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Database: UniProt
Entry: A0A0P1F3X5_THAGE
LinkDB: A0A0P1F3X5_THAGE
Original site: A0A0P1F3X5_THAGE 
ID   A0A0P1F3X5_THAGE        Unreviewed;       383 AA.
AC   A0A0P1F3X5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:CUH62315.1};
DE            EC=1.3.99.- {ECO:0000313|EMBL:CUH62315.1};
GN   Name=mmgC_1 {ECO:0000313|EMBL:CUH62315.1};
GN   ORFNames=TG4357_00003 {ECO:0000313|EMBL:CUH62315.1};
OS   Thalassovita gelatinovora (Thalassobius gelatinovorus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Thalassovita.
OX   NCBI_TaxID=53501 {ECO:0000313|EMBL:CUH62315.1, ECO:0000313|Proteomes:UP000051587};
RN   [1] {ECO:0000313|EMBL:CUH62315.1, ECO:0000313|Proteomes:UP000051587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 4357 {ECO:0000313|EMBL:CUH62315.1,
RC   ECO:0000313|Proteomes:UP000051587};
RG   Swine Surveillance;
RL   Submitted (SEP-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; CYSA01000001; CUH62315.1; -; Genomic_DNA.
DR   RefSeq; WP_058260827.1; NZ_FOFW01000018.1.
DR   AlphaFoldDB; A0A0P1F3X5; -.
DR   STRING; 53501.SAMN04488043_1184; -.
DR   OrthoDB; 9775090at2; -.
DR   Proteomes; UP000051587; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 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; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051587}.
FT   DOMAIN          2..112
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          117..215
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          228..361
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   383 AA;  42472 MW;  B4C9A8C2C6F976F2 CRC64;
     MTDSYEEIRD AVRALCATFP PEYHRKVDED RAYPEAFVDA LTEAGWLAAL IPEEFGGSGL
     GLTEASVIME EINRAGGNSG ACHGQMYNMG TLLRHGSEAQ KLKYLPKIAS GELRLQSMGV
     TEPTTGTDTT KIKTTAVKKG DRYVVNGQKV WISRVQHSDL MILLARTTPL TEVKKKSHGM
     SIFIVDLKDA IGNGMDVKPI PNMVNHETNE LFFDNLEIPE ENLIGEEGMG FKYILDGLNA
     ERTLIAAECI GDGYWFIDKV SDYVKERTVF GRPIGQNQGV QFPIAEAHIE VEAANLMRFE
     ACRLFDAKQP CGAQANMAKY LAAKASWEAA NACLQFHGGF GFANEYDVER KFRETRLYQV
     APISTNLILS YVAEHVLGLP RSF
//
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