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Database: UniProt
Entry: D7C7Q2_STRBB
LinkDB: D7C7Q2_STRBB
Original site: D7C7Q2_STRBB 
ID   D7C7Q2_STRBB            Unreviewed;       412 AA.
AC   D7C7Q2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Type 2 domain-containing Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ADI12600.1};
GN   OrderedLocusNames=SBI_09482 {ECO:0000313|EMBL:ADI12600.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI12600.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI12600.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI12600.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP002047; ADI12600.1; -; Genomic_DNA.
DR   RefSeq; WP_014182047.1; NC_016582.1.
DR   AlphaFoldDB; D7C7Q2; -.
DR   STRING; 749414.SBI_09482; -.
DR   KEGG; sbh:SBI_09482; -.
DR   PATRIC; fig|749414.3.peg.9763; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_10_0_11; -.
DR   Proteomes; UP000000377; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
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; PF00441; Acyl-CoA_dh_1; 1.
DR   PIRSF; PIRSF016578; HsaA; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000377}.
FT   DOMAIN          246..384
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   412 AA;  43151 MW;  2AB5EA1A533BFFE5 CRC64;
     MTTVGEAIDA EAGHAHWLRV AQEIADDLAT DAVDREQAGK APFDEVARLR EAGLLTLPTL
     AGPGAGDAGG TGGADWRTAY AVVRTISAAD GAIGYLLGCH YFLSSSARFF ASPALATRVE
     QESAARQWCW GGGLVSCEPS PGLTPTARGY VLNGRQSCVT GVGIADRLVV RATRSGSGDP
     LAVLVDPAHP GVVYVDDEDT FGQRLAAGGS VEFDSVPVTA DDVFGSLSSD EGALPPFAGL
     AAPTARLVSV QFCLGVAEGL LAEVREYSRV VNSSWQPSAQ HSWPGSPSRD PYVLGVYGEL
     TVAARSASAL ADQAVEALGR GFARGEDLDD DECAEIAVLA SVAESAASRA AQEITTRALD
     VIGARAAFLR HGFDRFWRNA RTHTLREPVA DRLREVGDYF LNGAHPPFTI PS
//
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