VALL_STRHJ
ID VALL_STRHJ Reviewed; 497 AA.
AC H2K885; Q1L2L2;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Validamine 7-phosphate valienyltransferase {ECO:0000303|PubMed:16632251};
DE EC=2.5.1.135 {ECO:0000250|UniProtKB:Q15JG1};
DE AltName: Full=Pseudoglycosyltransferase {ECO:0000250|UniProtKB:Q15JG1};
DE AltName: Full=Trehalose 6-phosphate synthase-like enzyme VldE {ECO:0000250|UniProtKB:Q15JG1};
GN Name=valL {ECO:0000303|PubMed:16632251};
GN OrderedLocusNames=SHJG_0274 {ECO:0000312|EMBL:AEY85552.1};
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], AND FUNCTION.
RC STRAIN=5008 {ECO:0000312|EMBL:ABA41504.1};
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 X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-497 IN COMPLEX WITH SUBSTRATE
RP ANALOG, FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RC STRAIN=5008;
RX PubMed=22384130; DOI=10.1371/journal.pone.0032033;
RA Zheng L., Zhou X., Zhang H., Ji X., Li L., Huang L., Bai L., Zhang H.;
RT "Structural and functional analysis of validoxylamine A 7'-phosphate
RT synthase ValL involved in validamycin A biosynthesis.";
RL PLoS ONE 7:E32033-E32033(2012).
CC -!- FUNCTION: Involved in the biosynthesis of the antifungal agent
CC validamycin A (PubMed:16632251). Catalyzes the condensation between
CC GDP-valienol and validamine 7-phosphate via a nonglycosidic C-N bond
CC formation to yield validoxylamine A 7'-phosphate (PubMed:22384130).
CC {ECO:0000269|PubMed:16632251, ECO:0000269|PubMed:22384130}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-valienol + validamine 7-phosphate = GDP + H(+) +
CC validoxylamine A 7'-phosphate; Xref=Rhea:RHEA:32119,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58189, ChEBI:CHEBI:91253,
CC ChEBI:CHEBI:111503, ChEBI:CHEBI:111504; EC=2.5.1.135;
CC Evidence={ECO:0000250|UniProtKB:Q15JG1};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22384130}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC both validoxylamine A and validamycin A. {ECO:0000269|PubMed:22384130}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000305}.
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DR EMBL; DQ164098; ABA41504.1; -; Genomic_DNA.
DR EMBL; CP003275; AEY85552.1; -; Genomic_DNA.
DR RefSeq; WP_014668900.1; NC_017765.1.
DR PDB; 3T5T; X-ray; 1.70 A; A/B=2-497.
DR PDB; 3T7D; X-ray; 1.70 A; A/B=2-497.
DR PDBsum; 3T5T; -.
DR PDBsum; 3T7D; -.
DR AlphaFoldDB; H2K885; -.
DR SMR; H2K885; -.
DR STRING; 1133850.SHJG_0274; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR EnsemblBacteria; AEY85552; AEY85552; SHJG_0274.
DR KEGG; shy:SHJG_0274; -.
DR PATRIC; fig|1133850.20.peg.413; -.
DR eggNOG; COG0380; Bacteria.
DR HOGENOM; CLU_002351_7_1_11; -.
DR OMA; SWIASAD; -.
DR OrthoDB; 556566at2; -.
DR BRENDA; 2.5.1.135; 14749.
DR Proteomes; UP000007170; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR InterPro; IPR001830; Glyco_trans_20.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..497
FT /note="Validamine 7-phosphate valienyltransferase"
FT /id="PRO_0000442847"
FT BINDING 158
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000250|UniProtKB:Q15JG1"
FT BINDING 182
FT /ligand="validamine 7-phosphate"
FT /ligand_id="ChEBI:CHEBI:111503"
FT /evidence="ECO:0000305|PubMed:22384130,
FT ECO:0007744|PDB:3T7D"
FT BINDING 290
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000305|PubMed:22384130,
FT ECO:0007744|PDB:3T7D"
FT BINDING 295
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000250|UniProtKB:Q15JG1"
FT BINDING 321
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000250|UniProtKB:Q15JG1"
FT BINDING 325..326
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000250|UniProtKB:Q15JG1"
FT BINDING 361..362
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000250|UniProtKB:Q15JG1"
FT BINDING 366
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000250|UniProtKB:Q15JG1"
FT BINDING 383..386
FT /ligand="validamine 7-phosphate"
FT /ligand_id="ChEBI:CHEBI:111503"
FT /evidence="ECO:0000305|PubMed:22384130,
FT ECO:0007744|PDB:3T7D"
FT BINDING 387..388
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000250|UniProtKB:Q15JG1"
FT BINDING 391
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000250|UniProtKB:Q15JG1"
FT CONFLICT 194..198
FT /note="Missing (in Ref. 1; ABA41504)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 54943 MW; 91CDAB5D51B859DC CRC64;
MTGSEIFLAS KRAAITYDTD PATGEPRAWL APGGTGNVVA EQAGVLNISW IASADSEDDR
RASALNPDGV TMELHSGREI LVRLIRHDPA VFRNVQNFMT ANLMWAANNY GWDRWTQPSF
GSDAREGWAD FGRFTRDFAD AILKSSAQSA DPVYLVHDYQ LVGVPALLRE QRPDAPILLF
VHIPWPSADY WRILPKEIRT GILHGMLPAT TIGFFADRWC RNFLESVADL LPDARIDREA
MTVEWRGHRT RLRTMPLGYS PLTLDGRNPQ LPEGIEEWAD GHRLVVHSGR TDPIKNAERA
VRAFVLAARG GGLEKTRMLV RMNPNRLYVP ANADYVHRVE TAVAEANAEL GSDTVRIDND
NDVNHTIACF RRADLLIFNS TVDGQNLSTF EAPLVNERDA DVILSETCGA AEVLGEYCRS
VNPFDLVEQA EAISAALAAG PRQRAEAAAR RRDAARPWTL EAWVQAQLDG LAADHAARTA
TAERFDTAPA VSTRADL
