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P00559

- PGK1_HORSE

UniProt

P00559 - PGK1_HORSE

Protein

Phosphoglycerate kinase 1

Gene

PGK1

Organism
Equus caballus (Horse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei39 – 391SubstrateBy similarity
    Binding sitei123 – 1231SubstrateBy similarity
    Binding sitei171 – 1711SubstrateBy similarity
    Binding sitei220 – 2201ATPBy similarity
    Binding sitei313 – 3131ATP; via carbonyl oxygenBy similarity
    Binding sitei344 – 3441ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. phosphoglycerate kinase activity Source: UniProtKB

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-UniPathway
    2. phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKP00559.
    UniPathwayiUPA00109; UER00185.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglycerate kinase 1 (EC:2.7.2.3)
    Gene namesi
    Name:PGK1
    Synonyms:PGK
    OrganismiEquus caballus (Horse)
    Taxonomic identifieri9796 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
    ProteomesiUP000002281: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 417416Phosphoglycerate kinase 1PRO_0000145829Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine
    Modified residuei6 – 61N6-succinyllysineBy similarity
    Modified residuei11 – 111N6-acetyllysineBy similarity
    Modified residuei48 – 481N6-acetyllysine; alternateBy similarity
    Modified residuei48 – 481N6-succinyllysine; alternateBy similarity
    Modified residuei75 – 751N6-acetyllysineBy similarity
    Modified residuei76 – 761PhosphotyrosineBy similarity
    Modified residuei86 – 861N6-acetyllysineBy similarity
    Modified residuei91 – 911N6-acetyllysineBy similarity
    Modified residuei97 – 971N6-acetyllysineBy similarity
    Modified residuei131 – 1311N6-acetyllysine; alternateBy similarity
    Modified residuei131 – 1311N6-malonyllysine; alternateBy similarity
    Modified residuei146 – 1461N6-acetyllysineBy similarity
    Modified residuei191 – 1911N6-succinyllysineBy similarity
    Modified residuei196 – 1961PhosphotyrosineBy similarity
    Modified residuei199 – 1991N6-acetyllysineBy similarity
    Modified residuei203 – 2031PhosphoserineBy similarity
    Modified residuei267 – 2671N6-acetyllysineBy similarity
    Modified residuei291 – 2911N6-acetyllysineBy similarity
    Modified residuei361 – 3611N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiP00559.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi9796.ENSECAP00000012929.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PGKX-ray3.00A-[»]
    ProteinModelPortaliP00559.
    SMRiP00559. Positions 2-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00559.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 186185Globular domain-1Add
    BLAST
    Regioni24 – 263Substrate bindingBy similarity
    Regioni63 – 664Substrate bindingBy similarity
    Regioni187 – 1904Linker
    Regioni191 – 417227Globular domain-2Add
    BLAST
    Regioni406 – 41712Associated with globular domain 1Add
    BLAST

    Sequence similaritiesi

    Belongs to the phosphoglycerate kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0126.
    HOGENOMiHOG000227107.
    HOVERGENiHBG008177.
    InParanoidiP00559.

    Family and domain databases

    Gene3Di3.40.50.1260. 1 hit.
    3.40.50.1270. 1 hit.
    HAMAPiMF_00145. Phosphoglyc_kinase.
    InterProiIPR001576. Phosphoglycerate_kinase.
    IPR015901. Phosphoglycerate_kinase_C.
    IPR015911. Phosphoglycerate_kinase_CS.
    IPR015824. Phosphoglycerate_kinase_N.
    [Graphical view]
    PANTHERiPTHR11406. PTHR11406. 1 hit.
    PfamiPF00162. PGK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000724. Pgk. 1 hit.
    PRINTSiPR00477. PHGLYCKINASE.
    SUPFAMiSSF53748. SSF53748. 1 hit.
    PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00559-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLSNKLTLD KLNVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC    50
    LDNGAKSVVL MSHLGRPDVG PMPDKYSLQP VAVELKSLLG KDVLFLKDCV 100
    GPEVEKACAD PAAGSVILLE NLRFHVEEEG KGKDASGNKV KAEPAKIETF 150
    RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAGGFLM KKELNYFAKA 200
    LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN 250
    MEIGTSLFDE EGAKIVKNLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ 300
    ATVASGIPAG WMGLDCGTES SKKYAEAVAR AKQIVWNGPV GVFEWEAFAR 350
    GTKALMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL 400
    ELLEGKVLPG VDALSNV 417
    Length:417
    Mass (Da):44,603
    Last modified:January 23, 2007 - v2
    Checksum:i5110E246AF96931A
    GO

    Sequence databases

    PIRiA92292. KIHOG.

    Cross-referencesi

    Sequence databases

    PIRi A92292. KIHOG.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PGK X-ray 3.00 A - [» ]
    ProteinModelPortali P00559.
    SMRi P00559. Positions 2-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9796.ENSECAP00000012929.

    Proteomic databases

    PRIDEi P00559.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0126.
    HOGENOMi HOG000227107.
    HOVERGENi HBG008177.
    InParanoidi P00559.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00185 .
    SABIO-RK P00559.

    Miscellaneous databases

    EvolutionaryTracei P00559.

    Family and domain databases

    Gene3Di 3.40.50.1260. 1 hit.
    3.40.50.1270. 1 hit.
    HAMAPi MF_00145. Phosphoglyc_kinase.
    InterProi IPR001576. Phosphoglycerate_kinase.
    IPR015901. Phosphoglycerate_kinase_C.
    IPR015911. Phosphoglycerate_kinase_CS.
    IPR015824. Phosphoglycerate_kinase_N.
    [Graphical view ]
    PANTHERi PTHR11406. PTHR11406. 1 hit.
    Pfami PF00162. PGK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000724. Pgk. 1 hit.
    PRINTSi PR00477. PHGLYCKINASE.
    SUPFAMi SSF53748. SSF53748. 1 hit.
    PROSITEi PS00111. PGLYCERATE_KINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of 3-phosphoglycerate kinase from horse muscle. II. Amino acid sequence of cyanogen bromide peptides CB1-CB4 and CB6-CB14, sequence of methionine-containing regions, and complete sequence of the enzyme."
      Merrett M.
      J. Biol. Chem. 256:10293-10305(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-417.
      Tissue: Muscle.
    2. "Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme."
      Banks R.D., Blake C.C.F., Evans P.R., Haser R., Rice D.W., Hardy G.W., Merrett M., Phillips A.W.
      Nature 279:773-777(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
      Tissue: Muscle.

    Entry informationi

    Entry nameiPGK1_HORSE
    AccessioniPrimary (citable) accession number: P00559
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 101 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3