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Q7SIB7 (PGK1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglycerate kinase 1

EC=2.7.2.3
Gene names
Name:PGK1
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. HAMAP-Rule MF_00145

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. HAMAP-Rule MF_00145

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00145.

Sequence similarities

Belongs to the phosphoglycerate kinase family.

Sequence caution

The sequence described in Ref.3 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.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphoglycerate kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 417416Phosphoglycerate kinase 1 HAMAP-Rule MF_00145
PRO_0000145837

Regions

Nucleotide binding373 – 3764ATP HAMAP-Rule MF_00145
Region24 – 263Substrate binding HAMAP-Rule MF_00145
Region63 – 664Substrate binding HAMAP-Rule MF_00145

Sites

Binding site391Substrate
Binding site1231Substrate
Binding site1711Substrate
Binding site2201ATP
Binding site3131ATP; via carbonyl oxygen
Binding site3441ATP

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue61N6-succinyllysine By similarity
Modified residue111N6-acetyllysine By similarity
Modified residue481N6-acetyllysine; alternate By similarity
Modified residue481N6-succinyllysine; alternate By similarity
Modified residue751N6-acetyllysine By similarity
Modified residue761Phosphotyrosine By similarity
Modified residue861N6-acetyllysine By similarity
Modified residue911N6-acetyllysine By similarity
Modified residue971N6-acetyllysine By similarity
Modified residue1311N6-acetyllysine; alternate By similarity
Modified residue1311N6-malonyllysine; alternate By similarity
Modified residue1461N6-acetyllysine By similarity
Modified residue1911N6-succinyllysine By similarity
Modified residue1961Phosphotyrosine By similarity
Modified residue1991N6-acetyllysine By similarity
Modified residue2031Phosphoserine By similarity
Modified residue2671N6-acetyllysine By similarity
Modified residue2911N6-acetyllysine By similarity
Modified residue3611N6-acetyllysine By similarity

Secondary structure

..................................................................................... 417
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7SIB7 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B014E769058C1135

FASTA41744,559
        10         20         30         40         50         60 
MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAIPSIKFC LDNGAKSVVL 

        70         80         90        100        110        120 
MSHLGRPDGI PMPDKYSLEP VAVELKSLPG KDVLFLKDCV GPEVEKACAD PAAGSVILLE 

       130        140        150        160        170        180 
NLRFHVEEEG KGKDASGSKV KADPAKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN 

       190        200        210        220        230        240 
LPKKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM 

       250        260        270        280        290        300 
AFTFLKVLNN MEIGTSLFDE EGSKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKIGQ 

       310        320        330        340        350        360 
ATVASGIPAG WMGLDCGPES SKKYSEAVAR AKQIVWNGPV GVFEWEAFAQ GTKALMDEVV 

       370        380        390        400        410 
KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNV 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY677198 mRNA. Translation: AAT77773.1.
RefSeqNP_001093402.1. NM_001099932.1.
UniGeneSsc.23800.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HDIX-ray1.80A5-417[»]
1KF0X-ray2.50A2-417[»]
1VJCX-ray2.10A2-417[»]
1VJDX-ray1.90A2-417[»]
ProteinModelPortalQ7SIB7.
SMRQ7SIB7. Positions 2-417.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ7SIB7.
PRIDEQ7SIB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID407608.
KEGGssc:407608.

Organism-specific databases

CTD5230.

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
HOVERGENHBG008177.
KOK00927.

Enzyme and pathway databases

SABIO-RKQ7SIB7.
UniPathwayUPA00109; UER00185.

Family and domain databases

Gene3D3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPMF_00145. Phosphoglyc_kinase.
InterProIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERPTHR11406. PTHR11406. 1 hit.
PfamPF00162. PGK. 1 hit.
[Graphical view]
PIRSFPIRSF000724. Pgk. 1 hit.
PRINTSPR00477. PHGLYCKINASE.
SUPFAMSSF53748. SSF53748. 1 hit.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ7SIB7.

Entry information

Entry namePGK1_PIG
AccessionPrimary (citable) accession number: Q7SIB7
Secondary accession number(s): Q6B6L7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 73 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways