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
//