ID A0A0D0QH12_9RHOB Unreviewed; 567 AA.
AC A0A0D0QH12;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KIQ70333.1};
GN ORFNames=Wenmar_00708 {ECO:0000313|EMBL:KIQ70333.1};
OS Wenxinia marina DSM 24838.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Wenxinia.
OX NCBI_TaxID=1123501 {ECO:0000313|EMBL:KIQ70333.1, ECO:0000313|Proteomes:UP000035100};
RN [1] {ECO:0000313|EMBL:KIQ70333.1, ECO:0000313|Proteomes:UP000035100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24838 {ECO:0000313|EMBL:KIQ70333.1,
RC ECO:0000313|Proteomes:UP000035100};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (JAN-2013) 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:KIQ70333.1}.
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DR EMBL; AONG01000005; KIQ70333.1; -; Genomic_DNA.
DR RefSeq; WP_018304078.1; NZ_KN848371.1.
DR AlphaFoldDB; A0A0D0QH12; -.
DR STRING; 1123501.Wenmar_00708; -.
DR PATRIC; fig|1123501.6.peg.775; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 9807883at2; -.
DR Proteomes; UP000035100; 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; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12418; AcylCoA_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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000035100}.
FT DOMAIN 3..33
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 37..156
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 161..269
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 280..437
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 453..560
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 567 AA; 59303 MW; F773B299A7925F47 CRC64;
MPYAAPVSEI RFLLDHVAGF PTVSATDRFA EASGETVEAI LTEAGKLCDE VLAPLQRKGD
TDPARLENGV VRTPEGFGDG FRAIAEGGWI GLAAPERYGG MALPQTLAVA VNDMMSGACL
ALELNPLMSQ GQIEALEHHA SDEMKALYIP KLISGEWCGT MNLTEPQAGS DVGALATRAE
PNGDGTYAVT GQKIYITWAD NDFSANVCHL VLARLPDAVP GTKGISLFMV PKFLPEADGS
PGARNALRVV SLEHKLGLHG SPTAVMSYEG ATGWLVGEPN GGMAAMFTMM NNARLGVGVQ
GIGVAEAATQ AALAYAMERR QGRVGGSGTI VEHADVRRML ATMRAETFAA RAIALMCGVA
IDLHTATGEA QHAARAAFLT PIAKAFGTET GIDVANLGVQ VHGGMGFIEE TGAAQFLRDV
RVTAIYEGTN GIQALDLVGR KLADGGEAAL RLLDEVEAGA EAAKADGLTE LAEAVWDAAE
TLRETTEWLV AQPPAERGAA AVPYLKAFAR VLGGHAHLAA ARAGDARRQR LAAFYIARLL
PEHAGLLRHV RAGAEALMAI TADDLAA
//
