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Protein

GDP-mannose-dependent alpha-(1-2)-phosphatidylinositol 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

Catalyzes the addition of a mannose residue from GDP-D-mannose to the position 2 of a phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Contrary to PimB, the mannosyltransferase PimA is unable to transfer a mannose residue to the position 6 of the phosphatidyl-myo-inositola of PIM1.2 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.

Pathwayi: phosphatidylinositol metabolism

This protein is involved in the pathway phosphatidylinositol metabolism, which is part of Phospholipid metabolism.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91Substrate1 Publication
Binding sitei16 – 161Substrate; via amide nitrogen1 Publication
Sitei118 – 1181Important for catalytic activity1 Publication
Binding sitei196 – 1961Substrate1 Publication
Binding sitei256 – 2561Substrate1 Publication
Sitei274 – 2741Important for catalytic activity1 Publication
Binding sitei282 – 2821Substrate1 Publication

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

Enzyme and pathway databases

BioCyciMSME246196:GJ4Y-2935-MONOMER.
BRENDAi2.4.1.57. 3512.
UniPathwayiUPA00949.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-mannose-dependent alpha-(1-2)-phosphatidylinositol mannosyltransferase (EC:2.4.1.57)
Alternative name(s):
Alpha-mannosyltransferase
Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase
Phosphatidylinositol alpha-mannosyltransferase
Short name:
PI alpha-mannosyltransferase
Gene namesi
Name:pimA
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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei113 – 13018HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91Y → A: Loss of mannosyltransferase activity. 1 Publication
Mutagenesisi77 – 815RKVKK → SSVSS: Loss of mannosyltransferase activity and the ability to bind phospholipid aggregates. 1 Publication
Mutagenesisi118 – 1181H → A: Loss of mannosyltransferase activity. 1 Publication
Mutagenesisi126 – 1261T → W: No change in the activity. 1 Publication
Mutagenesisi201 – 2011R → A: Loss of mannosyltransferase activity. 1 Publication
Mutagenesisi274 – 2741E → A: Loss of mannosyltransferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 386386GDP-mannose-dependent alpha-(1-2)-phosphatidylinositol mannosyltransferasePRO_0000393732Add
BLAST

Proteomic databases

PRIDEiA0QWG6.

Interactioni

Protein-protein interaction databases

STRINGi246196.MSMEG_2935.

Structurei

Secondary structure

1
386
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi16 – 3015Combined sources
Beta strandi34 – 407Combined sources
Beta strandi51 – 533Combined sources
Beta strandi57 – 593Combined sources
Beta strandi66 – 716Combined sources
Helixi73 – 8614Combined sources
Beta strandi89 – 946Combined sources
Beta strandi98 – 1003Combined sources
Helixi101 – 1088Combined sources
Beta strandi109 – 1179Combined sources
Helixi120 – 1234Combined sources
Helixi124 – 1263Combined sources
Helixi128 – 1314Combined sources
Helixi132 – 1343Combined sources
Helixi135 – 1384Combined sources
Beta strandi143 – 1464Combined sources
Helixi149 – 15911Combined sources
Beta strandi163 – 1653Combined sources
Helixi172 – 1765Combined sources
Beta strandi190 – 1956Combined sources
Helixi200 – 2023Combined sources
Helixi204 – 21714Combined sources
Beta strandi222 – 2276Combined sources
Helixi231 – 2388Combined sources
Helixi239 – 2446Combined sources
Beta strandi245 – 2506Combined sources
Helixi253 – 26210Combined sources
Beta strandi264 – 2685Combined sources
Helixi278 – 2869Combined sources
Beta strandi289 – 2935Combined sources
Helixi296 – 3016Combined sources
Helixi303 – 3053Combined sources
Beta strandi307 – 3115Combined sources
Helixi316 – 32813Combined sources
Helixi330 – 34314Combined sources
Helixi344 – 3474Combined sources
Helixi349 – 36315Combined sources
Beta strandi371 – 3733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GEJX-ray2.60A1-386[»]
2GEKX-ray2.40A1-386[»]
4N9WX-ray1.94A1-386[»]
4NC9X-ray3.19A/B/C/D1-386[»]
ProteinModelPortaliA0QWG6.
SMRiA0QWG6. Positions 1-373.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA0QWG6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 2022Substrate binding1 Publication
Regioni251 – 2533Substrate binding1 Publication
Regioni274 – 2785Substrate binding1 Publication

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105E2K. Bacteria.
COG0438. LUCA.
HOGENOMiHOG000077288.
KOiK08256.
OMAiIVCPYSW.
OrthoDBiEOG6WDSHM.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2GEJX-ray2.60A1-386[»]
2GEKX-ray2.40A1-386[»]
4N9WX-ray1.94A1-386[»]
4NC9X-ray3.19A/B/C/D1-386[»]
ProteinModelPortaliA0QWG6.
SMRiA0QWG6. Positions 1-373.
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.
OrthoDBiEOG6WDSHM.

Enzyme and pathway databases

UniPathwayiUPA00949.
BioCyciMSME246196:GJ4Y-2935-MONOMER.
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...

Publicationsi

« Hide 'large scale' publications
  1. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
    Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
    Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
    Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
    Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  4. "Definition of the first mannosylation step in phosphatidylinositol mannoside synthesis. PimA is essential for growth of mycobacteria."
    Kordulakova J., Gilleron M., Mikusova K., Puzo G., Brennan P.J., Gicquel B., Jackson M.
    J. Biol. Chem. 277:31335-31344(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A MANNOSYLTRANSFERASE, SUBCELLULAR LOCATION.
  5. "New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB' is an essential enzyme of Mycobacterium smegmatis."
    Guerin M.E., Kaur D., Somashekar B.S., Gibbs S., Gest P., Chatterjee D., Brennan P.J., Jackson M.
    J. Biol. Chem. 284:25687-25696(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AC1PIM2 BIOSYNTHESIS.
  6. "Molecular recognition and interfacial catalysis by the essential phosphatidylinositol mannosyltransferase PimA from mycobacteria."
    Guerin M.E., Kordulakova J., Schaeffer F., Svetlikova Z., Buschiazzo A., Giganti D., Gicquel B., Mikusova K., Jackson M., Alzari P.M.
    J. Biol. Chem. 282:20705-20714(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH GDP AND GDP-MANNOSE, MUTAGENESIS OF TYR-9; 77-ARG--LYS-81; HIS-118; THR-126; ARG-201 AND GLU-274.

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: July 6, 2016
This is version 74 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.

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.