ID D6AE58_STRFL Unreviewed; 523 AA.
AC D6AE58;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:EFE78833.2};
GN ORFNames=SSGG_06200 {ECO:0000313|EMBL:EFE78833.2};
OS Streptomyces filamentosus NRRL 15998.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=457431 {ECO:0000313|EMBL:EFE78833.2, ECO:0000313|Proteomes:UP000003986};
RN [1] {ECO:0000313|Proteomes:UP000003986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 15998 {ECO:0000313|Proteomes:UP000003986};
RA Molnar K.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000003986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 15998 {ECO:0000313|Proteomes:UP000003986};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M.,
RA Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces roseosporus strain NRRL 15998.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; DS999644; EFE78833.2; -; Genomic_DNA.
DR AlphaFoldDB; D6AE58; -.
DR Proteomes; UP000003986; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF152; OXIDASE (CODA), PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04090)-RELATED; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2}.
FT DOMAIN 245..259
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 523 AA; 57169 MW; 5F8C29E932DF3BE5 CRC64;
MTDYVIVGGG TAGSVIASRL TEDPDVTVTV IEGGPTDIDR DDVLTLRRWL GLLGGDLDYD
YPTTEQPRGN SHIRHSRARV LGGCSSHNTL ISFKPLPGDW DEWAEAGAEG WDAAAMDPYF
AKLRNNIVPV DEKDRNAIAR DFVDAAQEAA GVPRVDSFNS KPFHEGVGFF DLAYHPENNK
RSSASVAYLH PHIEAGDRPN LRILLETWAY RLEFDGTRAT GVHVRTKDGE EILLRAAREV
IVCAGAVDTP RLLLHSGIGP REDLSALGID VRHDLPGVGE NLLDHPESVI VWETDGPIPE
NSAMDSDAGL FVRRDPGSRG PDLMFHFYQI PFTDNPERLG YQKPEHGVSM TPNIPKPRSR
GRLYLTSADP EVKPALDFRY FTDEDDYDGR TLVDGIKLAR EIARTEPLAH WLKREVCPGP
EVTSDEDISE YARKVAHTVY HPAGTCKMGA IDDEAAVVDP QLRIRGLEGI RIADASVFPT
MPAVNPMIGV LMVGEKCAEL LADQARGTAP AAGTSTSTGG DAR
//