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Reviewed, UniProtKB/Swiss-Prot Q8NUV4 (PGCA_STAAW)

Last modified September 1, 2009. Version 36. 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: MW2411
OrganismStaphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]
Taxonomic identifier196620 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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_0000308344

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
Q8NUV4-1 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: C358457147BEBFB6

FASTA55262,428
        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 
LQSLNFNQFN LVEAQCKPDP NFSSVQSANP EDHRAFDQAV ELANKSHADL LISTDPDADR 

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

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

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

       490        500        510        520        530        540 
IEDYLTSEVY HLDKDTTSQI NSPKSNVIRV LFDEGFIALR PSGTEPKIKL YVSLKCRNFD 

       550 
DVAQKINAMI FS 

« Hide

References

[1]"Genome and virulence determinants of high virulence community-acquired MRSA."
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.
Lancet 359:1819-1827(2002) [PubMed: 12044378] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

BA000033 Genomic DNA. Translation: BAB96276.1. Different initiation.
RefSeqNP_647228.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ8NUV4.

Genome annotation databases

GeneID1004547.
GenomeReviewsGene locus MW2411 in contig BA000033_GR.
KEGGsam:MW2411.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8NUV4.

Enzyme and pathway databases

BioCycSAUR196620:MW2411-MON.

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.
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.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PRINTSPR00509. PGMPMM.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGCA_STAAW
AccessionPrimary (citable) accession number: Q8NUV4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 23, 2007
Last modified: September 1, 2009
This is version 36 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