Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

D-inositol 3-phosphate glycosyltransferase

Gene

mshA

Organism
Mycobacterium tuberculosis (strain F11)
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 (MSH) biosynthesis pathway (By similarity). MSH and WhiB3 are probably part of a regulatory circuit that mediates gene expression upon acid stress (like that found in host macrophage phagosomes). MSH is one of the major redox buffers which protects bacteria against redox stressors and antibiotics; loss of MSH or ergothioneine (ERG, the other major redox buffer in this bacteria) leads to respiratory alterations and bioenergetic deficiencies that negatively impact virulence (By similarity).UniRule annotationBy similarity

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)DescriptionActionsGraphical viewLength
Binding sitei531D-inositol 3-phosphateUniRule annotation1
Binding sitei67UDP-GlcNAc; via amide nitrogenUniRule annotation1
Binding sitei1221D-inositol 3-phosphateUniRule annotation1
Binding sitei1551D-inositol 3-phosphateUniRule annotation1
Binding sitei1791D-inositol 3-phosphateUniRule annotation1
Binding sitei1991D-inositol 3-phosphateUniRule annotation1
Binding sitei273UDP-GlcNAcUniRule annotation1
Binding sitei278UDP-GlcNAcUniRule annotation1
Binding sitei331UDP-GlcNAc; via amide nitrogen and carbonyl oxygenUniRule annotation1
Metal bindingi340Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi341Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi343Magnesium; via carbonyl oxygenUniRule annotation1
Binding sitei353UDP-GlcNAcUniRule annotation1
Binding sitei361UDP-GlcNAcUniRule annotation1
Metal bindingi367MagnesiumUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandMagnesium, 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:TBFG_10494
OrganismiMycobacterium tuberculosis (strain F11)
Taxonomic identifieri336982 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004001421 – 480D-inositol 3-phosphate glycosyltransferaseAdd BLAST480

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA5WJJ8.
SMRiA5WJJ8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni59 – 60UDP-GlcNAc bindingUniRule annotation2
Regioni64 – 691D-inositol 3-phosphate bindingUniRule annotation6

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000077288.
KOiK15521.
OMAiHTMAKVK.

Family and domain databases

HAMAPiMF_01695. MshA. 1 hit.
InterProiView protein in InterPro
IPR001296. Glyco_trans_1.
IPR028098. Glyco_trans_4-like_N.
IPR017814. Mycothiol_biosynthesis_MshA.
PfamiView protein in Pfam
PF13439. Glyco_transf_4. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
TIGRFAMsiTIGR03449. mycothiol_MshA. 1 hit.

Sequencei

Sequence statusi: Complete.

A5WJJ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVRHDDGS GLIAQRRPVR GEGATRSRGP SGPSNRNVSA ADDPRRVALL
60 70 80 90 100
AVHTSPLAQP GTGDAGGMNV YMLQSALHLA RRGIEVEIFT RATASADPPV
110 120 130 140 150
VRVAPGVLVR NVVAGPFEGL DKYDLPTQLC AFAAGVLRAE AVHEPGYYDI
160 170 180 190 200
VHSHYWLSGQ VGWLARDRWA VPLVHTAHTL AAVKNAALAD GDGPEPPLRT
210 220 230 240 250
VGEQQVVDEA DRLIVNTDDE ARQVISLHGA DPARIDVVHP GVDLDVFRPG
260 270 280 290 300
DRRAARAALG LPVDERVVAF VGRIQPLKAP DIVLRAAAKL PGVRIIVAGG
310 320 330 340 350
PSGSGLASPD GLVRLADELG ISARVTFLPP QSHTDLATLF RAADLVAVPS
360 370 380 390 400
YSESFGLVAV EAQACGTPVV AAAVGGLPVA VRDGITGTLV SGHEVGQWAD
410 420 430 440 450
AIDHLLRLCA GPRGRVMSRA AARHAATFSW ENTTDALLAS YRRAIGEYNA
460 470 480
ERQRRGGEVI SDLVAVGKPR HWTPRRGVGA
Length:480
Mass (Da):50,541
Last modified:July 28, 2009 - v1
Checksum:i2134755E894A9CCF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000717 Genomic DNA. Translation: ABR04837.1.
RefSeqiWP_003402367.1. NZ_KK339377.1.

Genome annotation databases

EnsemblBacteriaiABR04837; ABR04837; TBFG_10494.
KEGGimtf:TBFG_10494.
PATRICifig|336982.11.peg.535.

Similar proteinsi

Entry informationi

Entry nameiMSHA_MYCTF
AccessioniPrimary (citable) accession number: A5WJJ8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: July 28, 2009
Last modified: September 27, 2017
This is version 54 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families