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Q2Y9Z7 (GPMA2_NITMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2

Short name=BPG-dependent PGAM 2
Short name=PGAM 2
Short name=Phosphoglyceromutase 2
Short name=dPGM 2
EC=5.4.2.11
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.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

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

   Molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2512512,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2 HAMAP-Rule MF_01039
PRO_0000229132

Regions

Region21 – 2222-phospho-D-glycerate binding By similarity
Region87 – 9042-phospho-D-glycerate binding By similarity
Region114 – 11522-phospho-D-glycerate binding By similarity

Sites

Active site91Tele-phosphohistidine intermediate By similarity
Active site1821 By similarity
Binding site1512-phospho-D-glycerate By similarity
Binding site6012-phospho-D-glycerate By similarity
Binding site9812-phospho-D-glycerate By similarity
Binding site18412-phospho-D-glycerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2Y9Z7 [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].
Strain: ATCC 25196 / NCIMB 11849.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000103 Genomic DNA. Translation: ABB74424.1.
RefSeqYP_411816.1. NC_007614.1.

3D structure databases

ProteinModelPortalQ2Y9Z7.
SMRQ2Y9Z7. Positions 3-234.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323848.Nmul_A1121.

Proteomic databases

PRIDEQ2Y9Z7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB74424; ABB74424; Nmul_A1121.
GeneID3785701.
KEGGnmu:Nmul_A1121.
PATRIC22725470. VBINitMul110821_1303.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.
OrthoDBEOG6C8N1H.
ProtClustDBPRK14115.

Enzyme and pathway databases

BioCycNMUL323848:GKEC-1145-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. PTHR11931. 1 hit.
PfamPF00300. His_Phos_1. 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 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: February 19, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways