ID D5BS73_PUNMI Unreviewed; 396 AA.
AC D5BS73;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ADE39120.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:ADE39120.1};
GN OrderedLocusNames=SAR116_0877 {ECO:0000313|EMBL:ADE39120.1};
OS Puniceispirillum marinum (strain IMCC1322).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster;
OC Puniceispirillum.
OX NCBI_TaxID=488538 {ECO:0000313|EMBL:ADE39120.1, ECO:0000313|Proteomes:UP000007460};
RN [1] {ECO:0000313|EMBL:ADE39120.1, ECO:0000313|Proteomes:UP000007460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC1322 {ECO:0000313|EMBL:ADE39120.1,
RC ECO:0000313|Proteomes:UP000007460};
RX PubMed=20382761; DOI=10.1128/JB.00347-10;
RA Oh H.M., Kwon K.K., Kang I., Kang S.G., Lee J.H., Kim S.J., Cho J.C.;
RT "Complete genome sequence of "Candidatus Puniceispirillum marinum"
RT IMCC1322, a representative of the SAR116 clade in the
RT Alphaproteobacteria.";
RL J. Bacteriol. 192:3240-3241(2010).
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; CP001751; ADE39120.1; -; Genomic_DNA.
DR RefSeq; WP_013045749.1; NC_014010.1.
DR AlphaFoldDB; D5BS73; -.
DR STRING; 488538.SAR116_0877; -.
DR KEGG; apb:SAR116_0877; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_2_5; -.
DR OrthoDB; 9780544at2; -.
DR Proteomes; UP000007460; Chromosome.
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:SF20; ACYL-COA DEHYDROGENASE FADE28; 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 PIRSF; PIRSF016578; HsaA; 2.
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|RuleBase:RU362125,
KW ECO:0000313|EMBL:ADE39120.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007460}.
FT DOMAIN 21..124
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 130..229
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 241..389
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 396 AA; 42827 MW; F8F451AB28A18DDA CRC64;
MTPTQNANRP AGLNAGLYAD IRAGIAKICA DFPGSYWRAL DADRAYPEAF VAALTKAGYL
GCLIPEAYGG SGLDLTAAAV ILEEIHKQGA NAAACHAQIY TMGTVLRHGS DAQKRAYLPR
IADGSLRLQA FGVTEPTSGT DTLALQTTAR REGDRYIING QKIWTSRAEH SDLMLLLART
TPRDAVTKRT DGLSVFLLDL NSLLDKGVTI RPIRTMINHA TTEVFFDNVS IPADALIGDE
GKGFRYILSG MNAERILIAA ECIGDAKWFI DKASAYASER SVFGQPIGKN QGVQFPLAKA
YAHMIAAEAI VYRAAACYDA GEDPGADANM AKLLAADASW EAAEACMQTH GGFAFAEEYD
IERKFRETRL YQIAPISTNL ILSYIAERVL GLPKSY
//
