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Reviewed, UniProtKB/Swiss-Prot Q0A915 (GPMA_ALHEH)

Last modified February 9, 2010. Version 28. 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-dependent phosphoglycerate mutase
      Short name=Phosphoglyceromutase
      Short name=PGAM
      Short name=BPG-dependent PGAM
      Short name=dPGM
    EC=5.4.2.1
Gene names
Name: gpmA
Ordered Locus Names: Mlg_1323
OrganismAlkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeAlkalilimnicola

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. HAMAP MF_01039

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01039

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP MF_01039

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Ontologies

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

Inferred from electronic annotation. Source: HAMAP

   Molecular function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2322322,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP MF_01039
PRO_1000064026

Sites

Active site91Tele-phosphohistidine intermediate By similarity
Active site1821 By similarity
Site601Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0A915-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 648BEFD0EC0AD8C3

FASTA23226,825
        10         20         30         40         50         60 
MKKLVLLRHG QSIWNQENRF TGWHDVDLTE KGREEAQAAG QLMKRHGLRF DYAYTSVLKR 

        70         80         90        100        110        120 
AIRTLWIGLD ELDQMWIPVT KAWQLNERHY GALTGLNKAE TAEEYGAEQV HIWRRSYDTP 

       130        140        150        160        170        180 
PPPLDETSPY HPRHDPRYAS LKPEQLPATE SLALTLERVL PYWNERIVPT LRDCDNVLIA 

       190        200        210        220        230 
AHGNSIRALI KHLDGLDDEA IMKVEIATGD PLVYELDDAL AVVDKHYLRE RD 

« Hide

References

[1]"Complete sequence of Alkalilimnicola ehrilichei MLHE-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000453 Genomic DNA. Translation: ABI56672.1.
RefSeqYP_742162.1.

3D structure databases

SMRQ0A915. Positions 1-232.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0A915.

Genome annotation databases

GeneID4268662.
GenomeReviewsGene locus Mlg_1323 in contig CP000453_GR.
KEGGaeh:Mlg_1323.
NMPDRfig|187272.6.peg.1269.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHBG658938.
OMAVPLTECL.
PhylomeDBQ0A915.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
[Tree]
InterProIPR001345. PG/BPGM_mutase_AS.
IPR013078. PG_mutase.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. Phosphogly_mut1. 1 hit.
PfamPF00300. PGAM. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGPMA_ALHEH
AccessionPrimary (citable) accession number: Q0A915
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 17, 2006
Last modified: February 9, 2010
This is version 28 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