ID A0A0J7ZCY8_STRVR Unreviewed; 523 AA.
AC A0A0J7ZCY8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KMS73083.1};
GN ORFNames=ACM01_20170 {ECO:0000313|EMBL:KMS73083.1};
OS Streptomyces viridochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938 {ECO:0000313|EMBL:KMS73083.1, ECO:0000313|Proteomes:UP000037432};
RN [1] {ECO:0000313|EMBL:KMS73083.1, ECO:0000313|Proteomes:UP000037432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3414 {ECO:0000313|EMBL:KMS73083.1,
RC ECO:0000313|Proteomes:UP000037432};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUN-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:KMS73083.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFNT01000022; KMS73083.1; -; Genomic_DNA.
DR RefSeq; WP_048582687.1; NZ_LFNT01000022.1.
DR AlphaFoldDB; A0A0J7ZCY8; -.
DR PATRIC; fig|1938.3.peg.2922; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000037432; 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 254..268
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 523 AA; 56713 MW; 3C8579CDF00772B2 CRC64;
MATTPAPGTE SAYDYVIVGG GTAGCVLAAR LSEDPDCRVC VIEGGPSDVG DERVLRLRNW
INLLGSEFDY GYTTVEQPRG NSHILHSRAR VLGGCSSHNT LISFLPLPQD LDDWVSRGCS
GWDPATILPY RDRLLTQIVP VAEADRNPIA RDFVTAAARA LGVPVVDDFN AEPFADGTGF
FSLAYQPEGN LRSSASVAYL HPVLDRSNLT LLLETWAHRL LTDEAGRLTR VAVRDADGRP
ATVRAERELL LCAGAIDTPR LLMLSGIGPA DELRGLGIEV RADLPGVGEN LLDHPESVIV
WETAGPLPPN SAMDSDAGLF LRRDTGQPRP DLMFHFYQVP FTVNTERLGY PVPRHGVCMT
PNVPRARSTG RMWLRSADPA EHPALDFRYF TDPEGHDERT IVDGLRVARE VAATDPLRGW
LLREVAPGPA VVSDADLSEY GRRAAHTVYH PAGTCRMGAL DDPMAVCDPG LRLRGFEGVR
IVDASVFPTM PTINPMVTVL LAAERAADLI SGRPAAAERR AGQ
//
