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Conserved domains on  [gi|4557233|ref|NP_000008|]
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short-chain specific acyl-CoA dehydrogenase, mitochondrial isoform 1 precursor [Homo sapiens]

Protein Classification

acyl-CoA dehydrogenase( domain architecture ID 10100181)

acyl-CoA dehydrogenase, with similarity to short- and short/branched-chain CoA dehydrogenases, participates in consecutive cycles of fatty acid beta-oxidation to produce acetyl-CoA and reducing equivalents for generating energy

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 36-408 0e+00

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: 673.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   36 ETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVI 115
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  116 MSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAA 195
Cdd:cd01158  81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  196 VVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGI 275
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  276 ASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEA 355
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 4557233  356 ATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLR 408
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 36-408 0e+00

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: 673.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   36 ETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVI 115
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  116 MSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAA 195
Cdd:cd01158  81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  196 VVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGI 275
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  276 ASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEA 355
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 4557233  356 ATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLR 408
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 33-411 1.44e-174

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: 492.43  E-value: 1.44e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   33 ELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCAST 112
Cdd:COG1960   4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  113 GVIMSVNNSLyLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEA 192
Cdd:COG1960  84 ALPVGVHNGA-AEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  193 SAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGR 272
Cdd:COG1960 163 DVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  273 IGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAA 352
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFA 322

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4557233  353 SEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYR 411
Cdd:COG1960 323 TEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 6-408 4.03e-98

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 298.71  E-value: 4.03e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233     6 LARASGPARRAlcpRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQ--VKKMGGLGLLAMD 83
Cdd:PLN02519   1 MLLSAAKARRR---GLARRFSSSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGIT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    84 VPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDA 163
Cdd:PLN02519  78 APEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   164 GAASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIF 243
Cdd:PLN02519 158 VSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVF 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   244 EDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALES 323
Cdd:PLN02519 238 ENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQS 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   324 ARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 403
Cdd:PLN02519 318 SRSYVYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIG 397


                 ....*
gi 4557233   404 GHLLR 408
Cdd:PLN02519 398 RELFK 402
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 258-403 8.55e-53

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: 173.21  E-value: 8.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    258 GMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDN 337
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557233    338 KKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 403
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
 
Name Accession Description Interval E-value
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 36-408 0e+00

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: 673.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   36 ETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVI 115
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  116 MSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAA 195
Cdd:cd01158  81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  196 VVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGI 275
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  276 ASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEA 355
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 4557233  356 ATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLR 408
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 33-411 1.44e-174

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: 492.43  E-value: 1.44e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   33 ELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCAST 112
Cdd:COG1960   4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  113 GVIMSVNNSLyLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEA 192
Cdd:COG1960  84 ALPVGVHNGA-AEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  193 SAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGR 272
Cdd:COG1960 163 DVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  273 IGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAA 352
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFA 322

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4557233  353 SEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYR 411
Cdd:COG1960 323 TEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 34-403 3.21e-127

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: 371.74  E-value: 3.21e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   34 LPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTG 113
Cdd:cd01156   2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  114 VIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEAS 193
Cdd:cd01156  82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  194 AAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRI 273
Cdd:cd01156 162 TLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERL 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  274 GIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAAS 353
Cdd:cd01156 242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAA 321

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 4557233  354 EAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 403
Cdd:cd01156 322 EKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 36-403 4.37e-121

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: 354.28  E-value: 4.37e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   36 ETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGglgllamdvpeELGGAGldylayaiameeisrgcastgvi 115
Cdd:cd00567   1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELG-----------LLLGAA----------------------- 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  116 msvnnslylgPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAA 195
Cdd:cd00567  47 ----------LLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  196 VVFASTD-RALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIG 274
Cdd:cd00567 117 IVLARTDeEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  275 IASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFI-KEAAMAKLAAS 353
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEArLEAAMAKLFAT 276

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 4557233  354 EAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 403
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 34-408 7.57e-113

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: 335.18  E-value: 7.57e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   34 LPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTG 113
Cdd:cd01162   1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  114 VIMSVNNsLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEAS 193
Cdd:cd01162  81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  194 AAVVFASTDRAlQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRI 273
Cdd:cd01162 160 VYVVMARTGGE-GPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRL 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  274 GIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKP-FIKEAAMAKLAA 352
Cdd:cd01162 239 NIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPdAVKLCAMAKRFA 318

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4557233  353 SEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLR 408
Cdd:cd01162 319 TDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 33-410 3.06e-107

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: 322.11  E-value: 3.06e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   33 ELPETHQMLLQTCRDFAEKELFPiaAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGcAST 112
Cdd:cd01161  26 EQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMD-LGF 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  113 GVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTAR--AEGDSWVLNGTKAWITNAW 190
Cdd:cd01161 103 SVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVlsEDGKHYVLNGSKIWITNGG 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  191 EASAAVVFASTDRALQN----KGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQ 266
Cdd:cd01161 183 IADIFTVFAKTEVKDATgsvkDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMN 262

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  267 TLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDN--KKPFIKE 344
Cdd:cd01161 263 ILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRglKAEYQIE 342

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557233  345 AAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSY 410
Cdd:cd01161 343 AAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHA 408
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 36-407 6.81e-102

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: 307.12  E-value: 6.81e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   36 ETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISR-GCASTGV 114
Cdd:cd01160   1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARaGGSGPGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  115 imSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASA 194
Cdd:cd01160  81 --SLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  195 AVVFASTDR-ALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRI 273
Cdd:cd01160 159 VIVVARTGGeARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERL 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  274 GIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAAS 353
Cdd:cd01160 239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWAT 318

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 4557233  354 EAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLL 407
Cdd:cd01160 319 ELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 34-407 8.25e-101

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: 304.51  E-value: 8.25e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   34 LPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCasTG 113
Cdd:cd01157   1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGC--TG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  114 VIMSVN-NSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEA 192
Cdd:cd01157  79 VQTAIEaNSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  193 SAAVVFASTD---RALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLD 269
Cdd:cd01157 159 NWYFLLARSDpdpKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFD 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  270 MGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAK 349
Cdd:cd01157 239 KTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAK 318

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4557233  350 LAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLL 407
Cdd:cd01157 319 AFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 6-408 4.03e-98

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 298.71  E-value: 4.03e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233     6 LARASGPARRAlcpRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQ--VKKMGGLGLLAMD 83
Cdd:PLN02519   1 MLLSAAKARRR---GLARRFSSSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGIT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    84 VPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDA 163
Cdd:PLN02519  78 APEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   164 GAASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIF 243
Cdd:PLN02519 158 VSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVF 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   244 EDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALES 323
Cdd:PLN02519 238 ENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQS 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   324 ARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 403
Cdd:PLN02519 318 SRSYVYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIG 397


                 ....*
gi 4557233   404 GHLLR 408
Cdd:PLN02519 398 RELFK 402
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 34-403 1.82e-95

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: 291.18  E-value: 1.82e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   34 LPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMdVPEELGGAGLDYLAYAIAMEEISR---GCA 110
Cdd:cd01151  13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVERvdsGYR 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  111 STgviMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAW 190
Cdd:cd01151  92 SF---MSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSP 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  191 EASAAVVFASTDRalqNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILgePGM-GFKIAMQTLD 269
Cdd:cd01151 169 IADVFVVWARNDE---TGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL--PGAeGLRGPFKCLN 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  270 MGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAK 349
Cdd:cd01151 244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLK 323

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 4557233  350 LAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 403
Cdd:cd01151 324 RNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILG 377
PRK12341 PRK12341
acyl-CoA dehydrogenase;
34-411 8.95e-75

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 237.70  E-value: 8.95e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    34 LPETHQMLLQTCRDFAEKElFPIA--AQVDKEHLFPAAQVKKM--GGLGLLAmdVPEELGGAGLDYLAYAIAMEEISRGC 109
Cdd:PRK12341   5 LTEEQELLLASIRELITRN-FPEEyfRTCDENGTYPREFMRALadNGISMLG--VPEEFGGTPADYVTQMLVLEEVSKCG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   110 ASTGVImsvNNSLYLGPILKFGSKEQ-KQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITN 188
Cdd:PRK12341  82 APAFLI---TNGQCIHSMRRFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   189 AWEASAAVVFASTDRA-LQNKGISAFLVPMPTPGLTLGKKEdKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQT 267
Cdd:PRK12341 159 AKEYPYMLVLARDPQPkDPKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYN 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   268 LDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAM 347
Cdd:PRK12341 238 FEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAAL 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4557233   348 AKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQrLVIAGH-LLRSYR 411
Cdd:PRK12341 318 AKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM-IYIAGRqILKDYQ 381
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 35-411 1.75e-69

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 225.20  E-value: 1.75e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    35 PEtHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGV 114
Cdd:PTZ00461  39 PE-HAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   115 IMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGD-SWVLNGTKAWITNAWEAS 193
Cdd:PTZ00461 118 AYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVAD 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   194 AAVVFASTDRAlqnkgISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRI 273
Cdd:PTZ00461 198 VFLIYAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERV 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   274 GIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAA--MLKDNKKPFIKEAamAKLA 351
Cdd:PTZ00461 273 TLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVShnVHPGNKNRLGSDA--AKLF 350

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   352 ASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYR 411
Cdd:PTZ00461 351 ATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKGLK 410
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 42-408 3.80e-64

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: 211.09  E-value: 3.80e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   42 LQTCRDFAEKELFPIAAQVDKE--------HLFPAA---QVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCA 110
Cdd:cd01153   2 LEEVARLAENVLAPLNADGDREgpvfddgrVVVPPPfkeALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  111 STGVIMSVNNSLYLgpILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGD-SWVLNGTKAWITNA 189
Cdd:cd01153  82 PLMYASGTQGAAAT--LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  190 WEASAA----VVFASTDRALQN-KGISAFLVP-----MPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPkdsILGEPGM 259
Cdd:cd01153 160 EHDMSEnivhLVLARSEGAPPGvKGLSLFLVPkflddGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGM 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  260 GFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPL-TKLQV-------IQFKLADMALALESARLLTWRA 331
Cdd:cd01153 237 GLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIkAAPAVtiihhpdVRRSLMTQKAYAEGSRALDLYT 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  332 AMLKD--NKKPFIKEAA------------MAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEI 397
Cdd:cd01153 317 ATVQDlaERKATEGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396

                       410
                ....*....|.
gi 4557233  398 QRLVIAGHLLR 408
Cdd:cd01153 397 QALDLIGRKIV 407
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 34-411 8.32e-60

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 198.90  E-value: 8.32e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    34 LPETHQMLLQTCRDFAEKELF-PIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCAST 112
Cdd:PRK03354   5 LNDEQELFVAGIRELMASENWeAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   113 GVIMSVNNSLylGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEA 192
Cdd:PRK03354  85 YVLYQLPGGF--NTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   193 SAAVVFAStDRALQNKGI-SAFLVPMPTPGLTLGKKEdKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMG 271
Cdd:PRK03354 163 PYIVVMAR-DGASPDKPVyTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   272 RIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLA 351
Cdd:PRK03354 241 RFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYF 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   352 ASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYR 411
Cdd:PRK03354 321 CANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
PLN02526 PLN02526
acyl-coenzyme A oxidase
 29-403 3.45e-58

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 195.46  E-value: 3.45e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    29 YQSVEL--PEtHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVpEELGGAGLDYLAYAIAMEEIS 106
Cdd:PLN02526  23 YQFDDLltPE-EQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   107 RGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWI 186
Cdd:PLN02526 101 RVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWI 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   187 TNAWEASAAVVFAstdRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILgePGM-GFKIAM 265
Cdd:PLN02526 181 GNSTFADVLVIFA---RNTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL--PGVnSFQDTN 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   266 QTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEA 345
Cdd:PLN02526 256 KVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHA 335

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4557233   346 AMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 403
Cdd:PLN02526 336 SLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTG 393
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 71-407 2.94e-57

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: 192.18  E-value: 2.94e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   71 VKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLylGP-ILKFGSKEQKQAWVTPFTSGDKI 149
Cdd:cd01152  41 QRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLA--GPtILAYGTDEQKRRFLPPILSGEEI 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  150 GCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTD-RALQNKGISAFLVPMPTPGLTLGKKE 228
Cdd:cd01152 119 WCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDpEAPKHRGISILLVDMDSPGVTVRPIR 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  229 DKLGirGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIAsqalGIAQTALDCAVNYAENRMAFGAPLTKLQ 308
Cdd:cd01152 199 SING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIG----GSAATFFELLLARLLLLTRDGRPLIDDP 272

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  309 VIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAISHQAIQILGG---MGYVTEMPA-----ER 380
Cdd:cd01152 273 LVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGTaalLRDPAPGAElagrwEA 352

                       330       340
                ....*....|....*....|....*..
gi 4557233  381 HYRDARITEIYEGTSEIQRLVIAGHLL 407
Cdd:cd01152 353 DYLRSRATTIYGGTSEIQRNIIAERLL 379
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 258-403 8.55e-53

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: 173.21  E-value: 8.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    258 GMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDN 337
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557233    338 KKPFIKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 403
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 39-403 6.32e-51

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: 176.04  E-value: 6.32e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   39 QMLLQTCRDFAEKELFPIAAQVDKE-----HLFPAA-----QVKKMG-GLGLLAMDVPEELGGAGLDYLAYAIAMEEISR 107
Cdd:cd01155   4 QELRARVKAFMEEHVYPAEQEFLEYyaeggDRWWTPppiieKLKAKAkAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  108 --------GCAS--TGViMSVnnslylgpILKFGSKEQKQAWVTPFTSGDKIGCFALSEPG-NGSDAGAASTTARAEGDS 176
Cdd:cd01155  84 sffapevfNCQApdTGN-MEV--------LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDD 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  177 WVLNGTKAWITNAWE--ASAAVVFAST--DRALQNKGISAFLVPMPTPGLTlgkKEDKLGIRGSSTA-----NLIFEDCR 247
Cdd:cd01155 155 YVINGRKWWSSGAGDprCKIAIVMGRTdpDGAPRHRQQSMILVPMDTPGVT---IIRPLSVFGYDDAphghaEITFDNVR 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  248 IPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLL 327
Cdd:cd01155 232 VPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLL 311

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4557233  328 TWRAAMLKDNKKPFI--KEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIA 403
Cdd:cd01155 312 VLKAAHMIDTVGNKAarKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIA 389
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 35-147 3.42e-48

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: 159.94  E-value: 3.42e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233     35 PETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGV 114
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 4557233    115 IMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGD 147
Cdd:pfam02771  81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 127-400 8.18e-46

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: 162.93  E-value: 8.18e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  127 ILKFGSKEQKQaWVTPFTSGD-----KIGCFaLSEPGNGSDAGAASTTA-RAEGDSWVLNGTKaWITNAWEASAAVVFAS 200
Cdd:cd01154 123 LRKYGPEELKQ-YLPGLLSDRyktglLGGTW-MTEKQGGSDLGANETTAeRSGGGVYRLNGHK-WFASAPLADAALVLAR 199

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  201 TDRALQN-KGISAFLVPMPTPGLTLGKKE-----DKLGIRGSSTANLIFedcripKDSI---LGEPGMGFKIAMQTLDMG 271
Cdd:cd01154 200 PEGAPAGaRGLSLFLVPRLLEDGTRNGYRirrlkDKLGTRSVATGEVEF------DDAEaylIGDEGKGIYYILEMLNIS 273

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  272 RIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNK---KPfiKEAAMA 348
Cdd:cd01154 274 RLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAaadKP--VEAHMA 351

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4557233  349 KLA-------ASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRL 400
Cdd:cd01154 352 RLAtpvakliACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 41-400 1.09e-32

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 129.99  E-value: 1.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    41 LLQTCRDFAEKELFPIAAQVDKE--HLFPAAQVKKMGGL----------GLLAMDVPEELGGAGLDYLAYAIAMEEISrg 108
Cdd:PTZ00456  63 LLEEASKLATQTLLPLYESSDSEgcVLLKDGNVTTPKGFkeayqalkagGWTGISEPEEYGGQALPLSVGFITRELMA-- 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   109 CASTGVIMSVNNSL-YLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGD-SWVLNGTKAWI 186
Cdd:PTZ00456 141 TANWGFSMYPGLSIgAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFI 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   187 T----NAWEASAAVVFASTDRAL-QNKGISAFLVP--MPTPGLTLGKK--------EDKLGIRGSSTANLIFEDcriPKD 251
Cdd:PTZ00456 221 SagdhDLTENIVHIVLARLPNSLpTTKGLSLFLVPrhVVKPDGSLETAknvkciglEKKMGIKGSSTCQLSFEN---SVG 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   252 SILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGA---------PLTKL----QVIQFKLADMA 318
Cdd:PTZ00456 298 YLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMRAlsgtkepekPADRIichaNVRQNILFAKA 377

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   319 LAlESARLLTWRAAMLKD---NKKPFIKEAAM----------AKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDA 385
Cdd:PTZ00456 378 VA-EGGRALLLDVGRLLDihaAAKDAATREALdheigfytpiAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDA 456

                        410
                 ....*....|....*
gi 4557233   386 RITEIYEGTSEIQRL 400
Cdd:PTZ00456 457 RIGTLYEGTTGIQAL 471
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 151-244 3.23e-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: 114.68  E-value: 3.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    151 CFALSEPGNGSDAGA-ASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKED 229
Cdd:pfam02770   1 AFALTEPGAGSDVASlKTTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80

                          90
                  ....*....|....*
gi 4557233    230 KLGIRGSSTANLIFE 244
Cdd:pfam02770  81 KLGVRGLPTGELVFD 95
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 78-371 1.88e-29

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 120.83  E-value: 1.88e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    78 GLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLylGP---ILKFGSKEQKQAWVTPFTSGDKIGCFAL 154
Cdd:PRK13026 121 GFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSL--GPgelLTHYGTQEQKDYWLPRLADGTEIPCFAL 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   155 SEPGNGSDAGAASTTA-----RAEGDSWV---LNGTKAWITNAWEASA---AVVFASTDRALQNK---GISAFLVPMPTP 220
Cdd:PRK13026 199 TGPEAGSDAGAIPDTGivcrgEFEGEEVLglrLTWDKRYITLAPVATVlglAFKLRDPDGLLGDKkelGITCALIPTDHP 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   221 GLTLGKKEDKLGIR---GSSTANLIFedcrIPKDSILGEP---GMGFKIAMQTLDMGRiGIASQALGIA--QTALDCAVN 292
Cdd:PRK13026 279 GVEIGRRHNPLGMAfmnGTTRGKDVF----IPLDWIIGGPdyaGRGWRMLVECLSAGR-GISLPALGTAsgHMATRTTGA 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   293 YAENRMAFGAPLTKLQVIQFKLADMA---LALESARLLTwrAAMLKDNKKPFIKeAAMAKLAASEAATAISHQAIQILGG 369
Cdd:PRK13026 354 YAYVRRQFGMPIGQFEGVQEALARIAgntYLLEAARRLT--TTGLDLGVKPSVV-TAIAKYHMTELARDVVNDAMDIHAG 430


                 ..
gi 4557233   370 MG 371
Cdd:PRK13026 431 KG 432
PLN02876 PLN02876
acyl-CoA dehydrogenase
 86-403 7.25e-29

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 119.13  E-value: 7.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    86 EELGGAGLDYLAYAIAMEEISR----------GCASTGViMSVnnslylgpILKFGSKEQKQAWVTPFTSGDKIGCFALS 155
Cdd:PLN02876 487 DQLLGAGLSNLEYGYLCEIMGRsvwapqvfncGAPDTGN-MEV--------LLRYGNKEQQLEWLIPLLEGKIRSGFAMT 557

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   156 EPG-NGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAAV--VFASTD-RALQNKGISAFLVPMPTPGLTLGKKEDKL 231
Cdd:PLN02876 558 EPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVliVMGKTDfNAPKHKQQSMILVDIQTPGVQIKRPLLVF 637

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   232 GIRGS--STANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQV 309
Cdd:PLN02876 638 GFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGS 717

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   310 IQFKLADMALALESARLLTWRAAMLKD---NKKPFiKEAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDAR 386
Cdd:PLN02876 718 FLSDLAKCRVELEQTRLLVLEAADQLDrlgNKKAR-GIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATAR 796

                        330
                 ....*....|....*..
gi 4557233   387 ITEIYEGTSEIQRLVIA 403
Cdd:PLN02876 797 TLRIADGPDEVHLGTIA 813
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 111-412 7.12e-24

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: 103.95  E-value: 7.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  111 STGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTAR--AEGDSWVLN-----GTK 183
Cdd:cd01150  97 SLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATydPLTQEFVINtpdftATK 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  184 AWITN-AWEASAAVVFASTDRALQNKGISAFLVPM-------PTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILG 255
Cdd:cd01150 177 WWPGNlGKTATHAVVFAQLITPGKNHGLHAFIVPIrdpkthqPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLN 256

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  256 ----------------EPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFG-------APLTKLQVIQF 312
Cdd:cd01150 257 rfgdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGpkpsdpeVQILDYQLQQY 336

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  313 KLADMalaLESARLLTWRAAMLKDNKKPFIKEAAMAK---------LAASEAATAISH--QAIQIL----GGMGYVTEMP 377
Cdd:cd01150 337 RLFPQ---LAAAYAFHFAAKSLVEMYHEIIKELLQGNsellaelhaLSAGLKAVATWTaaQGIQECreacGGHGYLAMNR 413

                       330       340       350
                ....*....|....*....|....*....|....*
gi 4557233  378 AERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS 412
Cdd:cd01150 414 LPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQ 448
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 78-371 1.43e-21

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 97.19  E-value: 1.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    78 GLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLylGP---ILKFGSKEQKQAWVTPFTSGDKIGCFAL 154
Cdd:PRK09463 122 GFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSL--GPgelLLHYGTDEQKDHYLPRLARGEEIPCFAL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   155 SEPGNGSDAGAASTTARAEGDSWV--------LNGTKAWITNAweASAAVV---FASTD--RALQNK---GISAFLVPMP 218
Cdd:PRK09463 200 TSPEAGSDAGSIPDTGVVCKGEWQgeevlgmrLTWNKRYITLA--PIATVLglaFKLYDpdGLLGDKedlGITCALIPTD 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   219 TPGLTLGKKEDKLGIR---GSSTANLIFedcrIPKDSILGEP---GMGFKIAMQTLDMGR-IGIASQALGIAQTALDCAV 291
Cdd:PRK09463 278 TPGVEIGRRHFPLNVPfqnGPTRGKDVF----IPLDYIIGGPkmaGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATG 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   292 NYAENRMAFGAPLTKLQVIQFKLADM---ALALESARLLTWRAAMLKDnkKPFIKeAAMAKLAASEAA-TAISHqAIQIL 367
Cdd:PRK09463 354 AYARIRRQFKLPIGKFEGIEEPLARIagnAYLMDAARTLTTAAVDLGE--KPSVL-SAIAKYHLTERGrQVIND-AMDIH 429


                 ....
gi 4557233   368 GGMG 371
Cdd:PRK09463 430 GGKG 433
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 57-386 3.76e-21

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: 94.31  E-value: 3.76e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   57 AAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSvNNSLYLGPILKFGSKEQK 136
Cdd:cd01163  14 AAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALR-AHFGFVEALLLAGPEQFR 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  137 QAWVTPFTSGDKIGCfALSEPGnGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRalqNKGISAfLVP 216
Cdd:cd01163  93 KRWFGRVLNGWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEE---GKLVFA-AVP 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  217 MPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLdMGRIGIASQALGIAQTALDCAVNYAEN 296
Cdd:cd01163 167 TDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAGIARAALDDAVAYVRS 245

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  297 --RMAFGAPLTKL----QVIQfKLADMALALESARLLTWRAAMLKDN--KKPFIKEA----------AMAKLAASEAATA 358
Cdd:cd01163 246 rtRPWIHSGAESArddpYVQQ-VVGDLAARLHAAEALVLQAARALDAaaAAGTALTAeargeaalavAAAKVVVTRLALD 324

                       330       340
                ....*....|....*....|....*...
gi 4557233  359 ISHQAIQILGGMGYVTEMPAERHYRDAR 386
Cdd:cd01163 325 ATSRLFEVGGASATAREHNLDRHWRNAR 352
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
274-396 1.82e-18

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 81.24  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    274 GIASQALGIAQTALDCAVNYAENR--MAFGAPLTKLQVIQFKLADMALALESARLLTWRAA----MLKDNKKPF----IK 343
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRvrAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVtpalRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4557233    344 EAAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSE 396
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 137-397 4.51e-18

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 85.96  E-value: 4.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   137 QAWVTPFTS----------GDKIGCF---ALSEPGNGSDAGAASTTA-RAEGDSWVLNGTKaWITNAWEASAAVVFASTD 202
Cdd:PRK11561 154 QDWLTPLLSdrydshllpgGQKRGLLigmGMTEKQGGSDVLSNTTRAeRLADGSYRLVGHK-WFFSVPQSDAHLVLAQAK 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   203 ralqnKGISAFLVPMPTP-----GLTLGKKEDKLGIRGSSTANLIFEDCripKDSILGEPGMGFKIAMQTLDMGRIGIAS 277
Cdd:PRK11561 233 -----GGLSCFFVPRFLPdgqrnAIRLERLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRFDCAL 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   278 QALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDnKKPFIKEAAMAKLAASEAAT 357
Cdd:PRK11561 305 GSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWD-RRADAKEALWARLFTPAAKF 383

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 4557233   358 AISHQ-------AIQILGGMGYVTEMPAERHYRDARITEIYEGTSEI 397
Cdd:PRK11561 384 VICKRgipfvaeAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNI 430
PLN02636 PLN02636
acyl-coenzyme A oxidase
 98-411 3.47e-17

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 83.75  E-value: 3.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    98 YAIAMEEISRGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAE--GD 175
Cdd:PLN02636 123 YFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTD 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   176 SWVLN-----GTKAWITNAW-EASAAVVFA-----STDRAL-QNKGISAFLVPMPT-------PGLTLGKKEDKLGIRGS 236
Cdd:PLN02636 203 EFVINtpndgAIKWWIGNAAvHGKFATVFArlklpTHDSKGvSDMGVHAFIVPIRDmkthqvlPGVEIRDCGHKVGLNGV 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   237 STANLIFEDCRIPKDSILGEPG----------------MGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAF 300
Cdd:PLN02636 283 DNGALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQF 362

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   301 GAP------LTKLQVIQFKLADM-----ALALESARLLTWRAAMLKDNKKPFIkeAAMAKLAASEAATAISHQAIQI--- 366
Cdd:PLN02636 363 GPPkqpeisILDYQSQQHKLMPMlastyAFHFATEYLVERYSEMKKTHDDQLV--ADVHALSAGLKAYITSYTAKALstc 440

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 4557233   367 ---LGGMGY--VTEMPAERHyrDARITEIYEGTSEIQRLVIAGHLLRSYR 411
Cdd:PLN02636 441 reaCGGHGYaaVNRFGSLRN--DHDIFQTFEGDNTVLLQQVAADLLKQYK 488
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 57-386 5.47e-16

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: 78.93  E-value: 5.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   57 AAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNN--SLYLGpilKFGSKE 134
Cdd:cd01159  14 APEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVAthSRMLA---AFPPEA 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  135 QKQAWvtpftsgdkigcfalsepGNGSDAGAAST-----TARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRALQNKG 209
Cdd:cd01159  91 QEEVW------------------GDGPDTLLAGSyapggRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPL 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  210 ISAFLVPMptPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGM------GFKIA---MQTLDMGRIGIASQAL 280
Cdd:cd01159 153 PRAFVVPR--AEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMmagdgpGGSTPvyrMPLRQVFPLSFAAVSL 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233  281 GIAQTALDCAVNYAENRM---AFGAPLTKLQVIQFKLADMALALESARLL---TWRAAM--LKDNKKPFIKEAAMAKLAA 352
Cdd:cd01159 231 GAAEGALAEFLELAGKRVrqyGAAVKMAEAPITQLRLAEAAAELDAARAFlerATRDLWahALAGGPIDVEERARIRRDA 310

                       330       340       350
                ....*....|....*....|....*....|....*...
gi 4557233  353 SEAATaISHQAIQIL----GGMGYVTEMPAERHYRDAR 386
Cdd:cd01159 311 AYAAK-LSAEAVDRLfhaaGGSALYTASPLQRIWRDIH 347
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 126-300 1.86e-12

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 69.10  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   126 PILKF-GSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTAR--AEGDSWVLNGTKAWITNAWE------ASAAV 196
Cdd:PTZ00460 104 PAFQVlGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATydKQTNEFVIHTPSVEAVKFWPgelgflCNFAL 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   197 VFASTDRALQNKGISAFLVPM-------PTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSIL--------------- 254
Cdd:PTZ00460 184 VYAKLIVNGKNKGVHPFMVRIrdkethkPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikvsedgqverq 263

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 4557233   255 GEPGMGFKIAMqtldMGRIGIASQALGIAQTALDCAVNYAENRMAF 300
Cdd:PTZ00460 264 GNPKVSYASMM----YMRNLIIDQYPRFAAQALTVAIRYSIYRQQF 305
PLN02312 PLN02312
acyl-CoA oxidase
 111-300 3.92e-12

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 67.88  E-value: 3.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   111 STGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAAST--TARAEGDSWVLN-----GTK 183
Cdd:PLN02312 148 SLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETvtTYDPKTEEFVINtpcesAQK 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   184 AWITNAWE-ASAAVVFASTDRALQNKGISAFLVPMPT------PGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILG- 255
Cdd:PLN02312 228 YWIGGAANhATHTIVFSQLHINGKNEGVHAFIAQIRDqdgnicPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNs 307

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   256 ---------------EPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAF 300
Cdd:PLN02312 308 vadvspdgkyvsaikDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
PLN02443 PLN02443
acyl-coenzyme A oxidase
 131-313 4.18e-11

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 64.86  E-value: 4.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   131 GSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTAR--AEGDSWVLN-----GTKAWITNAWEASA-AVVFASTD 202
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATfdPKTDEFVIHsptltSSKWWPGGLGKVSThAVVYARLI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   203 RALQNKGISAFLVP-------MPTPGLTLGKKEDKLGIRGSSTAN---LIFEDCRIPKDSILGEPGMGFK---------- 262
Cdd:PLN02443 194 TNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSKVTRegkyvqsdvp 273

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4557233   263 --IAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAP--LTKLQVIQFK 313
Cdd:PLN02443 274 rqLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQdgGPETQVIDYK 328
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 87-282 1.10e-04

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 44.49  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233    87 ELGGAGLDYLAYAIAMEEISRGCASTgVIMSVNNSLYLGPILK-FGSKEQKQAWVTPFTSGDKIGCFALSEpGNGSDAGA 165
Cdd:PTZ00457  73 EYGGLGLGHTAHALIYEEVGTNCDSK-LLSTIQHSGFCTYLLStVGSKELKGKYLTAMSDGTIMMGWATEE-GCGSDISM 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557233   166 ASTTARAEGD-SWVLNGTKAWItNAWEASAAVVFAST-------DRALQNKGISAFLVPMPTPGLTlgkkedklgIRGSS 237
Cdd:PTZ00457 151 NTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKTltqtaaeEGATEVSRNSFFICAKDAKGVS---------VNGDS 220

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 4557233   238 TAnliFEDcrIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGI 282
Cdd:PTZ00457 221 VV---FEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGI 260
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
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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