ID A0A1H7SCK8_9GAMM Unreviewed; 825 AA.
AC A0A1H7SCK8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Acyl-coenzyme A dehydrogenase {ECO:0000256|ARBA:ARBA00020144};
DE EC=1.3.8.7 {ECO:0000256|ARBA:ARBA00012033};
DE EC=1.3.8.8 {ECO:0000256|ARBA:ARBA00012040};
GN ORFNames=SAMN05428989_2267 {ECO:0000313|EMBL:SEL69474.1};
OS Pseudoxanthomonas sp. GM95.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1881043 {ECO:0000313|EMBL:SEL69474.1, ECO:0000313|Proteomes:UP000199164};
RN [1] {ECO:0000313|Proteomes:UP000199164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM95 {ECO:0000313|Proteomes:UP000199164};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721,
CC ChEBI:CHEBI:83727; EC=1.3.8.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723,
CC ChEBI:CHEBI:83726; EC=1.3.8.7;
CC Evidence={ECO:0000256|ARBA:ARBA00034035};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR EMBL; FOAX01000002; SEL69474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7SCK8; -.
DR STRING; 1881043.SAMN05428989_2267; -.
DR OrthoDB; 9802447at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000199164; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IEA:InterPro.
DR CDD; cd00567; ACAD; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR015396; FadE_C.
DR PANTHER; PTHR48083:SF18; ACYL-COENZYME A DEHYDROGENASE; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF09317; ACDH_C; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 141..237
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 364..509
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 518..801
FT /note="Acyl-CoA dehydrogenase C-terminal bacterial-type"
FT /evidence="ECO:0000259|Pfam:PF09317"
SQ SEQUENCE 825 AA; 88965 MW; BF40428BD2B62729 CRC64;
MSILVPFLAV LLAAGLAAYH RMRLATWAAI SACALVACWL LGASAVACVI AAVIVAAITL
PLLLPPVRKA LVTAPMMKFF RKVLPPLSQT ERIALETGSV GFEGELFTGD PDWQKLLNYP
KPQLTAEEQA FIDGPVEELC TMINDWEITH VRADLPPQVW DFVKQHKFFG MIIPKEFGGL
GFSALMHHKV IQKISSISSV ASSTVGVPNS LGPGELLVHY GTQEQKDYYL PRLAAGQEVP
CFGLTGPFAG SDATSIPDYG IVCKGEWNGA NVLGVKLTFD KRYITLAPVA TLIGLAFRMY
DPDGLIGDTK DIGITLALLP RETPGVDIGR RHFPLNSPFQ NGPIHGKEVF IPLSQLIGGA
DMAGKGWNML NECLAVGRSI TLPSTASGGA KFGAVVTGTY ARIRKQFGLS IGRFEGVEEA
LARIGGKAYA ISALAQATAA AVDRGDVPSV PSAIAKYHCT NMGREVVSDV MDVVGGKGII
LGPKNFAGRS WQAAPIGITV EGANIMTRSL LIFGQGAILC HPWVMKEMKA AQDPDHAAGL
EAFDRSLFGH ISFGISNAVR SFWFGLTAAR IGAAPGDAYT KRFFRKLDRY SANLALMADV
SMLMLGGKLK FKESLSGRLG DVLSHIYMTS AMLKRYHDDG APQAEQPLLA WAFHHSVHEI
ELALSAALRN FPIRPVGWLM WVLIFPWGRR AEAPGDRLGH RVAALLMAPN AARDQLAKGV
FLTPCENNPG GRIASYLAKA VAAEPVERKF IKALKTKGIE ALDFPSQLDE AVREGLITAD
ERLQLEELRA LTMDTISVDD FDAEELRSAG YRPDALDEAA SREAA
//
