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Protein

Phosphatidyl-myo-inositol mannosyltransferase

Gene

pimA

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM). Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1) (PubMed:12068013, PubMed:19638342, PubMed:19520856). In contrary to PimB, the mannosyltransferase PimA is unable to transfer a mannose residue to the position 6 of the phosphatidyl-myo-inositol of PIM1 (PubMed:19638342).3 Publications

Catalytic activityi

Transfers one or more alpha-D-mannose residues from GDP-mannose to positions 2,6 and others in 1-phosphatidyl-myo-inositol.2 Publications

Cofactori

Mg2+By similarity

Pathwayi: phosphatidylinositol metabolism

This protein is involved in the pathway phosphatidylinositol metabolism, which is part of Phospholipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway phosphatidylinositol metabolism and in Phospholipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei9GDP-mannose1 Publication1
Binding sitei16GDP-mannose; via amide nitrogen2 Publications1
Binding sitei18Phosphatidyl-myo-inositol1 Publication1
Binding sitei68Phosphatidyl-myo-inositol1 Publication1
Sitei118Important for catalytic activity1 Publication1
Binding sitei196GDP-mannose1 Publication1 Publication1
Binding sitei256GDP-mannose2 Publications1
Binding sitei282GDP-mannose2 Publications1

GO - Molecular functioni

  • GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity Source: UniProtKB
  • phosphatidylinositol alpha-mannosyltransferase activity Source: UniProtKB

GO - Biological processi

  • glycolipid biosynthetic process Source: UniProtKB
  • pathogenesis Source: UniProtKB-KW
  • phosphatidylinositol metabolic process Source: UniProtKB
  • phospholipid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism, Virulence

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BRENDAi2.4.1.57. 3512.
UniPathwayiUPA00949.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidyl-myo-inositol mannosyltransferase1 Publication (EC:2.4.1.572 Publications)
Alternative name(s):
Alpha-mannosyltransferase1 Publication
GDP-mannose-dependent alpha-(1-2)-phosphatidylinositol mannosyltransferase1 Publication
Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferaseCurated
Phosphatidylinositol alpha-mannosyltransferase1 Publication
Short name:
PI alpha-mannosyltransferase1 Publication
Gene namesi
Name:pimA1 Publication
Ordered Locus Names:MSMEG_2935, MSMEI_2861
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000006158 Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9Y → A: Loss of mannosyltransferase activity. 1 Publication1
Mutagenesisi18Q → A: Strong decrease of mannosyltransferase activity. 1 Publication1
Mutagenesisi62Y → A: Loss of mannosyltransferase activity. 1 Publication1
Mutagenesisi63N → A: Loss of mannosyltransferase activity. 1 Publication1
Mutagenesisi65S → A: Same activity as the wild-type. 1 Publication1
Mutagenesisi68R → A: Loss of mannosyltransferase activity. 1 Publication1
Mutagenesisi70R → A: Same activity as the wild-type. 1 Publication1
Mutagenesisi77 – 81RKVKK → SSVSS: Loss of mannosyltransferase activity and the ability to bind phospholipid aggregates. 1 Publication5
Mutagenesisi118H → A: Loss of mannosyltransferase activity. 1 Publication1
Mutagenesisi123K → A: 23% less active than the wild-type. 1 Publication1
Mutagenesisi126T → C: Interacts only marginally with GDP and is inactive; when associated with C-359. 1 Publication1
Mutagenesisi126T → W: No change in the activity. 1 Publication1
Mutagenesisi196R → A: Loss of mannosyltransferase activity. 1 Publication1
Mutagenesisi199E → A: Loss of mannosyltransferase activity. 1 Publication1
Mutagenesisi201R → A: Loss of mannosyltransferase activity. 1 Publication1
Mutagenesisi274E → A: Loss of mannosyltransferase activity. 1 Publication1
Mutagenesisi359V → C: Interacts only marginally with GDP and is inactive; when associated with C-126. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003937321 – 386Phosphatidyl-myo-inositol mannosyltransferaseAdd BLAST386

Proteomic databases

PRIDEiA0QWG6.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi246196.MSMEG_2935.

Structurei

Secondary structure

1386
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi16 – 30Combined sources15
Beta strandi34 – 40Combined sources7
Beta strandi51 – 53Combined sources3
Beta strandi57 – 59Combined sources3
Beta strandi66 – 71Combined sources6
Helixi73 – 86Combined sources14
Beta strandi89 – 94Combined sources6
Beta strandi98 – 100Combined sources3
Helixi101 – 108Combined sources8
Beta strandi109 – 117Combined sources9
Helixi120 – 123Combined sources4
Helixi124 – 126Combined sources3
Helixi128 – 131Combined sources4
Helixi132 – 134Combined sources3
Helixi135 – 138Combined sources4
Beta strandi143 – 146Combined sources4
Helixi149 – 159Combined sources11
Beta strandi163 – 165Combined sources3
Helixi172 – 176Combined sources5
Beta strandi190 – 195Combined sources6
Helixi200 – 202Combined sources3
Helixi204 – 217Combined sources14
Beta strandi222 – 227Combined sources6
Helixi231 – 238Combined sources8
Helixi239 – 244Combined sources6
Beta strandi245 – 250Combined sources6
Helixi253 – 262Combined sources10
Beta strandi264 – 268Combined sources5
Helixi278 – 286Combined sources9
Beta strandi289 – 293Combined sources5
Helixi296 – 301Combined sources6
Helixi303 – 305Combined sources3
Beta strandi307 – 311Combined sources5
Helixi316 – 328Combined sources13
Helixi330 – 343Combined sources14
Helixi344 – 347Combined sources4
Helixi349 – 363Combined sources15
Beta strandi371 – 373Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GEJX-ray2.60A1-386[»]
2GEKX-ray2.40A1-386[»]
4N9WX-ray1.94A1-386[»]
4NC9X-ray3.19A/B/C/D1-386[»]
ProteinModelPortaliA0QWG6.
SMRiA0QWG6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA0QWG6.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni62 – 63Phosphatidyl-myo-inositol binding1 Publication2
Regioni201 – 202GDP-mannose binding1 Publication1 Publication2
Regioni251 – 253GDP-mannose binding2 Publications3
Regioni274 – 278GDP-mannose binding1 Publication5

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105E2K. Bacteria.
COG0438. LUCA.
HOGENOMiHOG000077288.
KOiK08256.
OMAiIVCPYSW.
OrthoDBiPOG091H07KJ.

Family and domain databases

InterProiIPR028098. Glyco_trans_4-like_N.
[Graphical view]
PfamiPF13439. Glyco_transf_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A0QWG6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIGMVCPYS FDVPGGVQSH VLQLAEVLRD AGHEVSVLAP ASPHVKLPDY
60 70 80 90 100
VVSGGKAVPI PYNGSVARLR FGPATHRKVK KWIAEGDFDV LHIHEPNAPS
110 120 130 140 150
LSMLALQAAE GPIVATFHTS TTKSLTLSVF QGILRPYHEK IIGRIAVSDL
160 170 180 190 200
ARRWQMEALG SDAVEIPNGV DVASFADAPL LDGYPREGRT VLFLGRYDEP
210 220 230 240 250
RKGMAVLLAA LPKLVARFPD VEILIVGRGD EDELREQAGD LAGHLRFLGQ
260 270 280 290 300
VDDATKASAM RSADVYCAPH LGGESFGIVL VEAMAAGTAV VASDLDAFRR
310 320 330 340 350
VLADGDAGRL VPVDDADGMA AALIGILEDD QLRAGYVARA SERVHRYDWS
360 370 380
VVSAQIMRVY ETVSGAGIKV QVSGAANRDE TAGESV
Length:386
Mass (Da):41,220
Last modified:January 9, 2007 - v1
Checksum:i1A5A6B5A2E36BC2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK72422.1.
CP001663 Genomic DNA. Translation: AFP39325.1.
RefSeqiWP_011728703.1. NZ_CP009494.1.
YP_887254.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK72422; ABK72422; MSMEG_2935.
AFP39325; AFP39325; MSMEI_2861.
GeneIDi4536758.
KEGGimsb:LJ00_14605.
msg:MSMEI_2861.
msm:MSMEG_2935.
PATRICi18078300. VBIMycSme59918_2898.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK72422.1.
CP001663 Genomic DNA. Translation: AFP39325.1.
RefSeqiWP_011728703.1. NZ_CP009494.1.
YP_887254.1. NC_008596.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GEJX-ray2.60A1-386[»]
2GEKX-ray2.40A1-386[»]
4N9WX-ray1.94A1-386[»]
4NC9X-ray3.19A/B/C/D1-386[»]
ProteinModelPortaliA0QWG6.
SMRiA0QWG6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_2935.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Proteomic databases

PRIDEiA0QWG6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK72422; ABK72422; MSMEG_2935.
AFP39325; AFP39325; MSMEI_2861.
GeneIDi4536758.
KEGGimsb:LJ00_14605.
msg:MSMEI_2861.
msm:MSMEG_2935.
PATRICi18078300. VBIMycSme59918_2898.

Phylogenomic databases

eggNOGiENOG4105E2K. Bacteria.
COG0438. LUCA.
HOGENOMiHOG000077288.
KOiK08256.
OMAiIVCPYSW.
OrthoDBiPOG091H07KJ.

Enzyme and pathway databases

UniPathwayiUPA00949.
BRENDAi2.4.1.57. 3512.

Miscellaneous databases

EvolutionaryTraceiA0QWG6.

Family and domain databases

InterProiIPR028098. Glyco_trans_4-like_N.
[Graphical view]
PfamiPF13439. Glyco_transf_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPIMA_MYCS2
AccessioniPrimary (citable) accession number: A0QWG6
Secondary accession number(s): I7FCT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: January 9, 2007
Last modified: November 30, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Was identified as a high-confidence drug target.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.