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Reviewed, UniProtKB/Swiss-Prot Q82TU0 (GPMA2_NITEU)

Last modified November 3, 2009. Version 34. 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 2
      Short name=Phosphoglyceromutase 2
      Short name=PGAM 2
      Short name=BPG-dependent PGAM 2
      Short name=dPGM 2
    EC=5.4.2.1
Gene names
Name: gpmA2
Ordered Locus Names: NE1780
OrganismNitrosomonas europaea [Complete proteome] [HAMAP]
Taxonomic identifier915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length249 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_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 – 2492492,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2 HAMAP MF_01039
PRO_0000179898

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q82TU0-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 1DB802FA9D9CA557

FASTA24928,317
        10         20         30         40         50         60 
MKKLVLLRHG ESIWNQENRF TGWTDVDLTP KGLKEAEEAG RLLRENGFSF DIAYTSLLKR 

        70         80         90        100        110        120 
AIRTLWIALD EMDQMWTPIE LNWRLNERHY GALQGLNKAE TAKQYGDEQV LVWRRSYDIR 

       130        140        150        160        170        180 
PPSITINDER YPGFDLRYRN MSSGDIPLAE SLKDTVARFL PYWNQSIAPQ IKAEKKVIIA 

       190        200        210        220        230        240 
AHGNSLRALI KHLDNISDQD ILNCNIPTGI PLVYELDDDL KPLNSYYLGD AGQIGEAISA 


VANQGKSGA 

« Hide

References

[1]"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea."
Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.
J. Bacteriol. 185:2759-2773(2003) [PubMed: 12700255] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19718 / IFO 14298.

Cross-references

Sequence databases

AL954747 Genomic DNA. Translation: CAD85691.1.
RefSeqNP_841810.1.

3D structure databases

HSSPHSSP built from PDB template 1E58 based on UniProtKB P31217.
ModBaseSearch...

Genome annotation databases

GeneID1082734.
GenomeReviewsGene locus NE1780 in contig AL954747_GR.
KEGGneu:NE1780.
NMPDRfig|228410.1.peg.1709.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ82TU0.
OMAFMLWRRS.

Enzyme and pathway databases

BioCycNEUR228410:NE1780-MON.
BRENDA5.4.2.1. 444.

Family and domain databases

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

Entry information

Entry nameGPMA2_NITEU
AccessionPrimary (citable) accession number: Q82TU0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 34 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