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Q5RFB8 (PGAM1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Phosphoglycerate mutase 1

EC=3.1.3.13
EC=5.4.2.11
EC=5.4.2.4
Alternative name(s):
BPG-dependent PGAM 1
Phosphoglycerate mutase isozyme B
Short name=PGAM-B
Gene names
Name:PGAM1
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity. HAMAP-Rule MF_01039

Catalytic activity

2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate. HAMAP-Rule MF_01039

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

3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate. HAMAP-Rule MF_01039

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01039

Tissue specificity

In mammalian tissues there are two types of phosphoglycerate mutase isozymes: type-M in muscles and type-B in other tissues.

Post-translational modification

Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose condition. Acetylation increases catalytic activity. Under glucose restriction SIRT1 levels dramatically increase and it deacetylates the enzyme By similarity. HAMAP-Rule MF_01039

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 254253Phosphoglycerate mutase 1 HAMAP-Rule MF_01039
PRO_0000179827

Regions

Compositional bias122 – 13110Pro-rich HAMAP-Rule MF_01039

Sites

Active site111Tele-phosphohistidine intermediate By similarity
Active site1861 By similarity
Site621Interaction with carboxyl group of phosphoglycerates By similarity

Amino acid modifications

Modified residue141Phosphoserine By similarity
Modified residue261Phosphotyrosine By similarity
Modified residue311Phosphoserine By similarity
Modified residue1061N6-acetyllysine By similarity
Modified residue2511N6-acetyllysine; alternate By similarity
Modified residue2511N6-succinyllysine; alternate By similarity
Modified residue2531N6-acetyllysine By similarity
Modified residue2541N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RFB8 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E650852BEBB23AF8

FASTA25428,778
        10         20         30         40         50         60 
MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY EFDICFTSVQ 

        70         80         90        100        110        120 
KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD 

       130        140        150        160        170        180 
VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKEGKR 

       190        200        210        220        230        240 
VLIAAHGNSL RGIVKHLEGL SEEAIMELNL PTGIPIVYEL DKNSKPIKPM QFLGDEETVR 

       250 
KAMEAVAAQG KAKK 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857242 mRNA. Translation: CAH89539.1.
RefSeqNP_001127164.1. NM_001133692.2.
UniGenePab.4825.

3D structure databases

ProteinModelPortalQ5RFB8.
SMRQ5RFB8. Positions 2-246.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5RFB8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174215.
KEGGpon:100174215.

Organism-specific databases

CTD5223.

Phylogenomic databases

HOVERGENHBG027528.
InParanoidQ5RFB8.
KOK01834.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
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]
SUPFAMSSF53254. SSF53254. 1 hit.
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGAM1_PONAB
AccessionPrimary (citable) accession number: Q5RFB8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 61 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families