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Entry version 90 (08 May 2019)
Sequence version 1 (09 Jan 2007)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

Was identified as a high-confidence drug target.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei9GDP-mannose1 Publication1
Binding sitei16GDP-mannose; via amide nitrogen2 Publications1
Binding sitei18Phosphatidyl-myo-inositol1 Publication1
Binding sitei68Phosphatidyl-myo-inositol1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei118Important for catalytic activity1 Publication1
Binding sitei196GDP-mannose1 Publication1 Publication1
Binding sitei256GDP-mannose2 Publications1
Binding sitei282GDP-mannose2 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processLipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism, Virulence
LigandMagnesium

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
GCF_000015005:MSMEG_2935-MONOMER
MSME246196:G1H7P-2940-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.57 3512

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00949

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT4 Glycosyltransferase Family 4

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Phosphatidyl-myo-inositol mannosyltransferase1 Publication (EC:2.4.1.3452 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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:pimA1 Publication
Ordered Locus Names:MSMEG_2935, MSMEI_2861
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri246196 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycolicibacterium
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000006158 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003937321 – 386Phosphatidyl-myo-inositol mannosyltransferaseAdd BLAST386

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
A0QWG6

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
246196.MSMEI_2861

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1386
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
A0QWG6

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
A0QWG6

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni62 – 63Phosphatidyl-myo-inositol binding1 Publication2
Regioni201 – 202GDP-mannose binding1 Publication1 Publication2
Regioni251 – 253GDP-mannose binding2 Publications3
Regioni274 – 278GDP-mannose binding1 Publication5

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105E2K Bacteria
COG0438 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000077288

KEGG Orthology (KO)

More...
KOi
K08256

Identification of Orthologs from Complete Genome Data

More...
OMAi
YCAPNLG

Database of Orthologous Groups

More...
OrthoDBi
948440at2

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR028098 Glyco_trans_4-like_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13439 Glyco_transf_4, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1A5A6B5A2E36BC2E
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CP000480 Genomic DNA Translation: ABK72422.1
CP001663 Genomic DNA Translation: AFP39325.1

NCBI Reference Sequences

More...
RefSeqi
WP_011728703.1, NZ_SIJM01000002.1
YP_887254.1, NC_008596.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABK72422; ABK72422; MSMEG_2935
AFP39325; AFP39325; MSMEI_2861

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4536758

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
msb:LJ00_14605
msg:MSMEI_2861
msm:MSMEG_2935

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|246196.19.peg.2898

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_SIJM01000002.1
YP_887254.1, NC_008596.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
SMRiA0QWG6
ModBaseiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEI_2861

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
PATRICifig|246196.19.peg.2898

Phylogenomic databases

eggNOGiENOG4105E2K Bacteria
COG0438 LUCA
HOGENOMiHOG000077288
KOiK08256
OMAiYCAPNLG
OrthoDBi948440at2

Enzyme and pathway databases

UniPathwayiUPA00949
BioCyciGCF_000015005:MSMEG_2935-MONOMER
MSME246196:G1H7P-2940-MONOMER
BRENDAi2.4.1.57 3512

Miscellaneous databases

EvolutionaryTraceiA0QWG6

Family and domain databases

InterProiView protein in InterPro
IPR028098 Glyco_trans_4-like_N
PfamiView protein in Pfam
PF13439 Glyco_transf_4, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPIMA_MYCS2
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: A0QWG6
Secondary accession number(s): I7FCT3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: January 9, 2007
Last modified: May 8, 2019
This is version 90 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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
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