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Q7SIB7

- PGK1_PIG

UniProt

Q7SIB7 - PGK1_PIG

Protein

Phosphoglycerate kinase 1

Gene

PGK1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 3 (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 – 391Substrate1 Publication
    Binding sitei123 – 1231Substrate1 Publication
    Binding sitei171 – 1711Substrate1 Publication
    Binding sitei220 – 2201ATP1 Publication
    Binding sitei313 – 3131ATP; via carbonyl oxygen1 Publication
    Binding sitei344 – 3441ATP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi373 – 3764ATP1 Publication

    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-RKQ7SIB7.
    UniPathwayiUPA00109; UER00185.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglycerate kinase 1 (EC:2.7.2.3)
    Gene namesi
    Name:PGK1
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: 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 – 11RemovedBy similarity
    Chaini2 – 417416Phosphoglycerate kinase 1PRO_0000145837Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    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

    PaxDbiQ7SIB7.
    PRIDEiQ7SIB7.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Structurei

    Secondary structure

    1
    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 53
    Helixi9 – 113
    Beta strandi18 – 225
    Beta strandi29 – 357
    Helixi38 – 5215
    Beta strandi56 – 616
    Turni73 – 753
    Helixi79 – 8911
    Beta strandi93 – 953
    Beta strandi99 – 1013
    Helixi102 – 1098
    Beta strandi115 – 1184
    Helixi122 – 1243
    Turni126 – 1305
    Beta strandi131 – 1333
    Beta strandi139 – 1413
    Helixi144 – 15613
    Beta strandi159 – 1635
    Helixi166 – 1683
    Helixi174 – 1774
    Beta strandi184 – 1863
    Helixi188 – 20114
    Beta strandi206 – 2127
    Helixi218 – 2203
    Helixi221 – 2288
    Beta strandi232 – 2365
    Helixi238 – 2403
    Helixi241 – 2499
    Helixi262 – 2643
    Helixi266 – 27611
    Beta strandi279 – 2813
    Beta strandi285 – 2939
    Beta strandi298 – 3025
    Turni303 – 3053
    Beta strandi312 – 3165
    Helixi318 – 33013
    Beta strandi332 – 3387
    Helixi346 – 3483
    Helixi350 – 36415
    Beta strandi368 – 3714
    Helixi375 – 3828
    Turni386 – 3883
    Beta strandi389 – 3924
    Helixi396 – 4038
    Helixi409 – 4124

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HDIX-ray1.80A5-417[»]
    1KF0X-ray2.50A2-417[»]
    1VJCX-ray2.10A2-417[»]
    1VJDX-ray1.90A2-417[»]
    ProteinModelPortaliQ7SIB7.
    SMRiQ7SIB7. Positions 2-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7SIB7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni24 – 263Substrate binding
    Regioni63 – 664Substrate binding

    Sequence similaritiesi

    Belongs to the phosphoglycerate kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0126.
    HOGENOMiHOG000227107.
    HOVERGENiHBG008177.
    KOiK00927.

    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.

    Q7SIB7-1 [UniParc]FASTAAdd to Basket

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    MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAIPSIKFC    50
    LDNGAKSVVL MSHLGRPDGI PMPDKYSLEP VAVELKSLPG KDVLFLKDCV 100
    GPEVEKACAD PAAGSVILLE NLRFHVEEEG KGKDASGSKV KADPAKIEAF 150
    RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPKKAGGFLM KKELNYFAKA 200
    LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN 250
    MEIGTSLFDE EGSKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKIGQ 300
    ATVASGIPAG WMGLDCGPES SKKYSEAVAR AKQIVWNGPV GVFEWEAFAQ 350
    GTKALMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL 400
    ELLEGKVLPG VDALSNV 417
    Length:417
    Mass (Da):44,559
    Last modified:January 23, 2007 - v3
    Checksum:iB014E769058C1135
    GO

    Sequence cautioni

    The sequence described in 1 Publication differs from that shown. Reason: The sequence shown in PDB entry 1KF0 is a tentative sequence based on the electron density. It differs from that shown in 14 positions.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY677198 mRNA. Translation: AAT77773.1.
    RefSeqiNP_001093402.1. NM_001099932.1.
    UniGeneiSsc.23800.

    Genome annotation databases

    GeneIDi407608.
    KEGGissc:407608.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY677198 mRNA. Translation: AAT77773.1 .
    RefSeqi NP_001093402.1. NM_001099932.1.
    UniGenei Ssc.23800.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HDI X-ray 1.80 A 5-417 [» ]
    1KF0 X-ray 2.50 A 2-417 [» ]
    1VJC X-ray 2.10 A 2-417 [» ]
    1VJD X-ray 1.90 A 2-417 [» ]
    ProteinModelPortali Q7SIB7.
    SMRi Q7SIB7. Positions 2-417.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi Q7SIB7.
    PRIDEi Q7SIB7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 407608.
    KEGGi ssc:407608.

    Organism-specific databases

    CTDi 5230.

    Phylogenomic databases

    eggNOGi COG0126.
    HOGENOMi HOG000227107.
    HOVERGENi HBG008177.
    KOi K00927.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00185 .
    SABIO-RK Q7SIB7.

    Miscellaneous databases

    EvolutionaryTracei Q7SIB7.

    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. "Molecular cloning and characterization of porcine PGK1."
      Xu D.Q., Xiong Y.Z.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Skeletal muscle.
    2. "A 1.8 A resolution structure of pig muscle 3-phosphoglycerate kinase with bound MgADP and 3-phosphoglycerate in open conformation: new insight into the role of the nucleotide in domain closure."
      Szilagyi A.N., Ghosh M., Garman E., Vas M.
      J. Mol. Biol. 306:499-511(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 5-417 IN COMPLEX WITH SUBSTRATE AND AMP.
    3. "Crystallographic and thiol-reactivity studies on the complex of pig muscle phosphoglycerate kinase with ATP analogues: correlation between nucleotide binding mode and helix flexibility."
      Kovari Z., Flachner B., Naray-Szabo G., Vas M.
      Biochemistry 41:8796-8806(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    4. "Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP."
      Flachner B., Kovari Z., Varga A., Gugolya Z., Vonderviszt F., Naray-Szabo G., Vas M.
      Biochemistry 43:3436-3449(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ATP.

    Entry informationi

    Entry nameiPGK1_PIG
    AccessioniPrimary (citable) accession number: Q7SIB7
    Secondary accession number(s): Q6B6L7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 75 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

    3D-structure, Complete proteome, 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