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Protein

GDP-mannose-dependent monoacylated alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase

Gene

pimB

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
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) (PubMed:18421567, PubMed:18178556, PubMed:19395496). Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 6 of a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1) to generate phosphatidyl-myo-inositol bearing alpha-1,2- and alpha-1,6-linked mannose residues (Ac1PIM2) (PubMed:18178556, PubMed:19395496). PimB also catalyzes the addition of a mannosyl residue from GDP-Man to the position 6 of phosphatidyl-myo-inositol bearing an acylated alpha-1,2-linked mannose residue (Ac1PIM1) to generate monoacylated phosphatidyl-myo-inositol bearing alpha-1,2- and alpha-1,6-linked mannose residues (Ac1PIM2) (By similarity). The addition of the second mannosyl residue by PimB preferentially occurs before the acylation of the mannosyl residue transferred by PimA (By similarity). Also able to transfer a mannosyl residue from GDP-Man to the position 6 of a phosphatidyl-myo-inositol (PI), but this reaction is very slow (By similarity).By similarity3 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.1 Publication

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 sitei206GDP-mannose1 Publication1
Binding sitei211GDP-mannose1 Publication1
Binding sitei261GDP-mannose; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei298GDP-mannose1 Publication1

GO - Molecular functioni

  • glycolipid 6-alpha-mannosyltransferase activity Source: UniProtKB
  • phosphatidylinositol alpha-mannosyltransferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciCORYNE:G18NG-11778-MONOMER.
UniPathwayiUPA00949.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-mannose-dependent monoacylated alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase1 Publication (EC:2.4.1.571 Publication)
Alternative name(s):
Alpha-D-mannose-alpha-(1-6)-phosphatidylmyo-inositol-mannosyltransferase1 Publication
Alpha-mannosyltransferase1 Publication
Short name:
Alpha-ManT1 Publication
Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase1 Publication
Phosphatidylinositol alpha-mannosyltransferase1 Publication
Short name:
PI alpha-mannosyltransferase1 Publication
Gene namesi
Name:pimB1 Publication
Ordered Locus Names:Cgl2186, cg2400
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000000582 Componenti: Chromosome

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are unable to produce monoacylated phosphatidyl-myo-inositol dimannoside (Ac1PIM2) resulting in the accumulation of Ac1PIM1, the absence of LAM and LM-A, and the presence of LM-B.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi290E → D: Reduces mannosyltransferase activity by more than 95%, and weakens but do not abrogate binding of GDP-mannose. 1 Publication1
Mutagenesisi291G → S: Reduces mannosyltransferase activity by more than 95%. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003937341 – 381GDP-mannose-dependent monoacylated alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferaseAdd BLAST381

Interactioni

Protein-protein interaction databases

STRINGi196627.cg2400.

Structurei

Secondary structure

1381
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 12Combined sources6
Helixi20 – 29Combined sources10
Helixi34 – 36Combined sources3
Beta strandi37 – 42Combined sources6
Helixi46 – 53Combined sources8
Beta strandi57 – 67Combined sources11
Helixi72 – 84Combined sources13
Beta strandi88 – 94Combined sources7
Helixi98 – 101Combined sources4
Helixi102 – 107Combined sources6
Beta strandi111 – 116Combined sources6
Helixi121 – 124Combined sources4
Helixi128 – 140Combined sources13
Beta strandi142 – 147Combined sources6
Helixi149 – 159Combined sources11
Beta strandi161 – 167Combined sources7
Turni174 – 176Combined sources3
Helixi182 – 191Combined sources10
Beta strandi200 – 205Combined sources6
Helixi209 – 211Combined sources3
Helixi213 – 226Combined sources14
Beta strandi231 – 235Combined sources5
Helixi241 – 247Combined sources7
Helixi249 – 254Combined sources6
Beta strandi255 – 260Combined sources6
Helixi263 – 272Combined sources10
Beta strandi274 – 278Combined sources5
Helixi284 – 286Combined sources3
Helixi294 – 301Combined sources8
Beta strandi306 – 308Combined sources3
Helixi314 – 317Combined sources4
Turni320 – 322Combined sources3
Beta strandi323 – 325Combined sources3
Helixi331 – 342Combined sources12
Helixi345 – 362Combined sources18
Helixi365 – 377Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OKAX-ray2.20A/B1-381[»]
3OKCX-ray2.40A1-381[»]
3OKPX-ray2.00A1-381[»]
ProteinModelPortaliQ8NNK8.
SMRiQ8NNK8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NNK8.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105JNK. Bacteria.
COG0438. LUCA.
HOGENOMiHOG000077286.
KOiK13668.
OMAiRSDHVTA.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
IPR028098. Glyco_trans_4-like_N.
[Graphical view]
PfamiPF13439. Glyco_transf_4. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8NNK8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASRKTLVV TNDFPPRIGG IQSYLRDFIA TQDPESIVVF ASTQNAEEAH
60 70 80 90 100
AYDKTLDYEV IRWPRSVMLP TPTTAHAMAE IIREREIDNV WFGAAAPLAL
110 120 130 140 150
MAGTAKQAGA SKVIASTHGH EVGWSMLPGS RQSLRKIGTE VDVLTYISQY
160 170 180 190 200
TLRRFKSAFG SHPTFEHLPS GVDVKRFTPA TPEDKSATRK KLGFTDTTPV
210 220 230 240 250
IACNSRLVPR KGQDSLIKAM PQVIAARPDA QLLIVGSGRY ESTLRRLATD
260 270 280 290 300
VSQNVKFLGR LEYQDMINTL AAADIFAMPA RTRGGGLDVE GLGIVYLEAQ
310 320 330 340 350
ACGVPVIAGT SGGAPETVTP ATGLVVEGSD VDKLSELLIE LLDDPIRRAA
360 370 380
MGAAGRAHVE AEWSWEIMGE RLTNILQSEP R
Length:381
Mass (Da):41,328
Last modified:October 1, 2002 - v1
Checksum:i99AECD1E156444DF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000036 Genomic DNA. Translation: BAB99579.1.
BX927154 Genomic DNA. Translation: CAF20527.1.
RefSeqiNP_601390.1. NC_003450.3.
WP_011014943.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB99579; BAB99579; BAB99579.
CAF20527; CAF20527; cg2400.
GeneIDi1020138.
KEGGicgb:cg2400.
cgl:NCgl2106.
PATRICi21496374. VBICorGlu203724_2123.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000036 Genomic DNA. Translation: BAB99579.1.
BX927154 Genomic DNA. Translation: CAF20527.1.
RefSeqiNP_601390.1. NC_003450.3.
WP_011014943.1. NC_006958.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OKAX-ray2.20A/B1-381[»]
3OKCX-ray2.40A1-381[»]
3OKPX-ray2.00A1-381[»]
ProteinModelPortaliQ8NNK8.
SMRiQ8NNK8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg2400.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB99579; BAB99579; BAB99579.
CAF20527; CAF20527; cg2400.
GeneIDi1020138.
KEGGicgb:cg2400.
cgl:NCgl2106.
PATRICi21496374. VBICorGlu203724_2123.

Phylogenomic databases

eggNOGiENOG4105JNK. Bacteria.
COG0438. LUCA.
HOGENOMiHOG000077286.
KOiK13668.
OMAiRSDHVTA.

Enzyme and pathway databases

UniPathwayiUPA00949.
BioCyciCORYNE:G18NG-11778-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ8NNK8.
PROiQ8NNK8.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
IPR028098. Glyco_trans_4-like_N.
[Graphical view]
PfamiPF13439. Glyco_transf_4. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPIMB_CORGL
AccessioniPrimary (citable) accession number: Q8NNK8
Secondary accession number(s): Q6M3P7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

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.