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Database: UniProt
Entry: I1PP16_ORYGL
LinkDB: I1PP16_ORYGL
Original site: I1PP16_ORYGL 
ID   I1PP16_ORYGL            Unreviewed;       591 AA.
AC   I1PP16;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
OS   Oryza glaberrima (African rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA04G0193500.1, ECO:0000313|Proteomes:UP000007306};
RN   [1] {ECO:0000313|Proteomes:UP000007306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA   Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA   Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA   Zuccolo A.;
RT   "The complete genome of Oryza glaberrima.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORGLA04G0193500.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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   AlphaFoldDB; I1PP16; -.
DR   SMR; I1PP16; -.
DR   STRING; 4538.I1PP16; -.
DR   EnsemblPlants; ORGLA04G0193500.1; ORGLA04G0193500.1; ORGLA04G0193500.
DR   Gramene; ORGLA04G0193500.1; ORGLA04G0193500.1; ORGLA04G0193500.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_026750_0_0_1; -.
DR   OMA; NHFESCA; -.
DR   Proteomes; UP000007306; 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; PTHR45968:SF3; OS04G0573100 PROTEIN; 1.
DR   PANTHER; PTHR45968; OSJNBA0019K04.7 PROTEIN; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
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   Disulfide bond {ECO:0000256|PIRSR:PIRSR000137-3};
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..591
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003648913"
FT   DOMAIN          281..295
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         123
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         236
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         521..522
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         550
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         561..562
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   DISULFID        458..513
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ   SEQUENCE   591 AA;  63981 MW;  4DF306D9CAB3AA2E CRC64;
     MASDMDTTRA LAILAATSFV AMLACVQAAG DESYTFMKDA VQSPQVSYYD YIIVGGGTAG
     CPLAATLSQR FRVLLLERGG SPYDDERIGN MTRFADTLSD TSPSSPAQRF VSEDGVINSR
     PRVLGGGSCI NAGFYTRASD EYVRGLGWDL EATTAAYRWV EDVVAFQPEL GPWQSALERG
     LLEAGIAPQN GFTFDHLGGT KVGGSIFDAE GRRHTAADLL RYARTDGIDV LLRARVAKIL
     FNVRAGRRPV AHGVVFHDSE GQMHRAYLSN GRGNEIILSA GAMGSPQLLM LSGVGPADHL
     RSFGITLVLN QPAVGQGMSD NPMNAIYVPS PSPVEVSLIQ VVGITEVGSY IEGASGANWG
     VRRSGSGGDR PHRNFGMFSP QTGQLATVPP KQRTPEAIAR AAEAMSQLDD TAFRGGFILE
     KILGPLSTGH LELRNRNPDD NPSVTFNYFA HPEDLRRCVA GVSVIERVIR SEAFANFTYP
     YFSVETLLNM TAGFPVNLRP RHDNDSTSLE QFCKDTVMTI WHYHGGCQVN RVVDAEYRVI
     GVDALRVIDG STFNASPGTN PQATVMMLGR YMGVKIQNER LGNEGLGRRN L
//
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