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Reviewed, UniProtKB/Swiss-Prot Q2Y9Z7 (GPMA2_NITMU)

Last modified November 3, 2009. Version 23. 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: Nmul_A1121
OrganismNitrosospira multiformis (strain ATCC 25196 / NCIMB 11849) [Complete proteome] [HAMAP]
Taxonomic identifier323848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosospira

Protein attributes

Sequence length251 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 – 2512512,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2 HAMAP MF_01039
PRO_0000229132

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q2Y9Z7-1 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: F50D2CD7F99244BB

FASTA25128,814
        10         20         30         40         50         60 
MKKLVLLRHG ESTWNKENRF TGWTDVDLTP KGAEEAHNSG RLLREAGFTF DIAYTSVLKR 

        70         80         90        100        110        120 
AIRTLWIVLD EMDQMWIPVE SSWRLNERHY GALQGLNKLE TAVAYGEEQV LIWRRSYDIR 

       130        140        150        160        170        180 
PPALTPDDPR YPGCDPRYRN LPKQDIPLTE CLQDTVSRFL PYWRESIAPQ VKSDKSVLIT 

       190        200        210        220        230        240 
AHGNSLRALV MYLDNLSEGE IMELNIPTGI PLVYELDDGL KPIRSYYLGD QAKIEQAMQV 

       250 
VANQGKILPN L 

« Hide

References

[1]"Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC 25196."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000103 Genomic DNA. Translation: ABB74424.1.
RefSeqYP_411816.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ2Y9Z7.

Genome annotation databases

GeneID3785701.
GenomeReviewsGene locus Nmul_A1121 in contig CP000103_GR.
KEGGnmu:Nmul_A1121.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2Y9Z7.
OMAFMLWRRS.

Enzyme and pathway databases

BioCycNMUL323848:NMUL_A1121-MON.

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_NITMU
AccessionPrimary (citable) accession number: Q2Y9Z7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: December 20, 2005
Last modified: November 3, 2009
This is version 23 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