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Database: UniProt
Entry: A0A101TV12_9ACTN
LinkDB: A0A101TV12_9ACTN
Original site: A0A101TV12_9ACTN 
ID   A0A101TV12_9ACTN        Unreviewed;       509 AA.
AC   A0A101TV12;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KUN98993.1};
GN   ORFNames=AQJ67_26875 {ECO:0000313|EMBL:KUN98993.1};
OS   Streptomyces caeruleatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=661399 {ECO:0000313|EMBL:KUN98993.1, ECO:0000313|Proteomes:UP000053429};
RN   [1] {ECO:0000313|EMBL:KUN98993.1, ECO:0000313|Proteomes:UP000053429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-24802 {ECO:0000313|EMBL:KUN98993.1,
RC   ECO:0000313|Proteomes:UP000053429};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces caeruleatus NRRL B-24802, type
RT   strain for the species Streptomyces caeruleatus.";
RL   Submitted (OCT-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUN98993.1}.
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DR   EMBL; LMWY01000035; KUN98993.1; -; Genomic_DNA.
DR   RefSeq; WP_062721868.1; NZ_KQ948932.1.
DR   AlphaFoldDB; A0A101TV12; -.
DR   STRING; 661399.AQJ67_26875; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000053429; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053429}.
FT   DOMAIN          249..263
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         86
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   509 AA;  55893 MW;  C01494EB52096551 CRC64;
     MSQNTPVYDY VVIGGGTAGS VIASRLTENP DTTVAVIEGG PSDVGRDDVL TLRRWMGLLG
     GDLDYDYPTT EQPRGNSHIR HSRARVLGGC SSHNTLIAFK PLPSDWDEWE EAGATGWGAV
     PMEAYYARLK NNIVPVDEKD RNAIARDFVD SAQGALGVPR VEGFNKQPFT EGVGFFDLAY
     HPENNKRSSA SVAYLHPVMD ERENLTILLE TWAYKLELNG TRAEGVHVRT KDGEEVLIRA
     RREVVLCAGA VDSPRLLMHS GIGPKEDLTQ LGIPVVHDLP GVGENLLDHP ESVIVWETNG
     PIPDNSAMDS DAGLFVRRDP EHQGPDLMFH FYQIPFTDNP ERLGYRRPEF GVSMTPNIPK
     PKSRGRLYLT SADPAVKPAL DFRYFTDEDD YDGRTLVDGI RIAREIAKTE PLASWLKREV
     CPGPDVDGDE ELGEYARKVA HTVYHPAGTC RMGAADDELA VVDPQLRIRG LDGIRIADAS
     VFPTMTAVNP MIGVLMVGEK AVDLLGGEA
//
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