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Database: UniProt
Entry: F1W545_9BURK
LinkDB: F1W545_9BURK
Original site: F1W545_9BURK 
ID   F1W545_9BURK            Unreviewed;       319 AA.
AC   F1W545;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:EGF30026.1};
GN   ORFNames=IMCC9480_2720 {ECO:0000313|EMBL:EGF30026.1};
OS   Oxalobacteraceae bacterium IMCC9480.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae.
OX   NCBI_TaxID=937450 {ECO:0000313|EMBL:EGF30026.1, ECO:0000313|Proteomes:UP000004494};
RN   [1] {ECO:0000313|EMBL:EGF30026.1, ECO:0000313|Proteomes:UP000004494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC9480 {ECO:0000313|EMBL:EGF30026.1,
RC   ECO:0000313|Proteomes:UP000004494};
RX   PubMed=21572000; DOI=10.1128/JB.05088-11;
RA   Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., Cho J.C.;
RT   "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing
RT   betaproteobacterium isolated from the Arctic Ocean.";
RL   J. Bacteriol. 193:3421-3421(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGF30026.1}.
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DR   EMBL; AEPR01000973; EGF30026.1; -; Genomic_DNA.
DR   AlphaFoldDB; F1W545; -.
DR   Proteomes; UP000004494; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; 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; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 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};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004494}.
FT   DOMAIN          52..146
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          158..305
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   319 AA;  34975 MW;  FEF623063DE6918A CRC64;
     MFEAAGYSPL GPVALNIHAP DEGNIHLMEH VASPAQKERW LRPLVEGRIR SCFAMTEPAP
     GAGSDPSMMQ TIAIQDGDDY LISGTKWFIT GAEGASFAII MARMEDGSAT MFLSDMDRPG
     IVLERLMESL DSCFAGGHGV LRFENVRVPA TDVLGEIGKG FRYAQIRLAP ARLTHCMRWL
     GQAQRAHDVA LDYASERQAF GKSLGEHEGV GFMLADNAMD LHTARLNILH TAWVLDEGGR
     GNIESSMTKV ICSEAIWRVV DRCVQILGGR GVTAETIVMR IFKDVRGFRI YDGPSEVHRW
     SIANKLVGAR KKEQGTATS
//
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