ID   VALG_STRHJ              Reviewed;         422 AA.
AC   H2K893; Q1L2K4;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Validoxylamine A glucosyltransferase {ECO:0000303|PubMed:16632251};
DE            EC=2.4.1.338 {ECO:0000269|PubMed:16632251, ECO:0000269|PubMed:18563934};
GN   Name=valG {ECO:0000303|PubMed:16632251};
GN   OrderedLocusNames=SHJG_0282 {ECO:0000312|EMBL:AEY85560.1};
OS   Streptomyces hygroscopicus subsp. jinggangensis (strain 5008).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=1133850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP   PHENOTYPE, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=5008 {ECO:0000312|EMBL:ABA41511.1};
RX   PubMed=16632251; DOI=10.1016/j.chembiol.2006.02.002;
RA   Bai L., Li L., Xu H., Minagawa K., Yu Y., Zhang Y., Zhou X., Floss H.G.,
RA   Mahmud T., Deng Z.;
RT   "Functional analysis of the validamycin biosynthetic gene cluster and
RT   engineered production of validoxylamine A.";
RL   Chem. Biol. 13:387-397(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5008 {ECO:0000312|Proteomes:UP000007170};
RA   Wu H., Bai L.;
RT   "Genomic analysis of Streptomyces hygroscopicus subsp. jinggangensis
RT   5008.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF 100-THR--GLY-101,
RP   DOMAIN, AND SUBSTRATE SPECIFICITY.
RX   PubMed=18563934; DOI=10.1021/np800185k;
RA   Xu H., Minagawa K., Bai L., Deng Z., Mahmud T.;
RT   "Catalytic analysis of the validamycin glycosyltransferase (ValG) and
RT   enzymatic production of 4''-epi-validamycin A.";
RL   J. Nat. Prod. 71:1233-1236(2008).
CC   -!- FUNCTION: Involved in the biosynthesis of the antifungal agent
CC       validamycin A (PubMed:16632251). Catalyzes the final attachment of
CC       glucose from UDP-alpha-D-glucose to validoxylamine A to yield
CC       validamycin A (PubMed:16632251, PubMed:18563934). UDP-glucose is the
CC       most efficient glycosyl donor, whereas GDP-glucose and ADP-glucose are
CC       much less efficient (PubMed:16632251). ValG also utilizes UDP-galactose
CC       as substrate to produce the new validamycin analog, 4''-epi-validamycin
CC       A (PubMed:18563934). {ECO:0000269|PubMed:16632251,
CC       ECO:0000269|PubMed:18563934}.
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:0000269|PubMed:16632251, ECO:0000269|PubMed:18563934};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:18563934};
CC       Note=Also able to use Mg(2+), Co(2+) and Ca(2+).
CC       {ECO:0000269|PubMed:18563934};
CC   -!- DOMAIN: Instead of having the common DXD motif at the position 99-101,
CC       it contains a DTG sequence, which may provide greater metal ion binding
CC       flexibility. {ECO:0000305|PubMed:18563934}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC       validamycin A, and show an accumulation of validoxylamine.
CC       {ECO:0000269|PubMed:16632251}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; DQ164098; ABA41511.1; -; Genomic_DNA.
DR   EMBL; CP003275; AEY85560.1; -; Genomic_DNA.
DR   RefSeq; WP_014668908.1; NC_017765.1.
DR   AlphaFoldDB; H2K893; -.
DR   SMR; H2K893; -.
DR   STRING; 1133850.SHJG_0282; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; AEY85560; AEY85560; SHJG_0282.
DR   KEGG; shy:SHJG_0282; -.
DR   PATRIC; fig|1133850.20.peg.424; -.
DR   eggNOG; COG1216; Bacteria.
DR   HOGENOM; CLU_025996_24_2_11; -.
DR   OMA; FEANERY; -.
DR   OrthoDB; 1445278at2; -.
DR   Proteomes; UP000007170; Chromosome.
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   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Manganese; Metal-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..422
FT                   /note="Validoxylamine A glucosyltransferase"
FT                   /id="PRO_0000442849"
FT   MUTAGEN         100..101
FT                   /note="TG->CD: Alters preferences for metal ion binding
FT                   (only use Mn(2+) and to some extent Co(2+)), but it does
FT                   not affect substrate specificity."
FT                   /evidence="ECO:0000269|PubMed:18563934"
SQ   SEQUENCE   422 AA;  47143 MW;  2637650FF4CCAAD1 CRC64;
     MPGATSHVPL LSVVIPTYNR AALLDRTLGT LARQTTALED FEVVVSDDGS TDTTRDVVRS
     YEDRLRIKYV FQEDLGYRVA SARNGGARLA SAPLLAFLDT GVLAGPQYVQ SVLAAHAGPA
     PAKVVLGCCY GYDPRNPHPE LHSLVEEFPP EEAVRRVGDA PWFQDMRLPE FTAVDFDLSR
     MHMPWLWFWT LNVSLPAADF WRVGGFDEDF TGWGGEDIEL GYRLHAHGIP MTVSRESWGI
     EAPHERTHEA NVSSLMLNCD RFVRKHPSLL PELFWAVTNR GIFGSVETER LRFEEWASQA
     RGQQVLDEIA IGLDTLPPSQ HTQRVAVFGS GTEGLPITPR QNVELFLCDY DEGVLARQES
     RDDAAVSTWH LSGLRTPWPD QHFDLVIITS RMDGPRQAWG EAFTKEAHRI ASSVVEPSLR
     GD