UniProtKB - P9WMY7 (MSHA_MYCTU)
Protein
D-inositol 3-phosphate glycosyltransferase
Gene
mshA
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Catalyzes the transfer of an 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 (PubMed:12754249). MSH and WhiB3 are probably part of a regulatory circuit that mediates gene expression upon acid stress (like that found in host macrophage phagosomes) (PubMed:26637353). 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 (PubMed:26774486).2 Publications1 Publication
Catalytic activityi
- 1D-myo-inositol 3-phosphate + UDP-N-acetyl-α-D-glucosamine = 1D-myo-inositol 2-acetamido-2-deoxy-α-D-glucopyranoside 3-phosphate + H+ + UDPUniRule annotationEC:2.4.1.250UniRule annotation
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 53 | 1D-inositol 3-phosphateUniRule annotation | 1 | |
Binding sitei | 67 | UDP-GlcNAc; via amide nitrogenUniRule annotation | 1 | |
Binding sitei | 122 | 1D-inositol 3-phosphateUniRule annotation | 1 | |
Binding sitei | 155 | 1D-inositol 3-phosphateUniRule annotation | 1 | |
Binding sitei | 179 | 1D-inositol 3-phosphateUniRule annotation | 1 | |
Binding sitei | 199 | 1D-inositol 3-phosphateUniRule annotation | 1 | |
Binding sitei | 273 | UDP-GlcNAcUniRule annotation | 1 | |
Binding sitei | 278 | UDP-GlcNAcUniRule annotation | 1 | |
Binding sitei | 331 | UDP-GlcNAc; via amide nitrogen and carbonyl oxygenUniRule annotation | 1 | |
Metal bindingi | 340 | Magnesium; via carbonyl oxygenUniRule annotation | 1 | |
Metal bindingi | 341 | Magnesium; via carbonyl oxygenUniRule annotation | 1 | |
Metal bindingi | 343 | Magnesium; via carbonyl oxygenUniRule annotation | 1 | |
Binding sitei | 353 | UDP-GlcNAcUniRule annotation | 1 | |
Binding sitei | 361 | UDP-GlcNAcUniRule annotation | 1 | |
Metal bindingi | 367 | MagnesiumUniRule annotation | 1 |
GO - Molecular functioni
- acetylglucosaminyltransferase activity Source: MTBBASE
- D-inositol-3-phosphate glycosyltransferase activity Source: UniProtKB-EC
- magnesium ion binding Source: UniProtKB-UniRule
- transferase activity, transferring glycosyl groups Source: GO_Central
GO - Biological processi
- mycothiol biosynthetic process Source: MTBBASE
Keywordsi
Molecular function | Glycosyltransferase, Transferase |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
Reactomei | R-MTU-879299, Mycothiol biosynthesis |
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:mshA1 PublicationUniRule annotation Ordered Locus Names:Rv0486 ORF Names:MTCY20G9.12 |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv0486 |
Pathology & Biotechi
Disruption phenotypei
Increased intracellular levels of ergothioneine, 8-fold increase in reactive oxygen species-producing cells, decreased resistance to the antibiotics rifampicin, isoniazid, bedaquiline and clofazimine (PubMed:26774486). Increased oxygen consumption and extracellular acidification rates, which are further increased by membrane uncoupler CCCP, indicative of electron chain dysfunction in the absence of MSH (PubMed:26774486). Absence leads to alteration of transcript levels for 139 genes which probably compensate for loss of redox control (PubMed:26774486). Loss of induction of some pH-inducible genes at pH 4.5, including the redox-sensor whiB3 (PubMed:26637353).2 Publications
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000080318 | 1 – 480 | D-inositol 3-phosphate glycosyltransferaseAdd BLAST | 480 |
Proteomic databases
PaxDbi | P9WMY7 |
Interactioni
Subunit structurei
Homodimer.
UniRule annotationProtein-protein interaction databases
STRINGi | 83332.Rv0486 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 59 – 60 | UDP-GlcNAc bindingBy similarity | 2 | |
Regioni | 64 – 69 | 1D-inositol 3-phosphate bindingUniRule annotation | 6 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0438, Bacteria |
OMAi | HTMAKVK |
PhylomeDBi | P9WMY7 |
Family and domain databases
HAMAPi | MF_01695, MshA, 1 hit |
InterProi | View protein in InterPro IPR001296, Glyco_trans_1 IPR028098, Glyco_trans_4-like_N IPR017814, Mycothiol_biosynthesis_MshA |
Pfami | View protein in Pfam PF13439, Glyco_transf_4, 1 hit PF00534, Glycos_transf_1, 1 hit |
TIGRFAMsi | TIGR03449, mycothiol_MshA, 1 hit |
i Sequence
Sequence statusi: Complete.
P9WMY7-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43220.1 |
PIRi | A70744 |
RefSeqi | NP_215000.1, NC_000962.3 WP_003402367.1, NZ_NVQJ01000002.1 |
Genome annotation databases
GeneIDi | 887160 |
KEGGi | mtu:Rv0486 |
PATRICi | fig|83332.111.peg.533 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43220.1 |
PIRi | A70744 |
RefSeqi | NP_215000.1, NC_000962.3 WP_003402367.1, NZ_NVQJ01000002.1 |
3D structure databases
SMRi | P9WMY7 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv0486 |
Proteomic databases
PaxDbi | P9WMY7 |
Genome annotation databases
GeneIDi | 887160 |
KEGGi | mtu:Rv0486 |
PATRICi | fig|83332.111.peg.533 |
Organism-specific databases
TubercuListi | Rv0486 |
Phylogenomic databases
eggNOGi | COG0438, Bacteria |
OMAi | HTMAKVK |
PhylomeDBi | P9WMY7 |
Enzyme and pathway databases
Reactomei | R-MTU-879299, Mycothiol biosynthesis |
Family and domain databases
HAMAPi | MF_01695, MshA, 1 hit |
InterProi | View protein in InterPro IPR001296, Glyco_trans_1 IPR028098, Glyco_trans_4-like_N IPR017814, Mycothiol_biosynthesis_MshA |
Pfami | View protein in Pfam PF13439, Glyco_transf_4, 1 hit PF00534, Glycos_transf_1, 1 hit |
TIGRFAMsi | TIGR03449, mycothiol_MshA, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MSHA_MYCTU | |
Accessioni | P9WMY7Primary (citable) accession number: P9WMY7 Secondary accession number(s): L0T3R4, P64707, Q11152 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | April 7, 2021 | |
This is version 39 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families