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P56196 (GPMI_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
Synonyms:pgm
Ordered Locus Names:HP_0974
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length491 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 term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglucose catabolic process

Inferred from electronic annotation. Source: InterPro

glycolytic process

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 – 4914912,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP-Rule MF_01038
PRO_0000212154

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

Secondary structure

.................................................................................. 491
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56196 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: F72F8CDA04EA9D6D

FASTA49154,788
        10         20         30         40         50         60 
MAQKTLLIIT DGIGYRKDSD HNAFFHAKKP TYDLMFKTLP YSLIDTHGLS VGLPKGQMGN 

        70         80         90        100        110        120 
SEVGHMCIGA GRVLYQDLVK ISLSLQNDEL KNNPAFLNTI QKSPVVHLMG LMSDGGVHSH 

       130        140        150        160        170        180 
IEHFIALALE CEKSHKKVCL HLITDGRDVA PKSALTYLKQ MQNICNESIQ IATISGRFYA 

       190        200        210        220        230        240 
MDRDKRFERI ELAYHSLMGL NHTPLSPSEY IQSQYDKNIT DEFIMPACFK NYCGMQDDES 

       250        260        270        280        290        300 
FIFINFRNDR AREIVSALGQ KQFSGFKRQV FKKLHIATMT PYDNTFPYPV LFPKESVQNT 

       310        320        330        340        350        360 
LAEVVSQHNL TQSHIAETEK YAHVTFFING GVETPFKNEN RVLIQSPKVT TYDLKPEMSA 

       370        380        390        400        410        420 
KEVTLAVLEQ MKLGTDLIIV NFANGDMVGH TGNFEASVKA VEAVDACLGE ILSLAKKLDY 

       430        440        450        460        470        480 
AMLLTSDHGN CERMKDENQN PLTNHTAGSV YCFVLGDGVK SIKNGALNNI ASSVLKLMGL 

       490 
KAPATMDEPL F 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000511 Genomic DNA. Translation: AAD08020.1.
PIRF64641.
RefSeqNP_207765.1. NC_000915.1.
YP_006934888.1. NC_018939.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LNOmodel-A3-491[»]
ProteinModelPortalP56196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-3166N.
IntActP56196. 1 interaction.
MINTMINT-172669.
STRING85962.HP0974.

Proteomic databases

PRIDEP56196.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD08020; AAD08020; HP_0974.
GeneID899506.
KEGGheo:C694_05010.
hpy:HP0974.
PATRIC20593263. VBIHelPyl33062_1013.

Phylogenomic databases

eggNOGCOG0696.
KOK15633.
OMAGMVEYSS.
OrthoDBEOG6HJ22X.

Enzyme and pathway databases

BioCycHPY:HP0974-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_HELPY
AccessionPrimary (citable) accession number: P56196
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 103 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names