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O24246 (PMGI_PRUDU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. 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-independent phosphoglycerate mutase

Short name=BPG-independent PGAM
Short name=Phosphoglyceromutase
EC=5.4.2.12
Alternative name(s):
PGAM-I
OrganismPrunus dulcis (Almond) (Amygdalus dulcis)
Taxonomic identifier3755 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeAmygdaleaePrunus

Protein attributes

Sequence length488 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

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.

Cofactor

Binds 2 manganese ions per subunit By similarity.

Pathway

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

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the BPG-independent phosphoglycerate mutase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionIsomerase
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmanganese ion binding

Inferred from electronic annotation. Source: InterPro

phosphoglycerate mutase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 488›4882,3-bisphosphoglycerate-independent phosphoglycerate mutase
PRO_0000212112

Sites

Active site101Phosphoserine intermediate By similarity
Metal binding101Manganese 2 By similarity
Metal binding3591Manganese 1 By similarity
Metal binding3631Manganese 1 By similarity
Metal binding4001Manganese 2 By similarity
Metal binding4011Manganese 2 By similarity
Metal binding4301Manganese 1 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
O24246 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: F103633B8FCD2D2A

FASTA48853,395
        10         20         30         40         50         60 
LPTEDDMGNS EVGHNALGAG RIFAQGAKLV DSALETGKLY EGEGFKYIKE SFPTNTLHLI 

        70         80         90        100        110        120 
GLLSDGGVHS RLDQLLLLVK GASERGAKRI RVHILTDGRD VLDGSSVGFA ETLENYLAQL 

       130        140        150        160        170        180 
REKGVDAQIA SGGGRMYVTM DRYENDWGVV KRGWDAQVLG EAPHKFKNAV EAIKTLRQEP 

       190        200        210        220        230        240 
NTSDQYLPPF VIVDENGKPV GPIVDGDAVV TFNFRADRMV MIAKALEYAD FDKFDRVRFP 

       250        260        270        280        290        300 
KIRYAGMLQY DGELKLPSKY LVEPPEIDRT SGEYLTYNGV RTFACSETVK FGHVTFFWNG 

       310        320        330        340        350        360 
NRSGYFNPQM EEYVEIPSDS GITFNVQPKM KAVEIAEKGR GAILSKKFEQ VRVNLPNSDM 

       370        380        390        400        410        420 
VGHTSSIEAT VVACKAADEA VKIIIDAIEQ VGGIYVVTAD HGNAEDMVKR NKKGQPLLDK 

       430        440        450        460        470        480 
NGNIQILTSH TLQPVPIAIG GPGLAPGVQF RKDVPNGGLA NVAATVMNLH GFEAPADYET 


TLIEVVDN 

« Hide

References

[1]"2,3-Bisphosphoglycerate-independent phosphoglycerate mutase is conserved among different phylogenic kingdoms."
Grana X., Perez de la Ossa P., Broceno C., Stocker M., Garriga J., Puigdomenech P., Climent F.
Comp. Biochem. Physiol. 112B:287-293(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Texas.
Tissue: Root.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75020 mRNA. Translation: CAA52928.1.
PIRT09138.

3D structure databases

ProteinModelPortalO24246.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEO24246.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00109; UER00186.

Family and domain databases

Gene3D3.40.1450.10. 1 hit.
3.40.720.10. 2 hits.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR011258. BPG-indep_PGM_N.
IPR006124. Metalloenzyme.
IPR005995. Pgm_bpd_ind.
[Graphical view]
PfamPF06415. iPGM_N. 1 hit.
PF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFPIRSF001492. IPGAM. 1 hit.
SUPFAMSSF53649. SSF53649. 2 hits.
SSF64158. SSF64158. 1 hit.
ProtoNetSearch...

Entry information

Entry namePMGI_PRUDU
AccessionPrimary (citable) accession number: O24246
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways