ID   VLDK_STRHL              Reviewed;         453 AA.
AC   Q15JF5;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Validoxylamine A glucosyltransferase {ECO:0000303|PubMed:16725283};
DE            EC=2.4.1.338 {ECO:0000250|UniProtKB:H2K893};
GN   Name=vldK {ECO:0000303|PubMed:16725283};
OS   Streptomyces hygroscopicus subsp. limoneus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=264445;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 21432 / NBRC 12704 / KCTC 1717 / KCCM 11405
RC   {ECO:0000312|EMBL:ABC67275.1};
RX   PubMed=16725283; DOI=10.1016/j.gene.2005.12.035;
RA   Singh D., Seo M.J., Kwon H.J., Rajkarnikar A., Kim K.R., Kim S.O.,
RA   Suh J.W.;
RT   "Genetic localization and heterologous expression of validamycin
RT   biosynthetic gene cluster isolated from Streptomyces hygroscopicus var.
RT   limoneus KCCM 11405 (IFO 12704).";
RL   Gene 376:13-23(2006).
CC   -!- FUNCTION: Involved in the biosynthesis of the antifungal agent
CC       validamycin A (PubMed:16725283). Catalyzes the final attachment of
CC       glucose from UDP-alpha-D-glucose to validoxylamine A to yield
CC       validamycin A (By similarity). {ECO:0000250|UniProtKB:H2K893,
CC       ECO:0000269|PubMed:16725283}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-alpha-D-glucose + validoxylamine A = H(+) + UDP +
CC         validamycin A; Xref=Rhea:RHEA:49388, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:90869,
CC         ChEBI:CHEBI:111505; EC=2.4.1.338;
CC         Evidence={ECO:0000250|UniProtKB:H2K893};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:H2K893};
CC   -!- DOMAIN: Instead of having the common DXD motif at the position 130-132,
CC       it contains a DTG sequence, which may provide greater metal ion binding
CC       flexibility. {ECO:0000250|UniProtKB:H2K893}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; DQ223652; ABC67275.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q15JF5; -.
DR   SMR; Q15JF5; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR027791; Galactosyl_T_C.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF02709; Glyco_transf_7C; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Manganese; Metal-binding; Transferase.
FT   CHAIN           1..453
FT                   /note="Validoxylamine A glucosyltransferase"
FT                   /id="PRO_0000442848"
SQ   SEQUENCE   453 AA;  50436 MW;  C32F42748E0E40AB CRC64;
     MEGVDIPGRP SPWRVCVTRP QVHPINAKVA PMPGATSHVP LLSVVIPTYN RDALLDRTLG
     TLARQTTAPE DFEVVVSDDG STDTTRDVVR SYEDRLRIKY VFQEDLGYRV ASARNGGARL
     ASAPLLAFLD TGVLAGPQYV QSVLAAHAGP APAKVVLGCC YGYDPRNPHP ELHSLVEEFP
     PEEAVRRVGD APWFQDMRLP EFTAVDFDLS RMHMPWLWFW TLNVSLPAAD FWRVGGFDED
     FTGWGGEDIE LGYRLHAHGI PMTVSRESWG IEAPHERTHE ANVSSLMLNC DRFVRKHPSL
     LPELFWAVTN RGIFGSVETE RLRFEEWASQ ARGQQVLDEI AIGLDTLPPS QHTQRVAVFG
     SGTEGLPTAP RQNVELFLCD YDEGVLARQE SRDDGAVSTW HLSGLRTPWP DQHFDLVIIT
     SRMDGPRQAW GEAFTKEAHR IASSVVEPSL SGD