VLDE_STRHL
ID VLDE_STRHL Reviewed; 497 AA.
AC Q15JG1;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Validamine 7-phosphate valienyltransferase {ECO:0000303|PubMed:21766819};
DE EC=2.5.1.135 {ECO:0000269|PubMed:21766819};
DE AltName: Full=Pseudoglycosyltransferase {ECO:0000303|PubMed:21766819};
DE AltName: Full=Trehalose 6-phosphate synthase-like enzyme VldE {ECO:0000303|PubMed:21766819};
GN Name=vldE {ECO:0000303|PubMed:16725283};
GN ORFNames=SHL15_8006 {ECO:0000312|EMBL:ALO98983.1};
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:ABC67269.1};
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:ALO98983.1, ECO:0000312|Proteomes:UP000057753};
RA Kim K.M.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP REACTION MECHANISM, AND SUBUNIT.
RC STRAIN=ATCC 21432 / NBRC 12704 / KCTC 1717 / KCCM 11405;
RX PubMed=23028689; DOI=10.1371/journal.pone.0044934;
RA Cavalier M.C., Yim Y.S., Asamizu S., Neau D., Almabruk K.H., Mahmud T.,
RA Lee Y.H.;
RT "Mechanistic insights into validoxylamine A 7'-phosphate synthesis by VldE
RT using the structure of the entire product complex.";
RL PLoS ONE 7:E44934-E44934(2012).
CC -!- FUNCTION: Involved in the biosynthesis of the antifungal agent
CC validamycin A (PubMed:16725283). 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:21766819).
CC {ECO:0000269|PubMed:16725283, ECO:0000269|PubMed:21766819}.
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:0000269|PubMed:21766819};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=59.7 uM for GDP-valienol {ECO:0000269|PubMed:21766819};
CC KM=308 uM for validamine 7-phosphate {ECO:0000269|PubMed:21766819};
CC Note=kcat is 7 min(-1) with GDP-valienol as substrate. kcat is 7
CC min(-1) with validamine 7-phosphate as substrate.
CC {ECO:0000269|PubMed:21766819};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23028689}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000305}.
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DR EMBL; DQ223652; ABC67269.1; -; Genomic_DNA.
DR EMBL; CP013220; ALO98983.1; -; Genomic_DNA.
DR RefSeq; WP_014668900.1; NZ_CP013220.1.
DR PDB; 3VDM; X-ray; 1.98 A; A/B=1-497.
DR PDB; 3VDN; X-ray; 2.55 A; B=1-497.
DR PDB; 4F96; X-ray; 2.15 A; A/B=1-497.
DR PDB; 4F97; X-ray; 2.11 A; A/B=1-497.
DR PDB; 4F9F; X-ray; 2.81 A; A/B/C/D/E/F=1-497.
DR PDBsum; 3VDM; -.
DR PDBsum; 3VDN; -.
DR PDBsum; 4F96; -.
DR PDBsum; 4F97; -.
DR PDBsum; 4F9F; -.
DR AlphaFoldDB; Q15JG1; -.
DR SMR; Q15JG1; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR EnsemblBacteria; ALO98983; ALO98983; SHL15_8006.
DR PATRIC; fig|264445.3.peg.8517; -.
DR BioCyc; MetaCyc:MON-13774; -.
DR BRENDA; 2.4.1.338; 6043.
DR BRENDA; 2.5.1.135; 14504.
DR Proteomes; UP000057753; Chromosome II.
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; Transferase.
FT CHAIN 1..497
FT /note="Validamine 7-phosphate valienyltransferase"
FT /id="PRO_0000442846"
FT BINDING 158
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000305|PubMed:23028689,
FT ECO:0007744|PDB:4F97"
FT BINDING 182
FT /ligand="validamine 7-phosphate"
FT /ligand_id="ChEBI:CHEBI:111503"
FT /evidence="ECO:0000305|PubMed:23028689,
FT ECO:0007744|PDB:4F97"
FT BINDING 290
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000305|PubMed:23028689,
FT ECO:0007744|PDB:4F96, ECO:0007744|PDB:4F97,
FT ECO:0007744|PDB:4F9F"
FT BINDING 295
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000305|PubMed:23028689,
FT ECO:0007744|PDB:4F96, ECO:0007744|PDB:4F97,
FT ECO:0007744|PDB:4F9F"
FT BINDING 321
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000305|PubMed:23028689,
FT ECO:0007744|PDB:4F97, ECO:0007744|PDB:4F9F"
FT BINDING 325..326
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000305|PubMed:23028689,
FT ECO:0007744|PDB:4F97"
FT BINDING 361..362
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000305|PubMed:23028689,
FT ECO:0007744|PDB:4F96, ECO:0007744|PDB:4F97,
FT ECO:0007744|PDB:4F9F"
FT BINDING 366
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000305|PubMed:23028689,
FT ECO:0007744|PDB:4F96, ECO:0007744|PDB:4F97,
FT ECO:0007744|PDB:4F9F"
FT BINDING 383..386
FT /ligand="validamine 7-phosphate"
FT /ligand_id="ChEBI:CHEBI:111503"
FT /evidence="ECO:0000305|PubMed:23028689,
FT ECO:0007744|PDB:4F97, ECO:0007744|PDB:4F9F"
FT BINDING 387..388
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000305|PubMed:23028689,
FT ECO:0007744|PDB:4F96, ECO:0007744|PDB:4F97,
FT ECO:0007744|PDB:4F9F"
FT BINDING 391
FT /ligand="GDP-valienol"
FT /ligand_id="ChEBI:CHEBI:91253"
FT /evidence="ECO:0000305|PubMed:23028689,
FT ECO:0007744|PDB:4F96, ECO:0007744|PDB:4F97,
FT ECO:0007744|PDB:4F9F"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3VDM"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3VDN"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4F97"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:3VDM"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 122..145
FT /evidence="ECO:0007829|PDB:3VDM"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:3VDN"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 217..230
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:3VDM"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 275..279
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 282..292
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 330..350
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 354..359
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 363..372
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:4F97"
FT HELIX 388..395
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:3VDM"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 426..438
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 441..455
FT /evidence="ECO:0007829|PDB:3VDM"
FT HELIX 460..480
FT /evidence="ECO:0007829|PDB:3VDM"
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
