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Database: UniProt
Entry: A0A0S8DSP5_9GAMM
LinkDB: A0A0S8DSP5_9GAMM
Original site: A0A0S8DSP5_9GAMM 
ID   A0A0S8DSP5_9GAMM        Unreviewed;       514 AA.
AC   A0A0S8DSP5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=GMC family oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMJ69_07205 {ECO:0000313|EMBL:KPK38882.1};
OS   Gammaproteobacteria bacterium SG8_47.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1703406 {ECO:0000313|EMBL:KPK38882.1, ECO:0000313|Proteomes:UP000054199};
RN   [1] {ECO:0000313|EMBL:KPK38882.1, ECO:0000313|Proteomes:UP000054199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_47 {ECO:0000313|EMBL:KPK38882.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KPK38882.1}.
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DR   EMBL; LJTV01000061; KPK38882.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8DSP5; -.
DR   STRING; 1703406.AMJ69_07205; -.
DR   PATRIC; fig|1703406.3.peg.1742; -.
DR   Proteomes; UP000054199; Unassembled WGS sequence.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          17..277
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          378..504
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   514 AA;  56513 MW;  B9F51C8034D4A33D CRC64;
     MFVDARTLDD NSTLTADLAI VGAGPAGITV ARAFAGRNLR VALIESGALE ATAETQALYE
     GESVGIDYPL AATRLRYFGG SSNHWGGFCR PLDVIDFEAR DWVPHSGWPF GRDELMLYYA
     TADGLVEVAP ANYEDSTYWQ RKTGKALLQL ATGRMVLGFV HYGPPTHFGT RYQDELVGAG
     NIQILLNANV VNIAAGPNAR TVTHLDVRTL TGKKHRVRAQ QFVLATGGLE NPRLLLLSND
     VMPMGLGNQH DLVGRFFMEH PHLPGFGEIV MVDEKRLPQI FRENIPADGH YVNAAFKPTA
     EFMRRERLLN ATLQVGVAGH YRRQDSVPHP DADKAAAHAD MLRAARPFLV EAGAPAGETA
     EQRLGVWLGL GCACEQVPNP DSRVTLADTR DALGLRRIRL DWRLTEQDRR SVVRHMRSLA
     LEFGALGIGR MLVDIEDDGQ WPEQVIGGSH HMGTTRMHDD PKQGVVDRNC KVHDIDNLYV
     AGSSVFPTCG TANPTLTLVA LAVRLAEHLQ EKFR
//
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