Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoglycerate mutase 1

Gene

PGAM1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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.

Catalytic activityi

2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate.
2-phospho-D-glycerate = 3-phospho-D-glycerate.
3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111Tele-phosphohistidine intermediateBy similarity
Sitei62 – 621Interaction with carboxyl group of phosphoglyceratesBy similarity
Active sitei186 – 1861By similarity

GO - Molecular functioni

  1. bisphosphoglycerate 2-phosphatase activity Source: UniProtKB-EC
  2. bisphosphoglycerate mutase activity Source: UniProtKB-EC
  3. phosphoglycerate mutase activity Source: InterPro

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Isomerase

Keywords - Biological processi

Glycolysis

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PGAM1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 254253Phosphoglycerate mutase 1PRO_0000179827Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141PhosphoserineBy similarity
Modified residuei23 – 231PhosphoserineBy similarity
Modified residuei26 – 261PhosphotyrosineBy similarity
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei106 – 1061N6-acetyllysineBy similarity
Modified residuei251 – 2511N6-acetyllysine; alternateBy similarity
Modified residuei251 – 2511N6-succinyllysine; alternateBy similarity
Modified residuei253 – 2531N6-acetyllysineBy similarity
Modified residuei254 – 2541N6-acetyllysineBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ5RFB8.

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5RFB8.
SMRiQ5RFB8. Positions 2-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi122 – 13110Pro-rich

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG027528.
InParanoidiQ5RFB8.
KOiK01834.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5RFB8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY
60 70 80 90 100
EFDICFTSVQ KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK
110 120 130 140 150
AETAAKHGEA QVKIWRRSYD VPPPPMEPDH PFYSNISKDR RYADLTEDQL
160 170 180 190 200
PSCESLKDTI ARALPFWNEE IVPQIKEGKR VLIAAHGNSL RGIVKHLEGL
210 220 230 240 250
SEEAIMELNL PTGIPIVYEL DKNSKPIKPM QFLGDEETVR KAMEAVAAQG

KAKK
Length:254
Mass (Da):28,778
Last modified:January 23, 2007 - v3
Checksum:iE650852BEBB23AF8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857242 mRNA. Translation: CAH89539.1.
RefSeqiNP_001127164.1. NM_001133692.2.
UniGeneiPab.4825.

Genome annotation databases

GeneIDi100174215.
KEGGipon:100174215.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857242 mRNA. Translation: CAH89539.1.
RefSeqiNP_001127164.1. NM_001133692.2.
UniGeneiPab.4825.

3D structure databases

ProteinModelPortaliQ5RFB8.
SMRiQ5RFB8. Positions 2-246.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ5RFB8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100174215.
KEGGipon:100174215.

Organism-specific databases

CTDi5223.

Phylogenomic databases

HOVERGENiHBG027528.
InParanoidiQ5RFB8.
KOiK01834.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiPGAM1_PONAB
AccessioniPrimary (citable) accession number: Q5RFB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 64 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.