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Database: UniProt
Entry: A0A3P1SX56_9GAMM
LinkDB: A0A3P1SX56_9GAMM
Original site: A0A3P1SX56_9GAMM 
ID   A0A3P1SX56_9GAMM        Unreviewed;       385 AA.
AC   A0A3P1SX56;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RRD01116.1};
GN   ORFNames=EHS89_00700 {ECO:0000313|EMBL:RRD01116.1};
OS   Amphritea balenae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Amphritea.
OX   NCBI_TaxID=452629 {ECO:0000313|EMBL:RRD01116.1, ECO:0000313|Proteomes:UP000267535};
RN   [1] {ECO:0000313|EMBL:RRD01116.1, ECO:0000313|Proteomes:UP000267535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAMM 1525 {ECO:0000313|EMBL:RRD01116.1,
RC   ECO:0000313|Proteomes:UP000267535};
RA   Fang Z., Zhang Y., Han X.;
RT   "The draft genome sequence of Amphritea balenae JAMM 1525T.";
RL   Submitted (NOV-2018) 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}.
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:RRD01116.1}.
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DR   EMBL; RQXV01000001; RRD01116.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P1SX56; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000267535; Unassembled WGS sequence.
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; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 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          6..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..215
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          227..377
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   385 AA;  42120 MW;  66A7FFF8293BC5AA CRC64;
     MDFELNEDQV AFADMARTFA QNELAPNAGE WDLHQTFPVE VLKAAGELGF CGLYSHEDVG
     GLGMSRLDSS IIFEQLAMGC TSTTAFITIH NMATWMISEF GAEDVRQQWC PELTAGEKLA
     SYCLTEPNAG SDAASLKTSA RRDGDDYILN GSKIFISGAG STDCLVVMAR TGVDGPKGIS
     AFAIDANLPG ITYGRKEEKM GWNSQPTRMI TFEDVRIPAS AILGQEGDGF KIAMRGLDGG
     RINIATCSIG TAQQALDKAT EYMHERKQFG KTLSNFQALQ FKLANSATEL VAARQMVRMA
     ASRLDNNHPD KTTYCAMAKR FATDVGFNVA DEALQIFGGN GYIKEYPMER FLRDNRVHRI
     LEGTNEIMNV IIARRLLLEN AAAVL
//
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