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Conserved domains on  [gi|2624510]
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Chain A, MEDIUM CHAIN ACYL-COA DEHYDROGENASE

Protein Classification

medium-chain specific acyl-CoA dehydrogenase( domain architecture ID 10100180)

mitochondrial medium-chain specific acyl-CoA dehydrogenase (MCAD) is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats

EC:  1.3.8.7
Gene Ontology:  GO:0050660|GO:0016627
PubMed:  12504675

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
16-393 0e+00

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: 785.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   16 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ 95
Cdd:cd01157   1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   96 TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 175
Cdd:cd01157  81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  176 YFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKE 255
Cdd:cd01157 161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  256 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF 335
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 2624510  336 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAREHIDK 393
Cdd:cd01157 321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
 
Name Accession Description Interval E-value
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
16-393 0e+00

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: 785.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   16 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ 95
Cdd:cd01157   1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   96 TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 175
Cdd:cd01157  81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  176 YFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKE 255
Cdd:cd01157 161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  256 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF 335
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 2624510  336 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAREHIDK 393
Cdd:cd01157 321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
14-395 8.42e-124

Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism];


Pssm-ID: 224871 [Multi-domain]  Cd Length: 393  Bit Score: 363.36  E-value: 8.42e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   14 FEFTEQQKEFQATARKFAREEIIPVAAEYD---KTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYG 90
Cdd:COG1960   3 FDLSEEQEALRAEVREFAEEELAPEAAEIDrriEDERFPRELLRALAEAGLLGLTIPEEYGGLGLSPLEQAAVLEELARA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   91 CTG----VQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIK-TKAEKKGDEYIINGQKM 165
Cdd:COG1960  83 DAGgalaLGLTHGGLGALAPTILRFGTEEQKRRYLPRLASGELIGAFALTEPGAGSDLASLRtTAAVRDDGDYVLNGQKI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  166 WITNGGKANWYFLLARSDPDPkaPANKAFTGFIVEAD-TPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAG 244
Cdd:COG1960 163 WISNAPVADWLLVLARTDPAP--GKHKGISLFLVPKDlTPGVSVGPILKKMGLRGSATGEVFFDDVRVPAENLLGEEGDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  245 FKVAMGAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR 324
Cdd:COG1960 241 FKIAMETLNVERLGIAAQALGIAEAALEEAVAYARERKQFGRPIADFQLVQFKLADMAAELEAARLLVLRAAELADAGDD 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2624510  325 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAREHIDKYK 395
Cdd:COG1960 321 AGAEAAMAKLFATEAALEVADEAVQVHGGYGYTEEYPVERYYRDARILRIYEGTSEIQRLIIARRLLGLPA 391
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
13-389 8.40e-86

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 266.36  E-value: 8.40e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    13 SFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP--VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEEL--A 88
Cdd:PLN02519  23 SLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEIsrA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    89 YGCTGVQTAIEGNsLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWIT 168
Cdd:PLN02519 103 SGSVGLSYGAHSN-LCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCT 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   169 NGGKANWYFLLARSDPdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVA 248
Cdd:PLN02519 182 NGPVAQTLVVYAKTDV---AAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVM 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   249 MGAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYY 328
Cdd:PLN02519 259 MSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKD 338
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2624510   329 ASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVARE 389
Cdd:PLN02519 339 CAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRE 399
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
242-388 2.18e-54

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: 176.68  E-value: 2.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    242 GAGFKVAMGAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDS 321
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2624510    322 GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAR 388
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
 
Name Accession Description Interval E-value
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
16-393 0e+00

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: 785.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   16 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ 95
Cdd:cd01157   1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   96 TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 175
Cdd:cd01157  81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  176 YFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKE 255
Cdd:cd01157 161 YFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  256 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF 335
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 2624510  336 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAREHIDK 393
Cdd:cd01157 321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
18-393 1.69e-148

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: 425.14  E-value: 1.69e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   18 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTA 97
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   98 IEG-NSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 176
Cdd:cd01158  81 VSVhNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  177 FLLARSDPDPKapaNKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKER 256
Cdd:cd01158 161 IVFAVTDPSKG---YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGR 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  257 PVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFA 336
Cdd:cd01158 238 IGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFA 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 2624510  337 GDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAReHIDK 393
Cdd:cd01158 318 SEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAK-HLLK 373
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
18-388 1.47e-133

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: 385.48  E-value: 1.47e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   18 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGlmnthipencgglglgtfdacliseelaygctgvqta 97
Cdd:cd00567   1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLL------------------------------------- 43
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   98 iegnslGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYF 177
Cdd:cd00567  44 ------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  178 LLARSDPDPkaPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKERP 257
Cdd:cd00567 118 VLARTDEEG--PGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRL 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  258 VVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRN-TYYASIAKAFA 336
Cdd:cd00567 196 LLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEaRLEAAMAKLFA 275
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 2624510  337 GDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAR 388
Cdd:cd00567 276 TEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
14-395 8.42e-124

Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism];


Pssm-ID: 224871 [Multi-domain]  Cd Length: 393  Bit Score: 363.36  E-value: 8.42e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   14 FEFTEQQKEFQATARKFAREEIIPVAAEYD---KTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYG 90
Cdd:COG1960   3 FDLSEEQEALRAEVREFAEEELAPEAAEIDrriEDERFPRELLRALAEAGLLGLTIPEEYGGLGLSPLEQAAVLEELARA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   91 CTG----VQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIK-TKAEKKGDEYIINGQKM 165
Cdd:COG1960  83 DAGgalaLGLTHGGLGALAPTILRFGTEEQKRRYLPRLASGELIGAFALTEPGAGSDLASLRtTAAVRDDGDYVLNGQKI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  166 WITNGGKANWYFLLARSDPDPkaPANKAFTGFIVEAD-TPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAG 244
Cdd:COG1960 163 WISNAPVADWLLVLARTDPAP--GKHKGISLFLVPKDlTPGVSVGPILKKMGLRGSATGEVFFDDVRVPAENLLGEEGDG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  245 FKVAMGAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRR 324
Cdd:COG1960 241 FKIAMETLNVERLGIAAQALGIAEAALEEAVAYARERKQFGRPIADFQLVQFKLADMAAELEAARLLVLRAAELADAGDD 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2624510  325 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAREHIDKYK 395
Cdd:COG1960 321 AGAEAAMAKLFATEAALEVADEAVQVHGGYGYTEEYPVERYYRDARILRIYEGTSEIQRLIIARRLLGLPA 391
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
16-389 4.42e-112

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: 332.84  E-value: 4.42e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   16 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ 95
Cdd:cd01156   2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   96 TAIEGNS---LGQmpIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGK 172
Cdd:cd01156  82 LSYGAHSnlcINQ--IYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  173 ANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAF 252
Cdd:cd01156 160 ADTLVVYAKTDPSAGA---HGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  253 DKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIA 332
Cdd:cd01156 237 DYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGV 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 2624510  333 KAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVARE 389
Cdd:cd01156 317 ILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRE 373
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
17-389 1.21e-110

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: 329.02  E-value: 1.21e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   17 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQT 96
Cdd:cd01162   2 NEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   97 AIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 176
Cdd:cd01162  82 YISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  177 FLLARSDpdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKER 256
Cdd:cd01162 162 VVMARTG----GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGR 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  257 PVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRN-TYYASIAKAF 335
Cdd:cd01162 238 LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDaVKLCAMAKRF 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 2624510  336 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVARE 389
Cdd:cd01162 318 ATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARA 371
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
18-389 6.69e-105

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: 314.05  E-value: 6.69e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   18 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY-GCTGVQT 96
Cdd:cd01160   1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARaGGSGPGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   97 AIEgNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWY 176
Cdd:cd01160  81 SLH-TDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  177 FLLARSDPDPKAPANKAFtgFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKER 256
Cdd:cd01160 160 IVVARTGGEARGAGGISL--FLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQER 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  257 PVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFA 336
Cdd:cd01160 238 LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWA 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 2624510  337 GDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVARE 389
Cdd:cd01160 318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
15-387 8.88e-90

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: 276.66  E-value: 8.88e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   15 EFTEQQKEFQATARKFAREEIIPvaAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY-GCTG 93
Cdd:cd01161  26 EQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMdLGFS 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   94 VQTAIEgNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWITNGG 171
Cdd:cd01161 104 VTLGAH-QSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWITNGG 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  172 KANWYFLLARSD-PDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMG 250
Cdd:cd01161 183 IADIFTVFAKTEvKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMN 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  251 AFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYY-- 328
Cdd:cd01161 263 ILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQie 342
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 2624510  329 ASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVA 387
Cdd:cd01161 343 AAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIA 401
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
13-389 8.40e-86

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 266.36  E-value: 8.40e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    13 SFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP--VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEEL--A 88
Cdd:PLN02519  23 SLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEIsrA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    89 YGCTGVQTAIEGNsLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWIT 168
Cdd:PLN02519 103 SGSVGLSYGAHSN-LCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCT 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   169 NGGKANWYFLLARSDPdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVA 248
Cdd:PLN02519 182 NGPVAQTLVVYAKTDV---AAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVM 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   249 MGAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYY 328
Cdd:PLN02519 259 MSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKD 338
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2624510   329 ASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVARE 389
Cdd:PLN02519 339 CAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRE 399
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
10-389 2.46e-70

Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.


Pssm-ID: 173840 [Multi-domain]  Cd Length: 386  Bit Score: 225.70  E-value: 2.46e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   10 LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNThIPENCGGLGLGTFDACLISEELAY 89
Cdd:cd01151   7 LNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVER 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   90 GCTGVQTAIE-GNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWIT 168
Cdd:cd01151  86 VDSGYRSFMSvQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWIT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  169 NGGKANWYFLLARSDPDPKapankaFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGdGAGFKVA 248
Cdd:cd01151 166 NSPIADVFVVWARNDETGK------IRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPG-AEGLRGP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  249 MGAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELArmsyQRAAWEV----DSGRR 324
Cdd:cd01151 239 FKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALG----LLACLRVgrlkDQGKA 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2624510  325 NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVARE 389
Cdd:cd01151 315 TPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRA 379
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
18-388 1.46e-64

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: 210.67  E-value: 1.46e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   18 EQQKEFQATARKFAREEIIP-----VAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCT 92
Cdd:cd01152   1 PSEEAFRAEVRAWLAAHLPPelreeSALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   93 GVQtaieGNSLGQM---PIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWIT 168
Cdd:cd01152  81 PVP----FNQIGIDlagPTILAyGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  169 NGGKANWYFLLARSDPDpkAPANKAFTGFIVEADTPGIQIgR--KELNMGqrcSDTRGIVFEDVKVPKENVLIGDGAGFK 246
Cdd:cd01152 157 GAHYADWAWLLVRTDPE--APKHRGISILLVDMDSPGVTV-RpiRSINGG---EFFNEVFLDDVRVPDANRVGEVNDGWK 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  247 VAMGAFDKERPVVAAGAVGLAQRALDeatkYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNT 326
Cdd:cd01152 231 VAMTTLNFERVSIGGSAATFFELLLA----RLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG 306
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  327 YYASIAKAFAGDIANQLATDAVQILG--------GNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAR 388
Cdd:cd01152 307 AEASIAKLFGSELAQELAELALELLGtaallrdpAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAE 376
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
17-378 1.65e-63

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 209.02  E-value: 1.65e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    17 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQT 96
Cdd:PTZ00461  38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    97 AIEGNS-LGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDE-YIINGQKMWITNGGKAN 174
Cdd:PTZ00461 118 AYLAHSmLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGnYVLNGSKIWITNGTVAD 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   175 WYFLLARSDpdpkapanKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDK 254
Cdd:PTZ00461 198 VFLIYAKVD--------GKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLEL 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   255 ERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKA 334
Cdd:PTZ00461 270 ERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKL 349
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 2624510   335 FAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGT 378
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
PRK12341 PRK12341
acyl-CoA dehydrogenase;
14-395 9.14e-63

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 206.12  E-value: 9.14e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    14 FEFTEQQKEFQATARKF-AREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYgcT 92
Cdd:PRK12341   3 FSLTEEQELLLASIRELiTRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSK--C 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    93 GVQTAIEGNSLGQMPIIIAGNDQQKKKYLgRMTEEPLMCAYC--VTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNG 170
Cdd:PRK12341  81 GAPAFLITNGQCIHSMRRFGSAEQLRKTA-ESTLETGDPAYAlaLTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   171 GKANWYFLLARsDPDPKAPaNKAFTGFIVEADTPGIQIGRKElNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMG 250
Cdd:PRK12341 160 KEYPYMLVLAR-DPQPKDP-KKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMY 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   251 AFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYAS 330
Cdd:PRK12341 237 NFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAA 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2624510   331 IAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAREHIDKYK 395
Cdd:PRK12341 317 LAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDYQ 381
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
25-382 3.38e-60

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: 200.31  E-value: 3.38e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   25 ATARKFAREEIIPVAAEYDKTG--------EYPVP---LIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTG 93
Cdd:cd01153   3 EEVARLAENVLAPLNADGDREGpvfddgrvVVPPPfkeALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   94 VqtAIEGNSLGQMPIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNGG 171
Cdd:cd01153  83 L--MYASGTQGAAATLLAhGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  172 KANW----YFLLARSDPDPkaPANKAFTGFIV-----EADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPkenvLIGD- 241
Cdd:cd01153 161 HDMSenivHLVLARSEGAP--PGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE----LIGEe 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  242 GAGFKVAMGAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVE--------HQAISFMLAEMAMKVELARMSYQ 313
Cdd:cd01153 235 GMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAapavtiihHPDVRRSLMTQKAYAEGSRALDL 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  314 RAAWEVDSGRR--------------NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTS 379
Cdd:cd01153 315 YTATVQDLAERkategedrkalsalADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTT 394

                ...
gi 2624510  380 QIQ 382
Cdd:cd01153 395 GIQ 397
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
242-388 2.18e-54

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: 176.68  E-value: 2.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    242 GAGFKVAMGAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDS 321
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2624510    322 GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAR 388
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
18-388 1.12e-52

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: 180.28  E-value: 1.12e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   18 EQQKEFQATARKFAREEIIPVAAEYDktgEYPVPLIRRAW--------------ELGLMNTHIPENCGGLGLGTFDACLI 83
Cdd:cd01155   1 RKAQELRARVKAFMEEHVYPAEQEFL---EYYAEGGDRWWtpppiieklkakakAEGLWNLFLPEVSGLSGLTNLEYAYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   84 SEEL--------AYGCTGVQTaiegnslGQMPIIIA-GNDQQKKKYLgrmteEPLM-----CAYCVTEPG-AGSDVAGIK 148
Cdd:cd01155  78 AEETgrsffapeVFNCQAPDT-------GNMEVLHRyGSEEQKKQWL-----EPLLdgkirSAFAMTEPDvASSDATNIE 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  149 TKAEKKGDEYIINGQKMWITNGG--KANWYFLLARSDPDpKAPANKAFTGFIVEADTPGIQIGRKELNMGQrcSDTRG-- 224
Cdd:cd01155 146 CSIERDGDDYVINGRKWWSSGAGdpRCKIAIVMGRTDPD-GAPRHRQQSMILVPMDTPGVTIIRPLSVFGY--DDAPHgh 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  225 --IVFEDVKVPKENVLIGDGAGFKVAMGAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMA 302
Cdd:cd01155 223 aeITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSR 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  303 MKVELARMSYQRAAWEVDSGRRNTYYASIA--KAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQ 380
Cdd:cd01155 303 IEIEQARLLVLKAAHMIDTVGNKAARKEIAmiKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDE 382

                ....*...
gi 2624510  381 IQRLIVAR 388
Cdd:cd01155 383 VHLRSIAR 390
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
14-395 1.91e-51

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 176.56  E-value: 1.91e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    14 FEFTEQQKEFQATARKF-AREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELayGCT 92
Cdd:PRK03354   3 FNLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--GRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    93 GVQTAIegnsLGQMP-----IIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWI 167
Cdd:PRK03354  81 GAPTYV----LYQLPggfntFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   168 TNGGKANWYFLLARSDPDPKAPAnkaFTGFIVEADTPGIQIGRKElNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKV 247
Cdd:PRK03354 157 TSSAYTPYIVVMARDGASPDKPV---YTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNR 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   248 AMGAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTY 327
Cdd:PRK03354 233 VKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSG 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2624510   328 YASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAREHIDKYK 395
Cdd:PRK03354 313 DAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
PLN02526 PLN02526
acyl-coenzyme A oxidase
17-389 1.29e-43

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 156.55  E-value: 1.29e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    17 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIP-ENCGGLGLgTFDACLISEELAYGCTGVQ 95
Cdd:PLN02526  30 TPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIKgYGCPGLSI-TASAIATAEVARVDASCST 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    96 TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 175
Cdd:PLN02526 109 FILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADV 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   176 YFLLARSdpdpkaPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAgFKVAMGAFDKE 255
Cdd:PLN02526 189 LVIFARN------TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNS-FQDTNKVLAVS 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   256 RPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF 335
Cdd:PLN02526 262 RVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAW 341
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 2624510   336 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVARE 389
Cdd:PLN02526 342 ITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGRE 395
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
17-124 8.71e-39

Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.


Pssm-ID: 426971 [Multi-domain]  Cd Length: 113  Bit Score: 134.90  E-value: 8.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510     17 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQT 96
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
                          90       100
                  ....*....|....*....|....*....
gi 2624510     97 AIE-GNSLGQMPIIIAGNDQQKKKYLGRM 124
Cdd:pfam02771  81 ALSvHSSLGAPPILRFGTEEQKERYLPKL 109
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
120-388 1.09e-32

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: 127.10  E-value: 1.09e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  120 YLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEK-KGDEYIINGQKmWITNGGKANWYFLLARsdPDPKAPANKAFTGFI 198
Cdd:cd01154 138 LLSDRYKTGLLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLAR--PEGAPAGARGLSLFL 214
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  199 VEADTP-----GIQIGRKELNMGQRCSDTRGIVFEDVkvpkENVLIGD-GAGFKVAMGAFDKERPVVAAGAVGLAQRALD 272
Cdd:cd01154 215 VPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA----EAYLIGDeGKGIYYILEMLNISRLDNAVAALGIMRRALS 290
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  273 EATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAA--WEVDSGRRNTYYA------SIAKAFAGDIANQLA 344
Cdd:cd01154 291 EAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAAraFDRAAADKPVEAHmarlatPVAKLIACKRAAPVT 370
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 2624510  345 TDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAR 388
Cdd:cd01154 371 SEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLR 414
PLN02876 PLN02876
acyl-CoA dehydrogenase
104-381 5.91e-32

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 127.99  E-value: 5.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   104 GQMPIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPG-AGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLAR 181
Cdd:PLN02876 524 GNMEVLLRyGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVM 603
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   182 SDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGqrCSDT----RGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKERP 257
Cdd:PLN02876 604 GKTDFNAPKHKQQSMILVDIQTPGVQIKRPLLVFG--FDDAphghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRL 681
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   258 VVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVD--SGRRNTYYASIAKAF 335
Cdd:PLN02876 682 HHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDrlGNKKARGIIAMAKVA 761
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 2624510   336 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQI 381
Cdd:PLN02876 762 APNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
132-228 6.91e-30

Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.


Pssm-ID: 426970 [Multi-domain]  Cd Length: 95  Bit Score: 110.82  E-value: 6.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    132 AYCVTEPGAGSDVAGIKTKA-EKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGR 210
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRH---GGISLFLVPKDAPGVTVRR 77
                          90
                  ....*....|....*...
gi 2624510    211 KELNMGQRCSDTRGIVFE 228
Cdd:pfam02770  78 IETKLGVRGLPTGELVFD 95
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
16-384 4.49e-21

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 94.93  E-value: 4.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    16 FTEQQKEFQ----ATARKFAREEIIPVAAEYD-------KTGEYPVPL-IRRAWEL----GLMNTHIPENCGGLGLgTFD 79
Cdd:PTZ00456  52 KTDVTKELMdsllEEASKLATQTLLPLYESSDsegcvllKDGNVTTPKgFKEAYQAlkagGWTGISEPEEYGGQAL-PLS 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    80 ACLISEELAYGCTGVQTAIEGNSLGQMPIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-E 157
Cdd:PTZ00456 131 VGFITRELMATANWGFSMYPGLSIGAANTLMAwGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgS 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   158 YIINGQKMWITNGG---KAN-WYFLLARSDPDPkaPANKAFTGFIVEADTP----------GIQIGRKELNMGQRCSDTR 223
Cdd:PTZ00456 211 YKITGTKIFISAGDhdlTENiVHIVLARLPNSL--PTTKGLSLFLVPRHVVkpdgsletakNVKCIGLEKKMGIKGSSTC 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   224 GIVFEDVKvpkeNVLIGD-GAGFKVAMGAFDKERPVVAAGAVGLAQRALDEATKYALERKTF------------GKLLVE 290
Cdd:PTZ00456 289 QLSFENSV----GYLIGEpNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIIC 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   291 HQAISFML------AE--MAMKVELAR-MSYQRAAWEVDS----GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFN 357
Cdd:PTZ00456 365 HANVRQNIlfakavAEggRALLLDVGRlLDIHAAAKDAATrealDHEIGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYI 444
                        410       420
                 ....*....|....*....|....*..
gi 2624510   358 TEYPVEKLMRDAKIYQIYGGTSQIQRL 384
Cdd:PTZ00456 445 KGNGMEQILRDARIGTLYEGTTGIQAL 471
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
258-380 1.68e-18

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 80.85  E-value: 1.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    258 VVAAGAVGLAQRALDEATKYALERKT--FGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWE----VDSGRRNTYY--- 328
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARieaaAAAGKPVTPAlra 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2624510    329 -ASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYGGTSQ 380
Cdd:pfam08028  81 eARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
106-285 8.03e-14

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: 72.75  E-value: 8.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  106 MPIIIA-GNDQQKKKYL-GRMTEEPLMCaYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGK-ANW 175
Cdd:cd01150 110 GNAIKNlGTDEHQDYWLqGANNLEIIGC-FAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWWPGNLGKtATH 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  176 YFLLARSDPDPKapaNKAFTGFIV---EADT----PGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------IGDG 242
Cdd:cd01150 189 AVVFAQLITPGK---NHGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLnrfgdvSPDG 265
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 2624510  243 A----------GFKVAMGAFDKERPVVAAGAVGLAQRALDEATKYALERKTFG 285
Cdd:cd01150 266 TyvspfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFG 318
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
23-370 1.64e-13

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: 71.20  E-value: 1.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   23 FQATARKFAREeiipvAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAygctgvqtAIEGNs 102
Cdd:cd01163   3 ARPLAARIAEG-----AAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELA--------AADSN- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  103 LGQMP---------IIIAGNDQQKKKYLGRMTEEPLM-CAycVTEPGaGSDVAGIKTKAEKKGDEYIINGQKmWITNGGK 172
Cdd:cd01163  69 IAQALrahfgfveaLLLAGPEQFRKRWFGRVLNGWIFgNA--VSERG-SVRPGTFLTATVRDGGGYVLNGKK-FYSTGAL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  173 ANWYFLLARSDPDPKApankafTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM-GA 251
Cdd:cd01163 145 FSDWVTVSALDEEGKL------VFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLlTA 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  252 FdkERPVVAAGAVGLAQRALDEATKYALER-KTFGKLLVEH--------QAIsfmlAEMAMKVELARMSYQRAAWEVD-- 320
Cdd:cd01163 219 I--YQLVLAAVLAGIARAALDDAVAYVRSRtRPWIHSGAESarddpyvqQVV----GDLAARLHAAEALVLQAARALDaa 292
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  321 --SGRRNTYYASI--------AKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAK 370
Cdd:cd01163 293 aaAGTALTAEARGeaalavaaAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
136-388 3.54e-11

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 64.77  E-value: 3.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   136 TEPGAGSDVAGIKTKAEKKGDE-YIINGQKmwitnggkanWYFLLARSDPD-PKAPANKAFTGFIVEADTP-----GIQI 208
Cdd:PRK11561 185 TEKQGGSDVLSNTTRAERLADGsYRLVGHK----------WFFSVPQSDAHlVLAQAKGGLSCFFVPRFLPdgqrnAIRL 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   209 GRKELNMGQRCSDTRGIVFEDVK---VPKEnvliGDGAGFKVAMGA---FDkerpvVAAGAVGLAQRALDEATKYALERK 282
Cdd:PRK11561 255 ERLKDKLGNRSNASSEVEFQDAIgwlLGEE----GEGIRLILKMGGmtrFD-----CALGSHGLMRRAFSVAIYHAHQRQ 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   283 TFGKLLVEHQAISFMLAEMAMKVE--------LARMSYQRA-AWEVDSGRRNTYYA--SIAKAFAGDIAnqlatDAVQIL 351
Cdd:PRK11561 326 VFGKPLIEQPLMRQVLSRMALQLEgqtallfrLARAWDRRAdAKEALWARLFTPAAkfVICKRGIPFVA-----EAMEVL 400
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 2624510   352 GGNGFNTEYPVEKLMRDAKIYQIYGGTSQIQRLIVAR 388
Cdd:PRK11561 401 GGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
150-378 1.94e-10

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: 61.60  E-value: 1.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  150 KAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFtgFIVEADtpgIQIGRKELNMGQRCSDTRGIVFED 229
Cdd:cd01159 112 RAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAF--VVPRAE---YEIVDTWHVVGLRGTGSNTVVVDD 186
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  230 VKVPKENVLIGDGA-----------GFKVAMGAFDKerPVVAAGAVGLAQRALDEATKYALER---KTFGKLLVEHQAIS 295
Cdd:cd01159 187 VFVPEHRTLTAGDMmagdgpggstpVYRMPLRQVFP--LSFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQ 264
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  296 FMLAEMAMKVELARMSYQRAAWEVDS---------------GRRNTYYASIAKAFAGDIANQLAtdavqilGGNGFNTEY 360
Cdd:cd01159 265 LRLAEAAAELDAARAFLERATRDLWAhalaggpidveerarIRRDAAYAAKLSAEAVDRLFHAA-------GGSALYTAS 337
                       250       260       270
                ....*....|....*....|....*....|
gi 2624510  361 PVEKLMRDA------------KIYQIYGGT 378
Cdd:cd01159 338 PLQRIWRDIhaaaqhaalnpeTAAEAYGRA 367
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
61-273 8.73e-10

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 60.28  E-value: 8.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    61 LMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSlGQMPIIIA--GNDQQKKKYLGRMTEEPLMCAYCVTEp 138
Cdd:PTZ00457  65 LYGARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHS-GFCTYLLStvGSKELKGKYLTAMSDGTIMMGWATEE- 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   139 GAGSDVAGIKTKAEKKGD-EYIINGQKMWItNGGKANWYFLLAR------SDPDPKAPANKAFtgFIVEADTPGIQIgrk 211
Cdd:PTZ00457 143 GCGSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKtltqtaAEEGATEVSRNSF--FICAKDAKGVSV--- 216
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2624510   212 elnmgqrcsDTRGIVFEDvkVPKENVLIGDGAGFKVAMGAFDKERPVVAAGAVGLAQRALDE 273
Cdd:PTZ00457 217 ---------NGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQE 267
PLN02636 PLN02636
acyl-coenzyme A oxidase
93-285 7.59e-09

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 57.56  E-value: 7.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    93 GVQTAIEGNSlgqmpIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKM 165
Cdd:PLN02636 142 GVQYSLWGGS-----VINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFVINtpndgAIKW 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   166 WITNG---GK-ANWYFLLARSDPDPKAPANKAFTGFIV-------EADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPK 234
Cdd:PLN02636 217 WIGNAavhGKfATVFARLKLPTHDSKGVSDMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPR 296
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2624510   235 ENVL--IGD--------------GAGFKVAMGAFDKERPVVAAGAVGLAQRALDEATKYALERKTFG 285
Cdd:PLN02636 297 DNLLnrFGDvsrdgkytsslptiNKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFG 363
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
66-355 4.67e-08

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 54.96  E-value: 4.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510    66 IPENCGGLGlgtFDA----CLISEELAYGCTGVQTAIEGNSLGQMPIIIA-GNDQQKKKYLGRM---TEEPlmCaYCVTE 137
Cdd:PRK13026 127 IPKEYGGKG---FSAyansTIVSKIATRSVSAAVTVMVPNSLGPGELLTHyGTQEQKDYWLPRLadgTEIP--C-FALTG 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   138 PGAGSDVA-----GIKTKAEKKGDEYI---INGQKMWITNGGKANWYFLLAR-SDPDP--KAPANKAFTGFIVEADTPGI 206
Cdd:PRK13026 201 PEAGSDAGaipdtGIVCRGEFEGEEVLglrLTWDKRYITLAPVATVLGLAFKlRDPDGllGDKKELGITCALIPTDHPGV 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   207 QIGRKELNMGQRCSD--TRGivfEDVKVPKEnVLIGD----GAGFKVAMGAFDKERPV-VAAGAVGLAQRALDEATKYAL 279
Cdd:PRK13026 281 EIGRRHNPLGMAFMNgtTRG---KDVFIPLD-WIIGGpdyaGRGWRMLVECLSAGRGIsLPALGTASGHMATRTTGAYAY 356
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2624510   280 ERKTFGKLLVEHQAISFMLAEMAMK---VELARMSYQRAaweVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNG 355
Cdd:PRK13026 357 VRRQFGMPIGQFEGVQEALARIAGNtylLEAARRLTTTG---LDLGVKPSVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
PLN02443 PLN02443
acyl-coenzyme A oxidase
112-285 4.89e-08

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 54.84  E-value: 4.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   112 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGKANWYFLL-ARSD 183
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTAtfDPKTDEFVIHsptltSSKWWPGGLGKVSTHAVVyARLI 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   184 PDPKapaNKAFTGFIVEADT-------PGI---QIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------------IGD 241
Cdd:PLN02443 194 TNGK---DHGIHGFIVQLRSlddhsplPGVtvgDIGMKFGNGAYNTMDNGFLRFDHVRIPRDQMLmrlskvtregkyVQS 270
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 2624510   242 GAGFKVAMGAFDKERPVVAAGAVGLAQRALDEATKYALERKTFG 285
Cdd:PLN02443 271 DVPRQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFG 314
PLN02312 PLN02312
acyl-CoA oxidase
112-284 1.14e-07

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 53.62  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   112 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWItnGGKAN---WYFLLAR 181
Cdd:PLN02312 168 GTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTtyDPKTEEFVINtpcesAQKYWI--GGAANhatHTIVFSQ 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   182 SDPDPKAPANKAFTGFIVEAD---TPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------IGDG---------- 242
Cdd:PLN02312 246 LHINGKNEGVHAFIAQIRDQDgniCPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLnsvadvSPDGkyvsaikdpd 325
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 2624510   243 AGFKVAMGAFDKERPVVAAGAVGLAQRALDEATKYALERKTF 284
Cdd:PLN02312 326 QRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
112-355 1.58e-07

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 53.28  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   112 GNDQQKKKYLGRM---TEEPlmCaYCVTEPGAGSDVA-----GIKTKAEKKGDEYI---INGQKMWITNG------GKAn 174
Cdd:PRK09463 176 GTDEQKDHYLPRLargEEIP--C-FALTSPEAGSDAGsipdtGVVCKGEWQGEEVLgmrLTWNKRYITLApiatvlGLA- 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   175 wyFLLarSDPDpkapankaftGFI------------VEADTPGIQIGRKELNMGQRCSD--TRGivfEDVKVPKENVlIG 240
Cdd:PRK09463 252 --FKL--YDPD----------GLLgdkedlgitcalIPTDTPGVEIGRRHFPLNVPFQNgpTRG---KDVFIPLDYI-IG 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   241 D----GAGFKVAMGAFDKER----PVVAAGAVGLAQRAldeATKYALERKTFGKLLVEHQAISFMLAEMAMKvelarmsy 312
Cdd:PRK09463 314 GpkmaGQGWRMLMECLSVGRgislPSNSTGGAKLAALA---TGAYARIRRQFKLPIGKFEGIEEPLARIAGN-------- 382
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 2624510   313 qraAWEVDSGRRNTYYA-----------SIAKAFAGDIANQLATDAVQILGGNG 355
Cdd:PRK09463 383 ---AYLMDAARTLTTAAvdlgekpsvlsAIAKYHLTERGRQVINDAMDIHGGKG 433
YoaI COG2368
Aromatic ring hydroxylase [Secondary metabolites biosynthesis, transport and catabolism];
118-353 4.81e-06

Aromatic ring hydroxylase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 225243 [Multi-domain]  Cd Length: 493  Bit Score: 48.49  E-value: 4.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  118 KKYLGRMTEEPLMCAycvtepGAGSDVAGIKTKA--------------EKKGDEYIINGQKMWITNGGKA--NWYFLLAR 181
Cdd:COG2368 134 REYYKEVQKNDLALT------HAITDPKGDRSKRpseqkdpdiyvrvvEETEDGIVVRGAKALATGSALTdeIFVLPTRS 207
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  182 SDPDPKAPAnkafTGFIVEADTPGIQ-IGRKELNMGQRCSD--------TRG------IVFEDVKVPKENVLI-GDgagF 245
Cdd:COG2368 208 MQEDDKDFA----VAFAIPMDTEGVKfICRRSYELGRGAEGgpfdyplsSRFdendaiLVFDDVFVPWERVFIyRD---L 280
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510  246 KVAMGAFDKE-------------RPVVAAGAVGLAQRALdeatkyalerKTFGklLVEHQAISFMLAEMAMKVELAR--- 309
Cdd:COG2368 281 ERAYAWYAVSgfarlhrqqavgrKAVKLDFILGAAYLIA----------ETNG--VEEFRHIQEKLGEMIALLELMWals 348
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 2624510  310 --MSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGG 353
Cdd:COG2368 349 daAAEEAQKNPNGAWLPNPAYANVGRVYAPKAYPRIKEILQDISGG 394
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
112-284 1.34e-05

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 47.15  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   112 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITN-GGKANWYFLLARSD 183
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLI 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624510   184 PDPKAPANKAFTGFIVEADT----PGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL-----IGDGAGF------KVA 248
Cdd:PTZ00460 190 VNGKNKGVHPFMVRIRDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikVSEDGQVerqgnpKVS 269
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 2624510   249 MGAFDKERPVVAAGAVGLAQRALDEATKYALERKTF 284
Cdd:PTZ00460 270 YASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQF 305
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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