Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q49W02 (GPMI_STAS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2,3-bisphosphoglycerate-independent phosphoglycerate mutase

Short name=BPG-independent PGAM
Short name=Phosphoglyceromutase
Short name=iPGM
EC=5.4.2.12
Gene names
Name:gpmI
Ordered Locus Names:SSP1913
OrganismStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) [Complete proteome] [HAMAP]
Taxonomic identifier342451 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. HAMAP-Rule MF_01038

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01038

Cofactor

Binds 2 manganese ions per subunit By similarity. HAMAP-Rule MF_01038

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01038

Subunit structure

Monomer By similarity. HAMAP-Rule MF_01038

Sequence similarities

Belongs to the BPG-independent phosphoglycerate mutase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandManganese
Metal-binding
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular_function2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5055052,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP-Rule MF_01038
PRO_0000212216

Sites

Active site621Phosphoserine intermediate By similarity
Metal binding121Manganese 2 By similarity
Metal binding621Manganese 2 By similarity
Metal binding3971Manganese 1 By similarity
Metal binding4011Manganese 1 By similarity
Metal binding4381Manganese 2 By similarity
Metal binding4391Manganese 2 By similarity
Metal binding4561Manganese 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q49W02 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 11E64347EBC3B1AD

FASTA50556,343
        10         20         30         40         50         60 
MAKQPTALII LDGFANRESE HGNAVKLANK PNFDRYYSKY PTTQIEASGL DVGLPEGQMG 

        70         80         90        100        110        120 
NSEVGHMNIG AGRVVYQSLT RINKSIEDGD FFENDVLNNA INHVKKNDSV LHVFGLLSDG 

       130        140        150        160        170        180 
GVHSHYKHLF ALLDLAKKQG LEKVYVHAFL DGRDVDQKSA LKYIEETEAK FKELGIGQFA 

       190        200        210        220        230        240 
SVSGRYYAMD RDKRWDREEK AYNAIRNFGG TTFESAKAGV EANYDKDLTD EFVEPFIVQD 

       250        260        270        280        290        300 
QNEGVNDGDA VIFYNFRPDR AGQLSEIFTD KAFEGFKVEQ INDLFYATFT KYNDNVNAEI 

       310        320        330        340        350        360 
VFEKVDLTNT IGEVAQDNGL KQLRIAETEK FPHVTYFMSG GRNEEFEGER RRLIDSPKVA 

       370        380        390        400        410        420 
TYDLKPEMSA YEVKDALIEE LNKGDLDLIL LNFANPDMVG HSGMLEPTIK AIEAVDECLG 

       430        440        450        460        470        480 
EVVDKITEMG GHAIITADHG NSDMVLTDDD QPMTTHTTNP VPVIVTKDGV TLRETGRLGD 

       490        500 
LAPTLLDLLN VDQPEDMTGE SLINH 

« Hide

References

[1]"Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection."
Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.
Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15305 / DSM 20229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008934 Genomic DNA. Translation: BAE19058.1.
RefSeqYP_302003.1. NC_007350.1.

3D structure databases

ProteinModelPortalQ49W02.
SMRQ49W02. Positions 2-503.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342451.SSP1913.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE19058; BAE19058; SSP1913.
GeneID3615267.
KEGGssp:SSP1913.
PATRIC19625407. VBIStaSap90642_1907.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0696.
HOGENOMHOG000223664.
KOK15633.
OMAGVHSHIE.
OrthoDBEOG6HJ22X.
ProtClustDBPRK05434.

Enzyme and pathway databases

BioCycSSAP342451:GKFA-1976-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

Gene3D3.40.1450.10. 1 hit.
3.40.720.10. 2 hits.
HAMAPMF_01038. GpmI.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR011258. BPG-indep_PGM_N.
IPR006124. Metalloenzyme.
IPR005995. Pgm_bpd_ind.
[Graphical view]
PfamPF06415. iPGM_N. 1 hit.
PF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFPIRSF001492. IPGAM. 1 hit.
SUPFAMSSF53649. SSF53649. 2 hits.
SSF64158. SSF64158. 1 hit.
TIGRFAMsTIGR01307. pgm_bpd_ind. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGPMI_STAS1
AccessionPrimary (citable) accession number: Q49W02
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways