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Reviewed, UniProtKB/Swiss-Prot Q9PI71 (GPMI_CAMJE)

Last modified June 16, 2009. Version 54. 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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    2,3-bisphosphoglycerate-independent phosphoglycerate mutase
      Short name=Phosphoglyceromutase
      Short name=BPG-independent PGAM
      Short name=iPGM
    EC=5.4.2.1
Gene names
Name: gpmI
Synonyms: pgm
Ordered Locus Names: Cj0434
OrganismCampylobacter jejuni [Complete proteome] [HAMAP]
Taxonomic identifier197 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 2 manganese ions per subunit By similarity.

Pathway

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

Subunit structure

Monomer By similarity.

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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular function2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

flaGQ0PAW91EBI-1194767,EBI-1191365

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4924922,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP MF_01038
PRO_0000212133

Sites

Active site611Phosphoserine intermediate By similarity
Metal binding111Manganese 2 By similarity
Metal binding611Manganese 2 By similarity
Metal binding3861Manganese 1 By similarity
Metal binding3901Manganese 1 By similarity
Metal binding4271Manganese 2 By similarity
Metal binding4281Manganese 2 By similarity
Metal binding4451Manganese 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PI71-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3A8DA60AD0D4C1BC

FASTA49255,721
        10         20         30         40         50         60 
MKQKCVLIIT DGIGYNKNSK FNAFEAAKKP SYEKLFKEVP NSLLKTSGLA VGLPEGQMGN 

        70         80         90        100        110        120 
SEVGHMCIGS GRIIYQNLVR INKAIENKEL EKNENLKKLL AKCKRVHIIG LYSDGGVHSM 

       130        140        150        160        170        180 
DTHFKAMLEI CAKNGNEVFA HAITDGRDVS PKSGLNFIKD LKEFCENLGV HFATLCGRFY 

       190        200        210        220        230        240 
AMDRDKRWDR VKEYYECLLG KAYKVPNLLE YLQKSYDENV TDEFIKAAQN ENYKGMREED 

       250        260        270        280        290        300 
GIIFINFRND RMKQLVEVLN SKDFKEFERE KIFENLLTMS VYDDKFKLPV LFEKEKIENT 

       310        320        330        340        350        360 
LAQVISKAGL SQLHTAETEK YAHVTFFFNG GKEELLENET RVLIPSPKVK TYDEKPQMSA 

       370        380        390        400        410        420 
FEVCDAVKKG IEKGEDFIVV NFANGDMVGH TGDFNATIKA VEAVDTCLGE ILECAKKHDY 

       430        440        450        460        470        480 
AFIITSDHGN CEAMQDEKGN LLTNHTTFDV FVFVQARGVS KIKDNMGLSN IAASVLKILD 

       490 
LEIPKEMNEA LF 

« Hide

References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed: 10688204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases

AL111168 Genomic DNA. Translation: CAL34584.1.
PIRH81387.
RefSeqYP_002343871.1.

3D structure databases

HSSPHSSP built from PDB template 1O98 based on UniProtKB Q9X519.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9PI71. 35 interactions.

Genome annotation databases

GeneID904759.
GenomeReviewsGene locus Cj0434 in contig AL111168_GR.
KEGGcje:Cj0434.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAQ9PI71. DHGNAEL.

Enzyme and pathway databases

BioCycCJEJ192222:CJ0434-MON.
BRENDA5.4.2.1. 255835.

Family and domain databases

HAMAPMF_01038.
[Tree]
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR011258. BPG-indep_PGM_N.
IPR006124. Metalloenzyme.
IPR005995. Pgm_bpd_ind.
[Graphical view]
Gene3DG3DSA:3.40.720.10. Alk_phosphtse. 1 hit.
G3DSA:3.40.1450.10. BPG-indep_PGM_N. 1 hit.
PfamPF06415. iPGM_N. 1 hit.
PF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFPIRSF001492. IPGAM. 1 hit.
ProDomPD004704. APGAM_DeoB. 1 hit.
PD004429. Pgm_bpd_ind. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01307. pgm_bpd_ind. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGPMI_CAMJE
AccessionPrimary (citable) accession number: Q9PI71
Secondary accession number(s): Q0PB76
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 54 of the entry and version 1 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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents