ID J5K9C5_9GAMM Unreviewed; 406 AA.
AC J5K9C5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 08-NOV-2023, entry version 32.
DE SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:EJP72188.1};
GN ORFNames=NT01SARS_0683 {ECO:0000313|EMBL:EJP72188.1};
OS SAR86 cluster bacterium SAR86A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX NCBI_TaxID=1123866 {ECO:0000313|EMBL:EJP72188.1, ECO:0000313|Proteomes:UP000010305};
RN [1] {ECO:0000313|EMBL:EJP72188.1, ECO:0000313|Proteomes:UP000010305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22170421; DOI=10.1038/ismej.2011.189;
RA Dupont C.L., Rusch D.B., Yooseph S., Lombardo M.J., Richter R.A., Valas R.,
RA Novotny M., Yee-Greenbaum J., Selengut J.D., Haft D.H., Halpern A.L.,
RA Lasken R.S., Nealson K., Friedman R., Venter J.C.;
RT "Genomic insights to SAR86, an abundant and uncultivated marine bacterial
RT lineage.";
RL ISME J. 6:1186-1199(2012).
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; JH611156; EJP72188.1; -; Genomic_DNA.
DR AlphaFoldDB; J5K9C5; -.
DR STRING; 1123866.NT01SARS_0683; -.
DR HOGENOM; CLU_018204_9_2_6; -.
DR Proteomes; UP000010305; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000010305}.
FT DOMAIN 6..124
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 128..222
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 234..384
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 406 AA; 44966 MW; 345EF5BCC90D4339 CRC64;
MDFNDTPEQA KFRKTCRDWL EKNAQLKDSS PSESNFANKD IIKEAKAWQK KKYDAGWAML
HWPKEYGGIG ASPIERIIWA NEESKFNVPK GIFEIGLGMC GPVMMQYASE EQKERYLPPM
AEGKEIWCQL FSEPSAGSDV AGLRSKAVQD GDKWIINGQK VWTSGAHFSD YGILVVRHDP
NLEKHKGLTF FFVDMKSPGI EVKPIKQITG GSSFNEVYFT DVEIPDSQRL GEIGDGWKVA
ITTLMNERLA VGDADGCDVE DAFKWAKTQD NQGEPLLNDK AARESIADWY CEASGLKNTK
LRTMSALSKG DTPGPEASIT KIVSAGKLQD IGNFGIDSMD MTGMLKTDDP DIRRFQNAWL
GAPGLRIAGG TDEILRNIIA ERVLGLPQDP RADKGVAYKD IPSGKS
//
