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Q5RFB8

- PGAM1_PONAB

UniProt

Q5RFB8 - PGAM1_PONAB

Protein

Phosphoglycerate mutase 1

Gene

PGAM1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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 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

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    MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY    50
    EFDICFTSVQ KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK 100
    AETAAKHGEA QVKIWRRSYD VPPPPMEPDH PFYSNISKDR RYADLTEDQL 150
    PSCESLKDTI ARALPFWNEE IVPQIKEGKR VLIAAHGNSL RGIVKHLEGL 200
    SEEAIMELNL PTGIPIVYEL DKNSKPIKPM QFLGDEETVR KAMEAVAAQG 250
    KAKK 254
    Length:254
    Mass (Da):28,778
    Last modified:January 23, 2007 - v3
    Checksum:iE650852BEBB23AF8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR857242 mRNA. Translation: CAH89539.1 .
    RefSeqi NP_001127164.1. NM_001133692.2.
    UniGenei Pab.4825.

    3D structure databases

    ProteinModelPortali Q5RFB8.
    SMRi Q5RFB8. Positions 2-246.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5RFB8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100174215.
    KEGGi pon:100174215.

    Organism-specific databases

    CTDi 5223.

    Phylogenomic databases

    HOVERGENi HBG027528.
    InParanoidi Q5RFB8.
    KOi K01834.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    HAMAPi MF_01039. PGAM_GpmA.
    InterProi IPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR001345. PG/BPGM_mutase_AS.
    IPR005952. Phosphogly_mut1.
    [Graphical view ]
    PANTHERi PTHR11931. PTHR11931. 1 hit.
    Pfami PF00300. His_Phos_1. 1 hit.
    [Graphical view ]
    SMARTi SM00855. PGAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53254. SSF53254. 1 hit.
    TIGRFAMsi TIGR01258. pgm_1. 1 hit.
    PROSITEi PS00175. PG_MUTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 62 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