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Protein

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

Gene

pimB

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 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 (PIM2). Can also add a mannose residue to the position 2 of a phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol mannoside (PIM1) or to the position 6 of a monoacyl phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (AcPIM1) to generate a mononacyl phosphatidyl-myo-inositol dimannoside (AcPIM2).1 Publication

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 sitei14 – 141Substrate; via amide nitrogen
Sitei114 – 1141Important for catalytic activityBy similarity
Binding sitei200 – 2001SubstrateBy similarity
Binding sitei257 – 2571SubstrateBy similarity
Binding sitei261 – 2611SubstrateBy similarity
Sitei286 – 2861Important for catalytic activityBy similarity
Binding sitei294 – 2941SubstrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  • glycolipid biosynthetic process Source: UniProtKB
  • mannosylation Source: GOC
  • pathogenesis Source: UniProtKB-KW
  • phosphatidylinositol metabolic process Source: UniProtKB-UniPathway
  • 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-4253-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-(1-6)-phosphatidylinositol monomannoside mannosyltransferase (EC:2.4.1.57)
Alternative name(s):
Alpha-D-mannose-alpha-(1-6)-phosphatidylmyo-inositol-mannosyltransferase
Alpha-mannosyltransferase
Short name:
Alpha-ManT
Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase
Phosphatidylinositol alpha-mannosyltransferase
Short name:
PI alpha-mannosyltransferase
Gene namesi
Name:pimB
Ordered Locus Names:MSMEG_4253, MSMEI_4154
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000006158 Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferasePRO_0000393735Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi246196.MSMEG_4253.

Structurei

3D structure databases

ProteinModelPortaliA0R043.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni204 – 2052Substrate bindingBy similarity
Regioni286 – 2905Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105JNK. Bacteria.
COG0438. LUCA.
HOGENOMiHOG000077286.
KOiK13668.
OMAiYAMSDIF.
OrthoDBiEOG68DD0W.

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.

A0R043-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLVTNDFPP RRGGIQSYLE AFVGELVRTH ELTVYAPKWK GAEEYDEKAA
60 70 80 90 100
RSGYRVVRHP TTLMLPEPTV ASRMKRLIGE HDIETVWFGA AAPLALLGPL
110 120 130 140 150
ARRAGARRIV ASTHGHEVGW SMLPVARTAL RRIGNDADVV TFVSRYTRSR
160 170 180 190 200
FASAFGPSAA LEHLPPGVDT DRFAPDPDAR ARMRERYGLG DRPVVVCLSR
210 220 230 240 250
LVPRKGQDML IRALPELRRR VPDTALAIVG GGPYLETLQR MASDLGVAEH
260 270 280 290 300
VVFTRGIPAE ELPAHHAMAD VFAMPCRTRG AGLDVEGLGI VYLEASACGV
310 320 330 340 350
PVVAGRSGGA PETVLDGKTG TVVDGTDVDA ITTAVGDLLA DPRRAAAMGV
360 370 380
AGRHWALDNW QWRTRGARLA ELLSGRREAR QA
Length:382
Mass (Da):41,407
Last modified:January 9, 2007 - v1
Checksum:i938A199444B1BA4D
GO

Sequence cautioni

The sequence AFP40611.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK74170.1.
CP001663 Genomic DNA. Translation: AFP40611.1. Different initiation.
RefSeqiWP_011729679.1. NC_008596.1.
YP_888531.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK74170; ABK74170; MSMEG_4253.
AFP40611; AFP40611; MSMEI_4154.
GeneIDi4536134.
KEGGimsg:MSMEI_4154.
msm:MSMEG_4253.
PATRICi18080865. VBIMycSme59918_4174.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK74170.1.
CP001663 Genomic DNA. Translation: AFP40611.1. Different initiation.
RefSeqiWP_011729679.1. NC_008596.1.
YP_888531.1. NC_008596.1.

3D structure databases

ProteinModelPortaliA0R043.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_4253.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK74170; ABK74170; MSMEG_4253.
AFP40611; AFP40611; MSMEI_4154.
GeneIDi4536134.
KEGGimsg:MSMEI_4154.
msm:MSMEG_4253.
PATRICi18080865. VBIMycSme59918_4174.

Phylogenomic databases

eggNOGiENOG4105JNK. Bacteria.
COG0438. LUCA.
HOGENOMiHOG000077286.
KOiK13668.
OMAiYAMSDIF.
OrthoDBiEOG68DD0W.

Enzyme and pathway databases

UniPathwayiUPA00949.
BioCyciMSME246196:GJ4Y-4253-MONOMER.
BRENDAi2.4.1.57. 3512.

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...

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. "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, SUBSTRATE SPECIFICITY.

Entry informationi

Entry nameiPIMB_MYCS2
AccessioniPrimary (citable) accession number: A0R043
Secondary accession number(s): I7GBP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: January 9, 2007
Last modified: April 13, 2016
This is version 68 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.