ID A0A023BWQ6_9FLAO Unreviewed; 603 AA.
AC A0A023BWQ6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EZH74043.1};
GN ORFNames=ATO12_14295 {ECO:0000313|EMBL:EZH74043.1};
OS Aquimarina atlantica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=1317122 {ECO:0000313|EMBL:EZH74043.1, ECO:0000313|Proteomes:UP000023541};
RN [1] {ECO:0000313|EMBL:EZH74043.1, ECO:0000313|Proteomes:UP000023541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S11-z7 {ECO:0000313|EMBL:EZH74043.1,
RC ECO:0000313|Proteomes:UP000023541};
RA Lai Q.;
RT "Aquimarina sp. 22II-S11-z7 Genome Sequencing.";
RL Submitted (APR-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:EZH74043.1}.
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DR EMBL; AQRA01000004; EZH74043.1; -; Genomic_DNA.
DR RefSeq; WP_034241562.1; NZ_AQRA01000004.1.
DR AlphaFoldDB; A0A023BWQ6; -.
DR STRING; 1317122.ATO12_14295; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 9802867at2; -.
DR Proteomes; UP000023541; 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; 2.
DR InterPro; IPR049426; Acyl-CoA-dh-like_C.
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:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF21263; Acyl-CoA-dh_C; 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; PS00072; ACYL_COA_DH_1; 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:UP000023541}.
FT DOMAIN 33..146
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 150..244
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 257..419
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 470..573
FT /note="Acyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21263"
SQ SEQUENCE 603 AA; 66624 MW; AE380A992F25D823 CRC64;
MSDKTINKDI LRGGQFLVKE TNCEDVFTPE DFSEEQRMMR DSAKEFVDRE LWAHWERFES
KDYAFTEECM RKAGELGLLG VSVPEAYDGL GMGFVSTMLV CDYISGATGS FSTAFGAHTG
IGTMPITLYG NEEQKKKYVP KLATGEWFGA YCLTEPGAGS DANSGKTKAV LSEDGTHYLI
SGQKMWISNA GFCSLFIVFA RIEDDKNITG FIVENDPSNG ISLGDEEKKL GIHSSSTRQV
FFSDTKVPVE NMLSERGNGF KIAMNALNVG RIKLAAACLD AQRRVIGEAT KYANERIQFK
TPIMNFGAIK AKIAEMATNV YADESASYRA AKNIEDRIAI RQAEGNTHQE AELKGVEEYA
IECSILKVAV SEDVQSCTDE GVQIFGGMGF SADTPMESAW RDARISRIYE GTNEINRMLA
VGMLVKKAMK GHVDLLGPAM KVADELTGIP SFDTPDYSVL FSEEKEIIAK LKKVFLMVAG
AAVQKFGPQL EEHQQLLLAA SDILIEIYMA ESAILRTEKN AKRFGEEAQE TQIAMSQLYL
YNAVDIVIKK GKEGIVSFAE GDEQRMMLMG LKRFTKYANQ PNVVALRTKI ADKIAKENGY
FIG
//
