ID A0A061FZT6_THECC Unreviewed; 582 AA.
AC A0A061FZT6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Glucose-methanol-choline (GMC) oxidoreductase family protein, putative {ECO:0000313|EMBL:EOY23060.1};
GN ORFNames=TCM_015068 {ECO:0000313|EMBL:EOY23060.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY23060.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY23060.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001881; EOY23060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FZT6; -.
DR STRING; 3641.A0A061FZT6; -.
DR EnsemblPlants; EOY23060; EOY23060; TCM_015068.
DR Gramene; EOY23060; EOY23060; TCM_015068.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_026750_0_0_1; -.
DR InParanoid; A0A061FZT6; -.
DR OMA; YPWPMPR; -.
DR Proteomes; UP000026915; Chromosome 3.
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:SF31; GLUCOSE-METHANOL-CHOLINE (GMC) OXIDOREDUCTASE FAMILY 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; 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 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:UP000026915};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 297..311
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 93..94
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 139
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 252
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 517..518
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 546
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 557..558
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 454..509
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 582 AA; 64224 MW; 0C84BA082B23B4A6 CRC64;
MDFSCFIREL FGSKVRKCYM HLESRKYPTV FLVAVFALHH FCHAEKAPYY SFVQESTSAP
PVSFHDYIIV GGGTAGCPLA ATLSESANVL VLERGGSPYV NPSKTDEANL FPTLFDPSPN
SYAQAFVSED GVYNHRARVL GGGSVINAGF YSHAETDFVK EAGLDEALVN DSYQWVEKEV
VFEPPVLQWQ SAVRDGLLEA GVLPYNGFTY DHIYGTKIGA TIFDMDGHRH SAADLLEYAD
PKKIKVYLHA KVPKIILTTE IGSRARAKGV IFEDALGVRH EAFLTEDSNI EIILAAGAIG
SPQLLMLSGV GPAHHLKALG MKVLIDQPMV GQGMADNPLN GLYIPSPLPV ELSLASVVGI
TRFGNYIEAI SGLNLAPSWI QWTSKISPTI LNQIESKTKI GSFLVNTRIK GGIIIDKVKG
PISTGHLELR SKNPNDTPKV WFNYFQVPED LRKCVQGIQT ILKVVDSKAF SKFRYKTIST
QDLLNLVAAL PLNLRPRHLN AAISLEQYCI DTVMTMWHYH GGCHVGKVVD QDYRVLGVDG
LRVVDGSTFN FSPGTNPQST VMMLGRYMGV RIQQDRHSYK RK
//
