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Database: UniProt
Entry: A0A0U1NJL8_9RHOB
LinkDB: A0A0U1NJL8_9RHOB
Original site: A0A0U1NJL8_9RHOB 
ID   A0A0U1NJL8_9RHOB        Unreviewed;       562 AA.
AC   A0A0U1NJL8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:CRK74920.1};
DE            EC=1.3.99.- {ECO:0000313|EMBL:CRK74920.1};
GN   Name=mmgC_1 {ECO:0000313|EMBL:CRK74920.1};
GN   ORFNames=NIG5292_00961 {ECO:0000313|EMBL:CRK74920.1};
OS   Nereida ignava.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Nereida.
OX   NCBI_TaxID=282199 {ECO:0000313|EMBL:CRK74920.1, ECO:0000313|Proteomes:UP000048949};
RN   [1] {ECO:0000313|EMBL:CRK74920.1, ECO:0000313|Proteomes:UP000048949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5292 {ECO:0000313|EMBL:CRK74920.1,
RC   ECO:0000313|Proteomes:UP000048949};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-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; CVQV01000005; CRK74920.1; -; Genomic_DNA.
DR   RefSeq; WP_048598359.1; NZ_CVQV01000005.1.
DR   AlphaFoldDB; A0A0U1NJL8; -.
DR   STRING; 282199.GCA_001049735_00960; -.
DR   OrthoDB; 9775090at2; -.
DR   Proteomes; UP000048949; 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: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,
KW   ECO:0000313|EMBL:CRK74920.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000048949}.
FT   DOMAIN          179..290
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          296..398
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          412..561
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   562 AA;  61427 MW;  262579C69EB5DA4F CRC64;
     MAHDGQDMTL TQATVLPDLL ALTADAIAPC EKVLETAKEC LRATVTDGDR ISGALIEQNQ
     TAAHGLAWLA TYVEALRQMQ NWAEGLQASG TFGETEQLLH QIAFGEYLWQ IYGGIPMNQG
     EILRLQDIGM TQEQMGALMT PAVMKLTQSG NTQAARSRLV ELMQEQSANI TVGASGLDEE
     LEMIREQFRR YAVEKVEPFA HEWHLKDELI PMEIIEELAE MGVFGLTIPE EYGGFGLSKA
     SMCVVSEELS RGYIGVGSLG TRSEIAAELI ICGGTEEQKQ KWLPRLASAE TLPTAVFTEP
     NTGSDLGALR TRAVKDDNGD YAVTGNKTWI THATRTQIMT LLARTDPETT NYKGLSMFIA
     EKTPGTEENP FPTEGMTGGE IEVLGYRGMK EYELAFDNFH VKGENLLGGT EGMGFKHLME
     TFESARIQTA ARAVGVAASA LDVGMQYALD RKQFGKALIN FPRVSSKLAM MAVETMVARQ
     LTYFSANEKD EGRRCDLEAG MAKLLGARVA WAAADNALQV HGGNGFALEY KISRILCDAR
     ILNIFEGAAE IQAQVIARRL LG
//
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