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Reviewed, UniProtKB/Swiss-Prot P58814 (APGM_PYRFU)

Last modified November 3, 2009. Version 40. 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:
    2,3-bisphosphoglycerate-independent phosphoglycerate mutase
      Short name=Phosphoglyceromutase
      Short name=BPG-independent PGAM
      Short name=aPGAM
    EC=5.4.2.1
Gene names
Name: apgM
Ordered Locus Names: PF1959
OrganismPyrococcus furiosus [Complete proteome] [HAMAP]
Taxonomic identifier2261 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length411 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. HAMAP MF_01402

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01402

Cofactor

Magnesium Probable.

Enzyme regulation

Inhibited to approximately 20% by EDTA. HAMAP MF_01402

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP MF_01402

Subunit structure

Homotetramer Probable.

Sequence similarities

Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.0. HAMAP MF_01402

Ontologies

Keywords
   Biological processGlycolysis
   LigandMagnesium
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4114112,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP MF_01402
PRO_0000138144

Sequences

Sequence LengthMass (Da)Tools
P58814-1 [UniParc].

Last modified May 2, 2002. Version 1.
Checksum: 870587E630C2B104

FASTA41145,314
        10         20         30         40         50         60 
MKQRKGVLII LDGLGDRPIK ELGGKTPLEY ANTPTMDYLA KIGILGQQDP IKPGQPAGSD 

        70         80         90        100        110        120 
TAHLSIFGYD PYKSYRGRGY FEALGVGLEL DEDDLAFRVN FATLENGVIT DRRAGRISTE 

       130        140        150        160        170        180 
EAHELAKAIQ ENVDIPVDFI FKGATGHRAV LVLKGMAEGY KVGENDPHEA GKPPHPFTWE 

       190        200        210        220        230        240 
DEASKKVAEI LEEFVKKAHE VLDKHPINEK RRKEGKPVAN YLLIRGAGTY PNIPMKFTEQ 

       250        260        270        280        290        300 
WKVKAAAVVA VALVKGVAKA IGFDVYTPKG ATGEYNTDEM AKARKAVELL KDYDFVFIHF 

       310        320        330        340        350        360 
KPTDAAGHDN NPKLKAELIE RADRMIKYIV DHVDLEDVVI AITGDHSTPC EVMNHSGDPV 

       370        380        390        400        410 
PLLIAGGGVR ADYTEKFGER EAMRGGLGRI RGHDIVPIMM DLMNRTEKFG A 

« Hide

References

« Hide 'large scale' references
[1]"The complete sequence of the Pyrococcus furiosus genome."
Weiss R.B., Dunn D.M., Robb F.T., Brown J.R.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]"Molecular characterization of phosphoglycerate mutase in archaea."
van der Oost J., Huynen M.A., Verhees C.H.
FEMS Microbiol. Lett. 212:111-120(2002) [PubMed: 12076796] [Abstract]
Cited for: CHARACTERIZATION.
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

AE009950 Genomic DNA. Translation: AAL82083.1.
RefSeqNP_579688.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1469841.
GenomeReviewsGene locus PF1959 in contig AE009950_GR.
KEGGpfu:PF1959.
NMPDRfig|186497.1.peg.2011.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP58814.
OMAITGDHST.

Enzyme and pathway databases

BRENDA5.4.2.1. 321.

Family and domain databases

HAMAPMF_01402.
[Tree]
InterProIPR004456. APGAM_arc.
IPR019304. bisP-indep_Pglycerate_Mutase.
IPR006124. Metalloenzyme.
[Graphical view]
PfamPF01676. Metalloenzyme. 1 hit.
PF10143. PhosphMutase. 1 hit.
[Graphical view]
PIRSFPIRSF006392. IPGAM_arch. 1 hit.
ProDomPD004704. APGAM_DeoB. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00306. apgM. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAPGM_PYRFU
AccessionPrimary (citable) accession number: P58814
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 2, 2002
Last modified: November 3, 2009
This is version 40 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents