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Protein

Glucosyl-3-phosphoglycerate synthase

Gene

MAP_2569c

Organism
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of methylglucose lipopolysaccharides (MGLPs). Catalyzes the condensation of UDP-glucose and 3-phospho-glycerate (3-PGA) to yield glucosyl-3-phosphoglycerate (GPG). Although UDP-glucose is the natural donor sugar, GpgS can also use UDP-GalNAc, UDPGlcNAc, UDP-alpha-L-arabinose, UDP-Gal, UDP-Glc, UDP-alpha-Dglucuronic acid, and UDP-alpha-D-xylose as donor substrates.1 Publication

Catalytic activityi

NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate.1 Publication

Cofactori

Mg2+1 Publication, Ca2+1 Publication, Mn2+1 Publication, Fe2+1 Publication, Co2+1 PublicationNote: Divalent metal cations. Probably Mg2+, but can also use Ca2+, Mn2+, Fe2+ or Co2+ ions.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei86 – 861NDP-glucose
Binding sitei116 – 1161NDP-glucose
Metal bindingi141 – 1411Magnesium
Binding sitei234 – 2341NDP-glucose
Sitei263 – 2631Important for coordination of the donor substrate and for stabilization of the donor substrate product
Binding sitei266 – 2661NDP-glucose
Binding sitei320 – 3201NDP-glucose

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMAVI262316:GCQR-2605-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucosyl-3-phosphoglycerate synthase (EC:2.4.1.266)
Gene namesi
Ordered Locus Names:MAP_2569c
OrganismiMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Taxonomic identifieri262316 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)
Proteomesi
  • UP000000580 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Glucosyl-3-phosphoglycerate synthasePRO_0000420164Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi262316.MAP2569c.

Structurei

Secondary structure

1
329
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 263Combined sources
Turni27 – 293Combined sources
Beta strandi30 – 323Combined sources
Helixi38 – 436Combined sources
Turni44 – 474Combined sources
Beta strandi50 – 589Combined sources
Turni60 – 623Combined sources
Helixi63 – 708Combined sources
Helixi71 – 733Combined sources
Turni75 – 773Combined sources
Beta strandi78 – 858Combined sources
Helixi92 – 987Combined sources
Beta strandi102 – 1054Combined sources
Helixi106 – 1094Combined sources
Helixi119 – 12911Combined sources
Beta strandi133 – 1375Combined sources
Beta strandi142 – 1443Combined sources
Helixi149 – 15810Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi165 – 1717Combined sources
Helixi190 – 1945Combined sources
Helixi196 – 2038Combined sources
Helixi205 – 2095Combined sources
Beta strandi218 – 2214Combined sources
Helixi222 – 2254Combined sources
Helixi233 – 2353Combined sources
Helixi236 – 24813Combined sources
Helixi250 – 2523Combined sources
Beta strandi253 – 2608Combined sources
Helixi268 – 2703Combined sources
Helixi271 – 28515Combined sources
Beta strandi296 – 3027Combined sources
Beta strandi308 – 3125Combined sources
Helixi323 – 3253Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CKJX-ray1.80A1-329[»]
3CKNX-ray2.20A1-329[»]
3CKOX-ray2.50A1-329[»]
3CKQX-ray3.00A1-329[»]
3CKVX-ray2.00A1-329[»]
ProteinModelPortaliQ73WU1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ73WU1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 595NDP-glucose binding
Regioni140 – 1412NDP-glucose binding
Regioni189 – 19243-phospho-D-glycerate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Phylogenomic databases

eggNOGiENOG4105C3Q. Bacteria.
COG0463. LUCA.
KOiK13693.
OMAiDRPPMNT.
OrthoDBiEOG6FJNC1.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q73WU1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSDLVAGE LAGDGLRDTR PGDTWLADRS WNRPGWTVAE LEAAKAGRTI
60 70 80 90 100
SVVLPALDEE DTIGSVIDSI SPLVDGLVDE LIVLDSGSTD DTEIRAVAAG
110 120 130 140 150
ARVVSREQAL PEVPIRPGKG EALWRSLAAS RGDIVVFVDS DLINPHPMFV
160 170 180 190 200
PWLVGPLLTG DGVHLVKSFY RRPLNVGDAG GGAGATGGGR VTELVARPLL
210 220 230 240 250
AALRPELGCI LQPLGGEYAA TRELLTSVPF APGYGVEIGL LVDTFDRLGL
260 270 280 290 300
DAIAQVNLGV REHRNRPLAE LGAMSRQVIA TLLSRCGIPD SGVGLTQFVA
310 320
DGPEGQSYTQ HTWPVSLADR PPMQAIRPR
Length:329
Mass (Da):34,795
Last modified:July 5, 2004 - v1
Checksum:i06493E07C809B6E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016958 Genomic DNA. Translation: AAS04886.1.
RefSeqiWP_003878473.1. NC_002944.2.

Genome annotation databases

EnsemblBacteriaiAAS04886; AAS04886; MAP_2569c.
GeneIDi2717539.
KEGGimpa:MAP_2569c.
PATRICi17997830. VBIMycAvi108102_2729.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016958 Genomic DNA. Translation: AAS04886.1.
RefSeqiWP_003878473.1. NC_002944.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CKJX-ray1.80A1-329[»]
3CKNX-ray2.20A1-329[»]
3CKOX-ray2.50A1-329[»]
3CKQX-ray3.00A1-329[»]
3CKVX-ray2.00A1-329[»]
ProteinModelPortaliQ73WU1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262316.MAP2569c.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS04886; AAS04886; MAP_2569c.
GeneIDi2717539.
KEGGimpa:MAP_2569c.
PATRICi17997830. VBIMycAvi108102_2729.

Phylogenomic databases

eggNOGiENOG4105C3Q. Bacteria.
COG0463. LUCA.
KOiK13693.
OMAiDRPPMNT.
OrthoDBiEOG6FJNC1.

Enzyme and pathway databases

BioCyciMAVI262316:GCQR-2605-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ73WU1.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
    Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
    Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-968 / K-10.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MANGANESE IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, SUBUNIT.

Entry informationi

Entry nameiGPGS_MYCPA
AccessioniPrimary (citable) accession number: Q73WU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: July 5, 2004
Last modified: March 16, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.