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Q7SIB7

- PGK1_PIG

UniProt

Q7SIB7 - PGK1_PIG

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Protein

Phosphoglycerate kinase 1

Gene

PGK1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
Complete GO annotation...

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.
InParanoidiQ7SIB7.
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

« Hide

        10         20         30         40         50
MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAIPSIKFC
60 70 80 90 100
LDNGAKSVVL MSHLGRPDGI PMPDKYSLEP VAVELKSLPG KDVLFLKDCV
110 120 130 140 150
GPEVEKACAD PAAGSVILLE NLRFHVEEEG KGKDASGSKV KADPAKIEAF
160 170 180 190 200
RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPKKAGGFLM KKELNYFAKA
210 220 230 240 250
LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN
260 270 280 290 300
MEIGTSLFDE EGSKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKIGQ
310 320 330 340 350
ATVASGIPAG WMGLDCGPES SKKYSEAVAR AKQIVWNGPV GVFEWEAFAQ
360 370 380 390 400
GTKALMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL
410
ELLEGKVLPG VDALSNV
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.
InParanoidi Q7SIB7.
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 29, 2014
This is version 76 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