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Protein

D-inositol 3-phosphate glycosyltransferase

Gene

mshA

Organism
Rhodococcus erythropolis (strain PR4 / NBRC 100887)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway.UniRule annotation

Catalytic activityi

UDP-N-acetyl-D-glucosamine + 1D-myo-inositol 3-phosphate = UDP + 1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol 3-phosphate.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei15 – 1511D-inositol 3-phosphateUniRule annotation
Binding sitei29 – 291UDP-GlcNAc; via amide nitrogenUniRule annotation
Binding sitei84 – 8411D-inositol 3-phosphateUniRule annotation
Binding sitei117 – 11711D-inositol 3-phosphateUniRule annotation
Binding sitei141 – 14111D-inositol 3-phosphateUniRule annotation
Binding sitei161 – 16111D-inositol 3-phosphateUniRule annotation
Binding sitei235 – 2351UDP-GlcNAcUniRule annotation
Binding sitei240 – 2401UDP-GlcNAcUniRule annotation
Binding sitei299 – 2991UDP-GlcNAc; via amide nitrogen and carbonyl oxygenUniRule annotation
Metal bindingi308 – 3081Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi309 – 3091Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi311 – 3111Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei321 – 3211UDP-GlcNAcUniRule annotation
Binding sitei329 – 3291UDP-GlcNAcUniRule annotation
Metal bindingi335 – 3351MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciRERY234621:GHDE-1636-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
D-inositol 3-phosphate glycosyltransferase (EC:2.4.1.250UniRule annotation)
Alternative name(s):
N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferaseUniRule annotation
Short name:
GlcNAc-Ins-P N-acetylglucosaminyltransferaseUniRule annotation
Gene namesi
Name:mshAUniRule annotation
Ordered Locus Names:RER_16170
OrganismiRhodococcus erythropolis (strain PR4 / NBRC 100887)
Taxonomic identifieri234621 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus
Proteomesi
  • UP000002204 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 442442D-inositol 3-phosphate glycosyltransferasePRO_0000400150Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi234621.RER_16170.

Structurei

3D structure databases

ProteinModelPortaliC0ZUT0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 222UDP-GlcNAc bindingUniRule annotation
Regioni26 – 3161D-inositol 3-phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the glycosyltransferase group 1 family. MshA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107R5M. Bacteria.
COG0438. LUCA.
HOGENOMiHOG000077288.
KOiK15521.
OMAiHTMAKVK.
OrthoDBiEOG647TVR.

Family and domain databases

HAMAPiMF_01695. MshA.
InterProiIPR001296. Glyco_trans_1.
IPR028098. Glyco_trans_4-like_N.
IPR017814. Mycothiol_biosynthesis_MshA.
[Graphical view]
PfamiPF13439. Glyco_transf_4. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03449. mycothiol_MshA. 1 hit.

Sequencei

Sequence statusi: Complete.

C0ZUT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHISRPRRVA VLSVHTSPLA QPGTGDAGGM NVYVLQSAIQ LAKRGVEVEI
60 70 80 90 100
FTRATSSADA PVVDAAPGVR VRNIAAGPFE GLDKADLPTQ LCAFVAGVLR
110 120 130 140 150
EEARHEPGYY SLIHSHYWLS GQVGWLARDR WGVPLVHTAH TLAAVKNLSL
160 170 180 190 200
AEGDTPEPAA RQIGEQQVVA ESDRLVANTT DEAKALHELY GADPTRIDVV
210 220 230 240 250
APGADLTRYR PGDRDSARAS LGLDPGEIVV TFVGRIQPLK APDVLLRAAA
260 270 280 290 300
EVISRSPGLP LRILVVGGPS GTGLARPDVL IELARSLGIT AQVTFLPPQA
310 320 330 340 350
PERLADVYRA SDLVAVPSYS ESFGLVAIEA QACGTPVIAA DVGGLGVAVR
360 370 380 390 400
NGETGLLVQG HRTEDWAGAL ESLVTAPTRL AELAAQAPRH AENFSWEHTA
410 420 430 440
DGLLESYRKA AVNYNNGTGP SDFSPRRARG LWRLRRTGGV RT
Length:442
Mass (Da):46,924
Last modified:May 26, 2009 - v1
Checksum:iD17A93497C9FBC33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008957 Genomic DNA. Translation: BAH32325.1.
RefSeqiWP_020906764.1. NC_012490.1.

Genome annotation databases

EnsemblBacteriaiBAH32325; BAH32325; RER_16170.
GeneIDi7715130.
KEGGirer:RER_16170.
PATRICi23189604. VBIRhoEry66701_2103.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008957 Genomic DNA. Translation: BAH32325.1.
RefSeqiWP_020906764.1. NC_012490.1.

3D structure databases

ProteinModelPortaliC0ZUT0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi234621.RER_16170.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAH32325; BAH32325; RER_16170.
GeneIDi7715130.
KEGGirer:RER_16170.
PATRICi23189604. VBIRhoEry66701_2103.

Phylogenomic databases

eggNOGiENOG4107R5M. Bacteria.
COG0438. LUCA.
HOGENOMiHOG000077288.
KOiK15521.
OMAiHTMAKVK.
OrthoDBiEOG647TVR.

Enzyme and pathway databases

BioCyciRERY234621:GHDE-1636-MONOMER.

Family and domain databases

HAMAPiMF_01695. MshA.
InterProiIPR001296. Glyco_trans_1.
IPR028098. Glyco_trans_4-like_N.
IPR017814. Mycothiol_biosynthesis_MshA.
[Graphical view]
PfamiPF13439. Glyco_transf_4. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03449. mycothiol_MshA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
    Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PR4 / NBRC 100887.

Entry informationi

Entry nameiMSHA_RHOE4
AccessioniPrimary (citable) accession number: C0ZUT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: May 26, 2009
Last modified: May 11, 2016
This is version 45 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

Complete proteome, Reference proteome

Documents

  1. 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.