ID A0A067EYC2_CITSI Unreviewed; 570 AA.
AC A0A067EYC2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=CISIN_1g008331mg {ECO:0000313|EMBL:KDO60139.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO60139.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO60139.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; KK784934; KDO60139.1; -; Genomic_DNA.
DR RefSeq; XP_006490298.1; XM_006490235.2.
DR AlphaFoldDB; A0A067EYC2; -.
DR STRING; 2711.A0A067EYC2; -.
DR PaxDb; 2711-XP_006490298-1; -.
DR GeneID; 102611629; -.
DR KEGG; cit:102611629; -.
DR eggNOG; KOG1238; Eukaryota.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000027120; 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 Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..570
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001639809"
FT DOMAIN 274..288
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 51..52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 116
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 229
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 506..507
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 535
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 546..547
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 442..498
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 570 AA; 62857 MW; F3C7BD21872396BF CRC64;
MGLQFWRFAV IIFLFHGFCF AEKAPYYTFV KDATSAPLIS YYDYIIVGGG TSGCPLAATL
SQNATVLLLE KGGSPYENPN ITDTGNFATT LLDPSPTSPS QQFISEDGVY NARARVLGGG
SVINAGFYTR ASLRYVREVG WTESLVNSSY EWVEKKVAHE PPMLQWQSAV RDGLLEAGVL
PYNGFTFDHI YGTKVSGTIF DEDGHRHSAA DLLEYADPEK LTVYLRAVVQ RIKFTETGRA
KPTAHCVTFY DHVGARHRAC LNNGGKNEII LSAGAIGSPQ LLMLSGVGPA NELRKRGIRV
VVDQPNVGQG MSDNPMNALF VPSARPVEVS LVQVVGITRF DSYIETASGL SLAPSWAQGL
TRDYSSFLNK TDIPSLVTPE TVAEAVETVN SYLNGTIRAG VIVEKIMGPR STGHLRLRTL
DADDNPSVTF NYFQEPEDLV RCVQGMRTII DVLNSRALSK FRYPDVSVQE LIDLMVNIPT
NLRPRHVVGA SISLEQFCRD TVMTIWHYHG GCQVDRVVDR DYKVLGVDGL RVIDGSTFYN
SPGTNPQATC MMLGRYMGLR ILQDRDRISF
//
