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Protein

D-inositol 3-phosphate glycosyltransferase

Gene

mshA

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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 sitei34 – 3411D-inositol 3-phosphateUniRule annotation
Binding sitei48 – 481UDP-GlcNAc; via amide nitrogenUniRule annotation
Binding sitei103 – 10311D-inositol 3-phosphateUniRule annotation
Binding sitei136 – 13611D-inositol 3-phosphateUniRule annotation
Binding sitei160 – 16011D-inositol 3-phosphateUniRule annotation
Binding sitei180 – 18011D-inositol 3-phosphateUniRule annotation
Binding sitei267 – 2671UDP-GlcNAcUniRule annotation
Binding sitei272 – 2721UDP-GlcNAcUniRule annotation
Binding sitei333 – 3331UDP-GlcNAc; via amide nitrogen and carbonyl oxygenUniRule annotation
Metal bindingi342 – 3421Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi343 – 3431Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi345 – 3451Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei355 – 3551UDP-GlcNAcUniRule annotation
Binding sitei363 – 3631UDP-GlcNAcUniRule annotation
Metal bindingi369 – 3691MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Magnesium, Metal-binding

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

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:SCO4204
ORF Names:2SCD46.18
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457D-inositol 3-phosphate glycosyltransferasePRO_0000400162Add
BLAST

Expressioni

Inductioni

Transiently induced by thiol-oxidant diamide, under control of SigR. Also induced when mycothiol is oxidized or conjugated.1 Publication

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi100226.SCO4204.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 412UDP-GlcNAc bindingUniRule annotation
Regioni45 – 5061D-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.
InParanoidiQ9FCG5.
KOiK15521.
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.

Q9FCG5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQYVSRLGR RSPAASPRLR LNRKPRRVAM LSVHTSPLHQ PGTGDAGGMN
60 70 80 90 100
VYIVELAQRL AAINIEVEIF TRATTAALPP AVELAPGVLV RHVDAGPYEG
110 120 130 140 150
LAKEELPAQL CAFTHGVMQA WAGHRPGHYD LVHSHYWLSG HVGWLAAQRW
160 170 180 190 200
GAPLVHAMHT MAKVKNANLA DGDTPEPAAR VIGETQIVAA SDRLIANTAE
210 220 230 240 250
EADELVRHYA ADPDKVAVVH PGVNLERFRP FPKGRVPGPG QHGNARAAAR
260 270 280 290 300
ARLGLPQDAL IPLFAGRIQP LKAPDILLRA VAVLLDERPE LRSRIVVPVV
310 320 330 340 350
GGPSGSGLAK PEGLQKLAAR LGIADVVRFR PPVGQEQLAD WFRAASVLVM
360 370 380 390 400
PSYSESFGLV AIEAQAAGTP VLAAAVGGLP VAVRDGHTGR LVHGHDPAAY
410 420 430 440 450
ARVLRDFADN PDLTPRMGDA AARHAQSFGW DSAAATTADV YTAAIQSYRR

RVRSHHG
Length:457
Mass (Da):48,864
Last modified:July 24, 2013 - v2
Checksum:i8763E5E709B4F7B1
GO

Sequence cautioni

The sequence CAC04040.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939119 Genomic DNA. Translation: CAC04040.1. Different initiation.
RefSeqiNP_628379.1. NC_003888.3.
WP_011029499.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAC04040; CAC04040; CAC04040.
GeneIDi1099644.
KEGGisco:SCO4204.
PATRICi23738206. VBIStrCoe124346_4268.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939119 Genomic DNA. Translation: CAC04040.1. Different initiation.
RefSeqiNP_628379.1. NC_003888.3.
WP_011029499.1. NC_003888.3.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO4204.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC04040; CAC04040; CAC04040.
GeneIDi1099644.
KEGGisco:SCO4204.
PATRICi23738206. VBIStrCoe124346_4268.

Phylogenomic databases

eggNOGiENOG4107R5M. Bacteria.
COG0438. LUCA.
HOGENOMiHOG000077288.
InParanoidiQ9FCG5.
KOiK15521.
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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.
  2. "Mycothiol regulates and is regulated by a thiol-specific antisigma factor RsrA and sigma(R) in Streptomyces coelicolor."
    Park J.H., Roe J.H.
    Mol. Microbiol. 68:861-870(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, PROBABLE START SITE.
    Strain: ATCC BAA-471 / A3(2) / M145.

Entry informationi

Entry nameiMSHA_STRCO
AccessioniPrimary (citable) accession number: Q9FCG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: July 24, 2013
Last modified: May 11, 2016
This is version 78 of the entry and version 2 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.