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Database: UniProt
Entry: A0A238JJK1_9RHOB
LinkDB: A0A238JJK1_9RHOB
Original site: A0A238JJK1_9RHOB 
ID   A0A238JJK1_9RHOB        Unreviewed;       563 AA.
AC   A0A238JJK1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SMX30839.1};
DE            EC=1.3.99.- {ECO:0000313|EMBL:SMX30839.1};
GN   Name=mmgC_2 {ECO:0000313|EMBL:SMX30839.1};
GN   ORFNames=COL8621_00145 {ECO:0000313|EMBL:SMX30839.1};
OS   Actibacterium lipolyticum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Actibacterium.
OX   NCBI_TaxID=1524263 {ECO:0000313|EMBL:SMX30839.1, ECO:0000313|Proteomes:UP000202922};
RN   [1] {ECO:0000313|Proteomes:UP000202922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8621 {ECO:0000313|Proteomes:UP000202922};
RA   Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL   Submitted (MAY-2017) 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; FXYE01000001; SMX30839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238JJK1; -.
DR   Proteomes; UP000202922; 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 YDBM-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   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:SMX30839.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000202922}.
FT   DOMAIN          181..292
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          298..398
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          413..562
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   563 AA;  61308 MW;  2B225C684F2E0C1D CRC64;
     MPHDGQDMPQ NDVKNAILPD LLKLTGAAVG PVEALLATAT EKMRTALTVD GRVSGAALEA
     EQHGAHALAW LATYVEALRQ MHAWANKLNT DGQLGEMEQL LLQIAFGEYL TQIQGGIPMS
     QGEMARLQDM GLSRTEQSVL DTAEITALCD GGNTSVARMR LVELMQDNHG HATFGSTGLD
     EELEMIREQF RRFADERVVP NAHEWHLKDE LIPMEIIEEL AELGVFGLTI PEEFGGFGLS
     KASMVVVSEE LSRGYIGVGS LGTRSEIAAE LILCGGTDEQ KANWLPKLAS AEILPTAVFT
     EPNTGSDLGS LRTRAVKEGD DYKVTGNKTW ITHAARTHVM TMLARTDPDT TDYKGLSMFL
     AEKTPGTDAD PFPTPGMTGG EIEVLGYRGM KEYELAFDGF EIKGENLLGG VEGQGFKQLM
     QTFESARIQT AARAVGVAQN ALEVGMQYAL DRKQFGKSLI NFPRVGGKLA MMAVEIMVAR
     QLTYFSAWEK DHDRRCDLEA GMAKLLGARV AWACADNALQ IHGGNGFALE YQISRILCDA
     RILNIFEGAA EIQAQVIARR VLG
//
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