ID A0A0D6AZL8_RHOSU Unreviewed; 560 AA.
AC A0A0D6AZL8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:BAQ68186.1};
GN ORFNames=NHU_01021 {ECO:0000313|EMBL:BAQ68186.1};
OS Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=35806 {ECO:0000313|EMBL:BAQ68186.1, ECO:0000313|Proteomes:UP000064912};
RN [1] {ECO:0000313|EMBL:BAQ68186.1, ECO:0000313|Proteomes:UP000064912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2351 {ECO:0000313|EMBL:BAQ68186.1,
RC ECO:0000313|Proteomes:UP000064912};
RA Nagao N.;
RT "Genome sequene of Rhodovulum sulfidophilum DSM 2351.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; AP014800; BAQ68186.1; -; Genomic_DNA.
DR RefSeq; WP_060834086.1; NZ_AP014800.1.
DR AlphaFoldDB; A0A0D6AZL8; -.
DR KEGG; rsu:NHU_01021; -.
DR PATRIC; fig|35806.4.peg.1045; -.
DR eggNOG; COG1960; Bacteria.
DR Proteomes; UP000064912; Chromosome.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
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 PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF25; ACYL-COA DEHYDROGENASE; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 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.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT DOMAIN 178..289
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 295..396
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 410..559
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 560 AA; 60721 MW; 131CC9B7F2DBEB04 CRC64;
MPHDGQDRPA ETALLADLLT LTEAALGPVE AVTEAARAAL AARVTEEGRV SGRLVEAEQH
AAHGLAWLAT YARALRQMRG WADRLTEQGK FGEIEQLILQ IAFGEYLAQI AGGIPMSQGE
IVRLPELGVS SEAHHAFYSD AVSALIRGGN TPAARARLVA LMREQVANVT LGATGLDDEL
EMIREQFRRF ALDRVEPNAH DWHLNDTLIP MEVIEEMAEL GVFGLTIPEE FGGFGLSKAS
MCVVSEELSR GYIGVGSLGT RSEIAAELIL CGGTDEQKAH WLPKIASGEI LPTAVFTEPN
TGSDLGALRT RAVKAGETYE VTGNKTWITH AARAHVMTLL ARTDPETTDY KGLSMFLAEK
TPGTEDAPFP SPGMTGGEIE VLGYRGMKEY ELGFDRFEVP AENLLGGVEG QGFKQLMQTF
ESARIQTAAR AIGVAQSALD VSMRYAEDRK QFGKPLIAFP RVADKLAMMA VEIMVARQLT
YFAAWEKDHD RRCDLEAGMA KLLGARVAWA AADNGLQIHG GNGFALEYTI SRILCDARIL
NIFEGAAEIQ AQVIARRVLG
//
