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Database: UniProt
Entry: A0A0F7M4L0_9GAMM
LinkDB: A0A0F7M4L0_9GAMM
Original site: A0A0F7M4L0_9GAMM 
ID   A0A0F7M4L0_9GAMM        Unreviewed;       388 AA.
AC   A0A0F7M4L0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AKH70450.1};
GN   ORFNames=IMCC21906_02807 {ECO:0000313|EMBL:AKH70450.1};
OS   Spongiibacter sp. IMCC21906.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae; Spongiibacter.
OX   NCBI_TaxID=1620392 {ECO:0000313|EMBL:AKH70450.1, ECO:0000313|Proteomes:UP000035013};
RN   [1] {ECO:0000313|EMBL:AKH70450.1, ECO:0000313|Proteomes:UP000035013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC21906 {ECO:0000313|EMBL:AKH70450.1,
RC   ECO:0000313|Proteomes:UP000035013};
RA   Cho J.-C., Yang S.-J., Kang I.;
RT   "Complete genome sequence of IMCC21906 belonging to the
RT   Gammaproteobacteria.";
RL   Submitted (MAY-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; CP011477; AKH70450.1; -; Genomic_DNA.
DR   RefSeq; WP_047012659.1; NZ_CP011477.1.
DR   AlphaFoldDB; A0A0F7M4L0; -.
DR   STRING; 1620392.IMCC21906_02807; -.
DR   KEGG; spoi:IMCC21906_02807; -.
DR   PATRIC; fig|1620392.3.peg.2910; -.
DR   OrthoDB; 6138585at2; -.
DR   Proteomes; UP000035013; 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; PTHR43831; ISOBUTYRYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43831:SF1; ISOBUTYRYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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   PIRSF; PIRSF016578; HsaA; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035013}.
FT   DOMAIN          6..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..379
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   388 AA;  41866 MW;  9797E4A79DA37669 CRC64;
     MDFNLTEDQK AYAESARSFA EGVFMPNAAE WDAEHIFPKD ALKAAGELGF MGLYTPEEAG
     GLGMSRLDTS VIVEELARGC TSTAAFLTIH NMATSMIGAY GNTETIEKWC PELVTGEKLA
     SYCLTEPGAG SDAGNLRSTA KKDGDNYIVN GSKMFISGAG DTDVLVAMLR TGDADSGARG
     ISAFAIPADA DGISYGKKEE KMGWNSQPTR AVTFEDVVVP ASAMLGSEGE GFKIAMKGLD
     GGRINIATCS IGTAQAALET AVEYVKERKQ FGQAIAGFQN TQFKLADMAT QLVASRQMVR
     LAAFKLDNKD PEATTYCAMA KRFVTDVCFD ICNDALQLHG GYGYIKEYPL ERHVRDNRVH
     QILEGTNEIM RVIIGRRLLM EGSLEVVK
//
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