ID   CGT_MANIN               Reviewed;         470 AA.
AC   A0A0M4KE44;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=UDP-glycosyltransferase 13 {ECO:0000303|PubMed:26331569};
DE            Short=MiUGT13 {ECO:0000303|PubMed:26331569};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=C-glycosyltransferase {ECO:0000303|PubMed:26331569};
DE            Short=MiCGT {ECO:0000303|PubMed:26331569};
GN   Name=CGT {ECO:0000303|PubMed:26331569};
GN   Synonyms=UGT13 {ECO:0000303|PubMed:26331569};
OS   Mangifera indica (Mango).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Anacardiaceae; Mangifera.
OX   NCBI_TaxID=29780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBSTRATE SPECIFICITY.
RX   PubMed=26331569; DOI=10.1002/anie.201506505;
RA   Chen D., Chen R., Wang R., Li J., Xie K., Bian C., Sun L., Zhang X.,
RA   Liu J., Yang L., Ye F., Yu X., Dai J.;
RT   "Probing the Catalytic Promiscuity of a Regio- and Stereospecific C-
RT   Glycosyltransferase from Mangifera indica.";
RL   Angew. Chem. Int. Ed. 54:12678-12682(2015).
CC   -!- FUNCTION: Benzophenone C-glycosyltransferase involved in the
CC       biosynthesis of mangiferin. Exhibits a robust regio- and stereospecific
CC       C-glycosylation activity toward over 35 substrates from 18 structurally
CC       different types with UDP-glucose. Also able to produce O- and N-
CC       glycosides and to use UDP-xylose as sugar donor. Generates only C-
CC       glycosides with 2,4,6-tri-hydroxy acceptors at the A ring, both C- and
CC       O- glycosides with 2,4-di-hydroxyl acceptors at the A ring, and only O-
CC       glycosides with 2- or 4-mono-hydroxy acceptors at the A ring.
CC       {ECO:0000269|PubMed:26331569}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=47.0 uM for maclurin {ECO:0000269|PubMed:26331569};
CC         KM=159.2 uM for norathyriol {ECO:0000269|PubMed:26331569};
CC         Note=kcat is 1.6 sec(-1) with maclurin as substrate. kcat is 0.8
CC         sec(-1) with norathyriol as substrate. {ECO:0000269|PubMed:26331569};
CC       pH dependence:
CC         Optimum pH is 9.0. {ECO:0000269|PubMed:26331569};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:26331569};
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; KT200208; ALD83754.1; -; mRNA.
DR   AlphaFoldDB; A0A0M4KE44; -.
DR   SMR; A0A0M4KE44; -.
DR   SABIO-RK; A0A0M4KE44; -.
DR   GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0042285; F:xylosyltransferase activity; IDA:UniProtKB.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   Pfam; PF00201; UDPGT; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..470
FT                   /note="UDP-glycosyltransferase 13"
FT                   /id="PRO_0000436352"
SQ   SEQUENCE   470 AA;  52123 MW;  B2B5D9ACDA4B35F0 CRC64;
     MSASDALNSC PHVALLLSSG MGHLTPCLRF AATLVQHHCR VTIITNYPTV SVAESRAISL
     LLSDFPQITE KQFHLLPFDP STANTTDPFF LRWEAIRRSA HLLNPLLSSI SPPLSALVID
     SSLVSSFVPV AANLDLPSYV LFTSSTRMCS LEETFPAFVA SKTNFDSIQL DDVIEIPGFS
     PVPVSSVPPV FLNLNHLFTT MLIQNGQSFR KANGILINTF EALEGGILPG INDKRAADGL
     PPYCSVGPLL PCKFEKTECS APVKWLDDQP EGSVVYVSFG SRFALSSEQI KELGDGLIRS
     GCRFLWVVKC KKVDQEDEES LDELLGRDVL EKIKKYGFVI KNWVNQQEIL DHRAVGGFVT
     HGGWNSSMEA VWHGVPMLVW PQFGDQKINA EVIERSGLGM WVKRWGWGTQ QLVKGEEIGE
     RIKDLMGNNP LRVRAKTLRE EARKAIEVGG SSEKTLKELI ENWKKTSRKT