ID Q93RY1_STRCO Unreviewed; 511 AA.
AC Q93RY1;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE SubName: Full=Secreted oxidase {ECO:0000313|EMBL:CAC37893.1};
GN OrderedLocusNames=SCO6291 {ECO:0000313|EMBL:CAC37893.1};
GN ORFNames=SCBAC8D1.04 {ECO:0000313|EMBL:CAC37893.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAC37893.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAC37893.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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DR EMBL; AL939127; CAC37893.1; -; Genomic_DNA.
DR RefSeq; NP_630389.1; NC_003888.3.
DR RefSeq; WP_011030798.1; NZ_VNID01000022.1.
DR AlphaFoldDB; Q93RY1; -.
DR STRING; 100226.gene:17763950; -.
DR PaxDb; 100226-SCO6291; -.
DR PATRIC; fig|100226.15.peg.6406; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_030705_1_2_11; -.
DR InParanoid; Q93RY1; -.
DR OrthoDB; 9801699at2; -.
DR PhylomeDB; Q93RY1; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR017224; Opine_Oxase_asu/HCN_bsu.
DR PANTHER; PTHR42949; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR PANTHER; PTHR42949:SF2; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF037495; Opine_OX_OoxA/HcnB; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001973}.
FT DOMAIN 6..334
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 394..441
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT REGION 468..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 52680 MW; BB449F1BD8E10ECE CRC64;
MTEPADLVVV GAGPAGMAAA ATALAGGLRV ALLDSGTALG GQYWRHPPEH ARAAVPTDDL
HHGLDRYRAL CRALAAHRTA GRLDLRLEHH AWSAVREGDG FAVHAADRRE APRETAVVLR
APRLLVATGA YDRQLPFPGW DLPGVLTAGG MQALLKGGSV AAGSRVALGG TGPFLLPVAA
GLAARGVEVV AVCEAAHPRA WLRHPGPLLS NPDKWAEGAG YAATLVRHRV PVRPRTAIVA
AEGGERVTSV RIASLAPDGS PRPGTERRVE VDAVGVGWGF APQLDLLVPL GASLTDSADG
NAVVAVDRGQ RTTVPGLYAA GETCGVGGAA LAVNEGRLAA ASVLADARAT TVPANGRLAA
LRSAVDRQRA FARAMALAHP VPPAWSSWLT DETVVCRCEE VTAGAIRTAR ADGAPDHRQI
KQLTRAGMGW CQGRMCGPAV HCLTARHRAY EPAERLVATP VTLGALADLD EDPPVSTASP
VSAASPVSAA SPVSATSTEP TDSSETDKEC P
//
