VALB_STRHJ
ID VALB_STRHJ Reviewed; 373 AA.
AC H2K888; Q3T6E3;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Valienol-1-phosphate guanylyltransferase {ECO:0000303|PubMed:20981366};
DE EC=2.7.7.91 {ECO:0000269|PubMed:20981366};
DE AltName: Full=Cyclitol nucleotidyltransferase {ECO:0000303|PubMed:20981366};
GN Name=valB {ECO:0000303|PubMed:16151088};
GN OrderedLocusNames=SHJG_0277 {ECO:0000312|EMBL:AEY85555.1};
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].
RC STRAIN=5008 {ECO:0000312|EMBL:AAW88570.1};
RX PubMed=16151088; DOI=10.1128/aem.71.9.5066-5076.2005;
RA Yu Y., Bai L., Minagawa K., Jian X., Li L., Li J., Chen S., Cao E.,
RA Mahmud T., Floss H.G., Zhou X., Deng Z.;
RT "Gene cluster responsible for validamycin biosynthesis in Streptomyces
RT hygroscopicus subsp. jinggangensis 5008.";
RL Appl. Environ. Microbiol. 71:5066-5076(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=5008 {ECO:0000312|EMBL:ABA41507.1};
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DISRUPTION PHENOTYPE, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=5008;
RX PubMed=20981366; DOI=10.1039/c0ob00475h;
RA Yang J., Xu H., Zhang Y., Bai L., Deng Z., Mahmud T.;
RT "Nucleotidylation of unsaturated carbasugar in validamycin biosynthesis.";
RL Org. Biomol. Chem. 9:438-449(2011).
CC -!- FUNCTION: Involved in the biosynthesis of the antifungal agent
CC validamycin A (PubMed:16632251, PubMed:20981366). Catalyzes the
CC conversion of valienol 1-phosphate to GDP-valienol. Also able to use
CC efficiently ATP as nucleotidyl donor, but other NDP derivatives are
CC less efficient (PubMed:20981366). {ECO:0000269|PubMed:16632251,
CC ECO:0000269|PubMed:20981366}.
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:20981366};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20981366};
CC Note=Can also use Mn(2+) and Co(2+). {ECO:0000269|PubMed:20981366};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC both validoxylamine A and validamycin A. {ECO:0000269|PubMed:20981366}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; AY753181; AAW88570.1; -; Genomic_DNA.
DR EMBL; DQ164098; ABA41507.1; -; Genomic_DNA.
DR EMBL; CP003275; AEY85555.1; -; Genomic_DNA.
DR RefSeq; WP_014668903.1; NC_017765.1.
DR AlphaFoldDB; H2K888; -.
DR SMR; H2K888; -.
DR STRING; 1133850.SHJG_0277; -.
DR EnsemblBacteria; AEY85555; AEY85555; SHJG_0277.
DR KEGG; shy:SHJG_0277; -.
DR PATRIC; fig|1133850.20.peg.417; -.
DR eggNOG; COG0448; Bacteria.
DR HOGENOM; CLU_029499_14_0_11; -.
DR OMA; CALPPRI; -.
DR OrthoDB; 1557977at2; -.
DR BRENDA; 2.7.7.91; 14749.
DR Proteomes; UP000007170; Chromosome.
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: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 GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..373
FT /note="Valienol-1-phosphate guanylyltransferase"
FT /id="PRO_0000442845"
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; 41472 MW; 772E04825E9C67BF CRC64;
MDGVRAVLLA GGEGRRMGPL GRGRLKPLVP FGGTSRLIDF SIANVHRSGL RDVLLLSQYE
ERRLMDDLHL VWNGRHRGFR IDFGPYDAVY RRSPGKLPEQ LPERTWPLER GTADALLTKA
EYVFRQGDAE ASEILVLHAD HVYRFDYGDM IREHRASKAA LTVSYQRIER RYVHLFGMVE
FDGDGLLTAF EEKPDDPTSD LVFAAFCLFD AATLRRYLEQ LRGTDWQHDI SRDVIPAMLA
GGELIRGYEV KSYWEDIGTV DRYHRAHRGL LRADPTLALS DMPLTVAPEV PRHLVPGGPG
RRASVVAADV ANEGEIVSSV VYPGARIGVD AHVVDCVVLP GAQVPDGTHL ASAIVLEDGS
VQQCEAEREE VAL
