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Reviewed, UniProtKB/Swiss-Prot A3MWR8 (APGM_PYRCJ)

Last modified November 3, 2009. Version 21. 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: Pcal_1668
OrganismPyrobaculum calidifontis (strain JCM 11548 / VA1) [Complete proteome] [HAMAP]
Taxonomic identifier410359 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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_01402

Pathway

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

Sequence similarities

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

Ontologies

Keywords
   Biological processGlycolysis
   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

metal ion binding

Inferred from electronic annotation. Source: InterPro

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_1000087369

Sequences

Sequence LengthMass (Da)Tools
A3MWR8-1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: EB97F9F82983C0E8

FASTA41143,940
        10         20         30         40         50         60 
MPSVLWILFD GGGDRPNGGK TPFHVAFKPT IDYLTSLGSC GLLDPISPGV RPGSDTAHLA 

        70         80         90        100        110        120 
LFGYDPYKYY TGRGAFEALG AGIELRPGDV AFRTNLATVD SSGVVIDRRA GRYIAPEETR 

       130        140        150        160        170        180 
AVEEVMAKIG DEVAKRYGVE VVYKSTVEHR GVLVLRGPVS HKVSDTDPHK VGMPVAKAAP 

       190        200        210        220        230        240 
LGNDREAALT AEVVNYITAR FTEAAGGLEI NKARAASGRP PINAILLRGG GYMPAIEPVA 

       250        260        270        280        290        300 
EKYRVKAAAI AGVALIRGVA KAVGMDVYTA QGLGGTKDDV FDHAVKLAVE LMGKYDVVFL 

       310        320        330        340        350        360 
HVKGTDSTSH DGDFQGKVAV IERLDKALAP YLDHLLKNYF IVTSDHATPV SIREHTGEPV 

       370        380        390        400        410 
PLTLYGPDVV PDDVAKFSEL TCWRGALGRL RGIDIMPILA SYLGLSEKFG E 

« Hide

References

[1]"Complete sequence of Pyrobaculum calidifontis JCM 11548."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000561 Genomic DNA. Translation: ABO09085.1.
RefSeqYP_001056551.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA3MWR8.

Genome annotation databases

GeneID4909890.
GenomeReviewsGene locus Pcal_1668 in contig CP000561_GR.
KEGGpcl:Pcal_1668.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAITGDHST.

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_PYRCJ
AccessionPrimary (citable) accession number: A3MWR8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 3, 2007
Last modified: November 3, 2009
This is version 21 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