345 SM-RALSGTKEPE-KPADRIIChanvrqnilfakavAEGGRALLLDVGRLLDihAAAKDAATREALdheigfytpiAKGC 422
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 522082706 326 ATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRL-IISRDLLK 382
Cdd:PTZ00456 423 LTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVLS 480
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
103-371 |
4.84e-28 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 116.05 E-value: 4.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 103 RFGTEAQRQKWLPSMMSMDLIASYCLTEPS-AGSDAAALKTKAVKDGTDFVLNGTKQFISGA--GTSDLYLVMARTGGDG 179
Cdd:PLN02876 531 RYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTDFNA 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 180 A--AGVSCFLVPKDAPGVS-------FGANEKKMGwKAQptrtVILEDVRIPAENMIGDEGQGFKIAMMGLDGGRLNIGA 250
Cdd:PLN02876 611 PkhKQQSMILVDIQTPGVQikrpllvFGFDDAPHG-HAE----ISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCM 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 251 CSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDAKAHDATRWC-AMAKRFATDT 329
Cdd:PLN02876 686 RLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLGNKKARGIiAMAKVAAPNM 765
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 522082706 330 GFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEI 371
Cdd:PLN02876 766 ALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
104-345 |
1.24e-20 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 93.87 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 104 FGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALK-----TKAVKDGTD---FVLNGTKQFISGAGTSDLyLVMA-- 173
Cdd:PRK13026 174 YGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEvlgLRLTWDKRYITLAPVATV-LGLAfk 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 174 ------RTGGDGAAGVSCFLVPKDAPGVSFGANEKKMGWKAQ--PTRTvilEDVRIPAENMIGDE---GQGFKIAMMGLD 242
Cdd:PRK13026 253 lrdpdgLLGDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMngTTRG---KDVFIPLDWIIGGPdyaGRGWRMLVECLS 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 243 GGRlNIGACSLGGAQAALDKAVT--YMGERKAFGKNLAQFQALQFKVADM--LT-ELEAARTLLyKAACKLDAKAHDATr 317
Cdd:PRK13026 330 AGR-GISLPALGTASGHMATRTTgaYAYVRRQFGMPIGQFEGVQEALARIagNTyLLEAARRLT-TTGLDLGVKPSVVT- 406
|
250 260
....*....|....*....|....*...
gi 522082706 318 wcAMAKRFATDTGFSVANEALQIHGGYG 345
Cdd:PRK13026 407 --AIAKYHMTELARDVVNDAMDIHAGKG 432
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
105-382 |
2.08e-20 |
|
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: 92.78 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 105 GTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGT--DFVLN-----GTKQFISGAG-TSDLYLVMAR-- 174
Cdd:cd01150 117 GTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLtqEFVINtpdftATKWWPGNLGkTATHAVVFAQli 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 175 TGGDgAAGVSCFLVP-KDA------PGVSFGANEKKMGWKAQPTRTVILEDVRIPAENM----------------IGDEG 231
Cdd:cd01150 197 TPGK-NHGLHAFIVPiRDPkthqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLlnrfgdvspdgtyvspFKDPN 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 232 QGFKIAMMGLDGGRLNIGACSLGGAQAALDKAVTYMGERKAFGKNLAQ-------FQALQFKVADMLteleaARTLLYK- 303
Cdd:cd01150 276 KRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKPSDpevqildYQLQQYRLFPQL-----AAAYAFHf 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 304 AACKLDAKAHDATRWCAMA---------------KRFATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGT 368
Cdd:cd01150 351 AAKSLVEMYHEIIKELLQGnsellaelhalsaglKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGD 430
|
330
....*....|....
gi 522082706 369 NEIMRLIISRDLLK 382
Cdd:cd01150 431 NTVLLQQTANYLLK 444
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
248-370 |
2.85e-18 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 80.47 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 248 IGACSLGGAQAALDKAVTYMGERK--AFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDAKAHDATRWC------ 319
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKPVTpalrae 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 522082706 320 -AMAKRFATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNE 370
Cdd:pfam08028 82 aRRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
103-345 |
2.33e-17 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 83.71 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 103 RFGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALK-----TKAVKDGTD---FVLNGTKQFISGAGTSDLyLVMA- 173
Cdd:PRK09463 174 HYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEvlgMRLTWNKRYITLAPIATV-LGLAf 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 174 RT-------GGDGAAGVSCFLVPKDAPGVSFGANEKKMGWKAQ--PTRTvilEDVRIPAENMIGDE---GQGFKIAMMGL 241
Cdd:PRK09463 253 KLydpdgllGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQngPTRG---KDVFIPLDYIIGGPkmaGQGWRMLMECL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 242 DGGR-LNIGACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADM---LTELEAARTLlykAACKLDAKAHDATR 317
Cdd:PRK09463 330 SVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIagnAYLMDAARTL---TTAAVDLGEKPSVL 406
|
250 260
....*....|....*....|....*...
gi 522082706 318 wCAMAKRFATDTGFSVANEALQIHGGYG 345
Cdd:PRK09463 407 -SAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
26-362 |
7.32e-17 |
|
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: 81.22 E-value: 7.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 26 DKIAPFALEWDEKEHFPVDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEALASGCPAVSAFISIHNMASWMIDRFG 105
Cdd:cd01163 8 ARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVEALLLAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 106 TEAQRQKWLPSMMSMDLIAsyCLTEPSAGSDAAALKTKAVKDGTDFVLNGTKQFISGAGTSDLYLVMARTGGDGAAGVsc 185
Cdd:cd01163 88 PEQFRKRWFGRVLNGWIFG--NAVSERGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKLVFA-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 186 fLVPKDAPGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMIGDeGQGFKIAMMGLDGGRLNIGACSLGGAQAALDKAVT 265
Cdd:cd01163 164 -AVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPR-PNAPDRGTLLTAIYQLVLAAVLAGIARAALDDAVA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 266 YMGERKAFGKNLAQFQA-----LQFKVADMLTELEAARTLLYKAACKLDAKAHDATRWC-----------AMAKRFATDT 329
Cdd:cd01163 242 YVRSRTRPWIHSGAESArddpyVQQVVGDLAARLHAAEALVLQAARALDAAAAAGTALTaeargeaalavAAAKVVVTRL 321
|
330 340 350
....*....|....*....|....*....|...
gi 522082706 330 GFSVANEALQIHGGYGYLADYGVEKIVRDLRVH 362
Cdd:cd01163 322 ALDATSRLFEVGGASATAREHNLDRHWRNARTH 354
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
25-361 |
1.11e-15 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 77.77 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 25 RDKIAPFALEWDEKEHFPVDVMREAAALGMGGIYVRDDVGGTGLGRLDAALIFEALASGCPAVSAFISIHNMASWMIDRF 104
Cdd:cd01159 7 APLIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATHSRMLAAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 105 GTEAQRQKWLpsmmsmdliasyclTEPSAG-SDAAALKTKAVKDGTDFVLNGTKQFISGAGTSDLYLVMARTGGDGAAGV 183
Cdd:cd01159 87 PPEAQEEVWG--------------DGPDTLlAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 184 SC-FLVPKDapGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMI--GDEGQG---------FKIAMMGLDGgrLNIGAC 251
Cdd:cd01159 153 PRaFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtaGDMMAGdgpggstpvYRMPLRQVFP--LSFAAV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 252 SLGGAQAALDKAVTYMGER---KAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLDAKAHD-----------ATR 317
Cdd:cd01159 229 SLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAggpidveerarIRR 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 522082706 318 WCAmakrFATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRV 361
Cdd:cd01159 309 DAA----YAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHA 348
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
111-382 |
1.58e-15 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 77.87 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 111 QKWLPSMMS-------------MDLIASYCLTEPSAGSDAAALKTKAVK-DGTDFVLNGTKQFISgAGTSDLYLVMARTG 176
Cdd:PRK11561 154 QDWLTPLLSdrydshllpggqkRGLLIGMGMTEKQGGSDVLSNTTRAERlADGSYRLVGHKWFFS-VPQSDAHLVLAQAK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 177 GdgaaGVSCFLVPKDAP-----GVSFGANEKKMGWKAQPTRTVILEDVripAENMIGDEGQGFK--IAMMGLDggRLNIG 249
Cdd:PRK11561 233 G----GLSCFFVPRFLPdgqrnAIRLERLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRliLKMGGMT--RFDCA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 250 ACSLGGAQAALDKAVTYMGERKAFGKNLAQFQALQFKVADMLTELEAARTLLYKAACKLD--AKAHDATrWCAM----AK 323
Cdd:PRK11561 304 LGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDrrADAKEAL-WARLftpaAK 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 522082706 324 RFATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIMRLIISRDLLK 382
Cdd:PRK11561 383 FVICKRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNK 441
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
56-241 |
3.59e-12 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 67.60 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 56 GIYVRDDVGGTGLGRLDAALIFEALASGCPAVSAFISIH-NMASWMIDRFGTEAQRQKWLPSMMSMDLIASYClTEPSAG 134
Cdd:PTZ00457 67 GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHsGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 135 SDAAALKTKAV-KDGTDFVLNGTKQFISGAGTSDlYLVMART--------GGDGAAGVSCFLVPKDAPGVSFGANekkmg 205
Cdd:PTZ00457 146 SDISMNTTKASlTDDGSYVLTGQKRCEFAASATH-FLVLAKTltqtaaeeGATEVSRNSFFICAKDAKGVSVNGD----- 219
|
170 180 190
....*....|....*....|....*....|....*.
gi 522082706 206 wkaqptrTVILEDVriPAENMIGDEGQGFKIAMMGL 241
Cdd:PTZ00457 220 -------SVVFENT--PAADVVGVVGEGFKDAMITL 246
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
105-385 |
2.33e-10 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 62.17 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 105 GTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKD--GTDFVLN-----GTKQFISGAG-TSDLYLVMARTG 176
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDkqTNEFVIHtpsveAVKFWPGELGfLCNFALVYAKLI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 177 GDGAA-GVSCFLVP-------KDAPGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMI---------------GDEGQG 233
Cdd:PTZ00460 190 VNGKNkGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikvsedgqverqGNPKVS 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 234 FKiAMMGLDggRLNIGACSLGGAQaALDKAVTYMGERKAFGKNLAQ------FQALQFKVADMLTELEAA---------- 297
Cdd:PTZ00460 270 YA-SMMYMR--NLIIDQYPRFAAQ-ALTVAIRYSIYRQQFTNDNKQensvleYQTQQQKLLPLLAEFYACifgglkikel 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 298 -------------RTLLYKAACKLDAKAH------DATRWCAMAkrfatdtgfsvanealqiHGGYGYLADYGVEKIVRD 358
Cdd:PTZ00460 346 vddnfnrvqkndfSLLQLTHAILSAAKANytyfvsNCAEWCRLS------------------CGGHGYAHYSGLPAIYFD 407
|
330 340
....*....|....*....|....*..
gi 522082706 359 LRVHQILEGTNEIMRLIISRDLLKGGQ 385
Cdd:PTZ00460 408 MSPNITLEGENQIMYLQLARYLLKQLQ 434
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
105-382 |
2.23e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 59.08 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 105 GTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKD-GTD-FVLN-----GTKQFISGAG-TSDLYLVMARTG 176
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDpKTDeFVIHsptltSSKWWPGGLGkVSTHAVVYARLI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 177 GDGAA-GVSCFLVP-------KDAPGVSFGANEKKMGWKAQPTR---TVILEDVRIPAENM------IGDEGQ--GFKIA 237
Cdd:PLN02443 194 TNGKDhGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMdngFLRFDHVRIPRDQMlmrlskVTREGKyvQSDVP 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 238 MMGLDGGRLNIGACSLGGAQAALDKAVT----YMGERKAFGKN-------LAQFQALQFKVADMLTELEAARTL------ 300
Cdd:PLN02443 274 RQLVYGTMVYVRQTIVADASTALSRAVCiatrYSAVRRQFGSQdggpetqVIDYKTQQSRLFPLLASAYAFRFVgewlkw 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 301 LYKAAC-KLDAK-------AHDATrwcAMAKRFATDTGFSVANEALQIHGGYGYLADYGVEKIVRDLRVHQILEGTNEIM 372
Cdd:PLN02443 354 LYTDVTqRLEANdfstlpeAHACT---AGLKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGDNVVL 430
|
330
....*....|
gi 522082706 373 RLIISRDLLK 382
Cdd:PLN02443 431 LLQVARFLMK 440
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
104-382 |
9.73e-08 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 54.09 E-value: 9.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 104 FGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDG-TD-FVLN-----GTKQFISGAGTSDLYL-VMAR- 174
Cdd:PLN02636 155 LGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPlTDeFVINtpndgAIKWWIGNAAVHGKFAtVFARl 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 175 ------TGGDGAAGVSCFLVP----KD---APGVSFGANEKKMGWKAQPTRTVILEDVRIPAENMIGDEG---------- 231
Cdd:PLN02636 235 klpthdSKGVSDMGVHAFIVPirdmKThqvLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGdvsrdgkyts 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 232 ------QGFKIAMMGLDGGRLNIGACSLGGAQAALDKAVTYMGERKAFGK------NLAQFQALQFKVADMLTELEA--- 296
Cdd:PLN02636 315 slptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPpkqpeiSILDYQSQQHKLMPMLASTYAfhf 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 297 ARTLLYKAACKLDaKAH------DATRWCAMAKRFATD---TGFSVANEALqihGGYGYLADYGVEKIVRDLRVHQILEG 367
Cdd:PLN02636 395 ATEYLVERYSEMK-KTHddqlvaDVHALSAGLKAYITSytaKALSTCREAC---GGHGYAAVNRFGSLRNDHDIFQTFEG 470
|
330
....*....|....*
gi 522082706 368 TNEIMRLIISRDLLK 382
Cdd:PLN02636 471 DNTVLLQQVAADLLK 485
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
101-273 |
5.09e-05 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 45.15 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 101 IDRFGTEAQRQKWLPSMMSMDLIASYCLTEPSAGSDAAALKTKAVKDGT--DFVLN-----GTKQFISGAGTSDLY-LVM 172
Cdd:PLN02312 164 IKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKteEFVINtpcesAQKYWIGGAANHATHtIVF 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522082706 173 ARTGGDGA-AGVSCFLVP-KDA-----PGVSFGANEKKMGWKAQPTRTVILEDVRIPAEN----------------MIGD 229
Cdd:PLN02312 244 SQLHINGKnEGVHAFIAQiRDQdgnicPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENllnsvadvspdgkyvsAIKD 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 522082706 230 EGQGFKIAMMGLDGGRLNIGACSLGGAQAALDKAVTYMGERKAF 273
Cdd:PLN02312 324 PDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
|
|
| |
