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Reviewed, UniProtKB/Swiss-Prot Q99RE2 (PGCA_STAAM)

Last modified January 19, 2010. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoglucomutase
      Short name=PGM
    EC=5.4.2.2
Alternative name(s):
    Alpha-phosphoglucomutase
    Glucose phosphomutase
Gene names
Name: pgcA
Ordered Locus Names: SAV2491
OrganismStaphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]
Taxonomic identifier158878 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the interconversion between glucose-6-phosphate and alpha-glucose-1-phosphate. This is the first step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in the S.aureus membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA) By similarity.

Catalytic activity

Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.

Sequence similarities

Belongs to the phosphohexose mutase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglucomutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 552552Phosphoglucomutase
PRO_0000308340

Sites

Active site1431Phosphoserine intermediate By similarity
Metal binding1431Magnesium; via phosphate group By similarity
Metal binding2951Magnesium By similarity
Metal binding2971Magnesium By similarity
Metal binding2991Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q99RE2-1 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: 37A8F8FFA0EF6976

FASTA55262,359
        10         20         30         40         50         60 
MKGCLATMDK ELWIERANDS LVKHFYEQQS DIEQREGFES KLTFGTAGIR GKFGLGEGRL 

        70         80         90        100        110        120 
NKFTIEKLAL GLARYLNAQT NSPTIVIHYD IRHLSTEFAQ IIANVLANHQ ITVYLPDTYK 

       130        140        150        160        170        180 
TTPELSFAVR NLNTTAGIMI TASHNPKDYN GIKVYGSDGA QLSTDASELA SRYIEEVGDP 

       190        200        210        220        230        240 
LQIDIPISKQ NTSYIKPFPK SVTDDYMKHI QNMIGYIPKS DLQVVFTSLH GTSVPIVPEL 

       250        260        270        280        290        300 
LKSLNFNQFN LVDAQCKPDP NFSSVQSANP EDHRAFDQAV ELANKSHADL LISTDPDADR 

       310        320        330        340        350        360 
LGIAERDAHG HITYFNGNQI GALLLNYRIQ QTSQLRHRLM IQSIVSSELT KSLARYNNVK 

       370        380        390        400        410        420 
YKEVLTGFKF IAQEIRQLDD HQNMIFAFEE SYGFLSEPFV RDKDAVQIVP LIIKYASELK 

       430        440        450        460        470        480 
LYGKTLKDEL EQIYQTVGRH EDTLFSHTLE GLEGKKKIES IMTHFRSNPP QEIQGLKVKA 

       490        500        510        520        530        540 
IEDYLTSEVY HLDKDTTSQI NSSKSNVIRV LFDEGFIALR PSGTEPKIKL YVSLKCPDFD 

       550 
DVAQKINAMI FS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000017 Genomic DNA. Translation: BAB58653.1. Different initiation.
RefSeqNP_373015.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ99RE2.

2-D gel databases

World-2DPAGE0002:Q99RE2.

Genome annotation databases

GeneID1122516.
GenomeReviewsGene locus SAV2491 in contig BA000017_GR.
KEGGsav:SAV2491.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG571743.

Enzyme and pathway databases

BioCycSAUR158878:SAV2491-MONOMER.

Family and domain databases

InterProIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. A-D-PHexomutase_N.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PfamPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PRINTSPR00509. PGMPMM.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGCA_STAAM
AccessionPrimary (citable) accession number: Q99RE2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 23, 2007
Last modified: January 19, 2010
This is version 43 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents