ID A0A0C1UEH5_9ACTN Unreviewed; 420 AA.
AC A0A0C1UEH5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KIE51159.1};
GN ORFNames=MB52_03820 {ECO:0000313|EMBL:KIE51159.1};
OS marine actinobacterium MedAcidi-G1.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1550399 {ECO:0000313|EMBL:KIE51159.1, ECO:0000313|Proteomes:UP000031399};
RN [1] {ECO:0000313|EMBL:KIE51159.1, ECO:0000313|Proteomes:UP000031399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL Submitted (SEP-2014) 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:KIE51159.1}.
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DR EMBL; JUEM01000008; KIE51159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1UEH5; -.
DR Proteomes; UP000031399; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 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.
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 63..139
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 145..239
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 251..400
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 420 AA; 46983 MW; ADC26424DEF3491B CRC64;
MINDITLNEF ESKARNWLDA NAQKKQAVSE KEAEWGEGEF SVSVFHNLTF EEERDLLQEA
AEWQIAKSEE GYHAITWPTQ YGGLDLPIEY ARAFARLESD YITPSRHETF SVTTRLIAPT
VLHYGTDDQK DELLSDLFSA RIYCCQLFSE PGTGSDLAGL GCKAVKDGDE WVINGQKVWS
SGAQFSQWGE LIARTHFDQP KHKGMTAFII PMDLPGIEIR QIRQMSGGTS FNEVFFSDVR
VPDNLRLGPE GEGWGVALTT LSFERDHSDS DGGGRAGGKW SQLLDTAKSL DLLQDPQIRQ
RLMEVYTQTQ IQRFVNRRAA DLRKSGKPPG PEGSLGKLLW TEGMGLMSDV VSEILGPRLI
ADTETWGTYE WGEHVLGAPG YRIAGGSDEI QRNIIGERVL GLPKEPDPYK GLPWEEIPKN
//
