ID   VLDB_STRHL              Reviewed;         373 AA.
AC   Q15JG4;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Valienol-1-phosphate guanylyltransferase {ECO:0000303|PubMed:21766819};
DE            EC=2.7.7.91 {ECO:0000269|PubMed:21766819};
DE   AltName: Full=Cyclitol nucleotidyltransferase {ECO:0000303|PubMed:21766819};
GN   Name=vldB {ECO:0000303|PubMed:16725283};
GN   ORFNames=SHL15_8009 {ECO:0000312|EMBL:ALO98986.1};
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:ABC67266.1};
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21432 / NBRC 12704 / KCTC 1717 / KCCM 11405
RC   {ECO:0000312|EMBL:ALO98986.1, ECO:0000312|Proteomes:UP000057753};
RA   Kim K.M.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PRELIMINARY FUNCTION.
RC   STRAIN=ATCC 21432 / NBRC 12704 / KCTC 1717 / KCCM 11405;
RA   Seo M.J., Im E.M., Singh D., Rajkarnikar A., Kwon H.J., Hyun C.G.,
RA   Suh J.W., Pyun Y.R., Kim S.O.;
RT   "Characterization of D-glucose alpha-1-phosphate uridylyltransferase (VldB)
RT   and glucokinase (VldC) involved in validamycin biosynthesis of Streptomyces
RT   hygroscopicus var. limoneus KCCM 11405.";
RL   J. Microbiol. Biotechnol. 16:1311-1315(2006).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 21432 / NBRC 12704 / KCTC 1717 / KCCM 11405;
RX   PubMed=21766819; DOI=10.1021/ja203574u;
RA   Asamizu S., Yang J., Almabruk K.H., Mahmud T.;
RT   "Pseudoglycosyltransferase catalyzes nonglycosidic C-N coupling in
RT   validamycin a biosynthesis.";
RL   J. Am. Chem. Soc. 133:12124-12135(2011).
CC   -!- FUNCTION: Involved in the biosynthesis of the antifungal agent
CC       validamycin A (PubMed:16725283). Catalyzes the conversion of valienol
CC       1-phosphate to GDP-valienol and less effectively to ADP-valienol or
CC       other NDP derivatives (PubMed:21766819). {ECO:0000269|PubMed:16725283,
CC       ECO:0000269|PubMed:21766819}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H(+) + valienol 1-phosphate = diphosphate + GDP-
CC         valienol; Xref=Rhea:RHEA:26055, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:91252, ChEBI:CHEBI:91253; EC=2.7.7.91;
CC         Evidence={ECO:0000269|PubMed:21766819};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000305|PubMed:21766819};
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be a glucose 1-phosphate
CC       uridylyltransferase. {ECO:0000305|Ref.3}.
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DR   EMBL; DQ223652; ABC67266.1; -; Genomic_DNA.
DR   EMBL; CP013220; ALO98986.1; -; Genomic_DNA.
DR   RefSeq; WP_058084465.1; NZ_CP013220.1.
DR   AlphaFoldDB; Q15JG4; -.
DR   SMR; Q15JG4; -.
DR   EnsemblBacteria; ALO98986; ALO98986; SHL15_8009.
DR   PATRIC; fig|264445.3.peg.8522; -.
DR   BioCyc; MetaCyc:MON-19688; -.
DR   Proteomes; UP000057753; Chromosome II.
DR   GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR011831; ADP-Glc_PPase.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43523; PTHR43523; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; GTP-binding; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..373
FT                   /note="Valienol-1-phosphate guanylyltransferase"
FT                   /id="PRO_0000442844"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6V1"
FT   BINDING         192..193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6V1"
SQ   SEQUENCE   373 AA;  41512 MW;  51F5F9825864A98F CRC64;
     MDGVRAVLLA GGEGRRMGPL GRGRLKPLVP FGGTSRLIDF SIANVHRSGL RDVLLLSQYE
     ERRLMDDLHL VWNGRHRGFR IDFGPYDAVY RRSPGKLPEQ LPERIWPLER GTADALLTKA
     EYVFRQGDAE ASEILVLHAD HVYRFDYGDM IREHRASKAA LTVSYQRIER RYVHLFGMVE
     FDGDGLLTAF EEKPDDPTSD LVFAAFCLFD AATLRRYLEQ LRGTDWQHDI SRDVIPAMLA
     GGELIRGYEV KSYWEDIGTV DRYHRAHRGL LRADPTLALS DMPLTVAPEV PRHLVPGGPG
     RRASVVAADV ANEGEIVSSV VYPGARIGVD AHVVDCVVLP GARVPDGTHL ASAIVLEDGS
     VQQCEAEREE VAL