Phosphoglycerate kinase 1 - Sus scrofa (Pig)

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Names and origin

Protein names

Recommended name:
Phosphoglycerate kinase 1
EC=2.7.2.3

Gene names

Name:

PGK1

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the phosphoglycerate kinase family.
Sequence caution	The sequence described in Ref.3 differs from that shown. Reason: Miscellaneous discrepancy. The sequence shown in PDB entry 1KF0 is a tentative sequence based on the electron density. It differs from that shown in 14 positions.

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Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB phosphoglycerate kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed

Chain

2 – 417

416

Phosphoglycerate kinase 1

PRO_0000145837

Regions

Nucleotide binding

373 – 376

4

ATP

Region

24 – 26

3

Substrate binding

Region

63 – 66

4

Substrate binding

Sites

Binding site

39

1

Substrate

Binding site

123

1

Substrate

Binding site

171

1

Substrate

Binding site

220

1

ATP

Binding site

313

1

ATP; via carbonyl oxygen

Binding site

344

1

ATP

Amino acid modifications

Modified residue

11

1

N6-acetyllysine By similarity

Modified residue

30

1

N6-acetyllysine By similarity

Modified residue

48

1

N6-acetyllysine By similarity

Modified residue

75

1

N6-acetyllysine By similarity

Modified residue

76

1

Phosphotyrosine By similarity

Modified residue

86

1

N6-acetyllysine By similarity

Modified residue

97

1

N6-acetyllysine By similarity

Modified residue

131

1

N6-acetyllysine By similarity

Modified residue

136

1

Phosphoserine By similarity

Modified residue

146

1

N6-acetyllysine By similarity

Modified residue

196

1

Phosphotyrosine By similarity

Modified residue

199

1

N6-acetyllysine By similarity

Modified residue

203

1

Phosphoserine By similarity

Modified residue

243

1

Phosphothreonine By similarity

Modified residue

267

1

N6-acetyllysine By similarity

Modified residue

291

1

N6-acetyllysine By similarity

Modified residue

323

1

N6-acetyllysine By similarity

Modified residue

390

1

Phosphoserine By similarity

Modified residue

406

1

N6-acetyllysine By similarity

Secondary structure

1

.

417

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q7SIB7-1 [UniParc].

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

417

44,559

        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

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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: 11178909] [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: 12102622] [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: 15035615] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ATP.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY677198 mRNA. Translation: AAT77773.1.

RefSeq

NP_001093402.1.

UniGene

Ssc.23800

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSSSCT00000013604; ENSSSCP00000013238; ENSSSCG00000012440; Sus scrofa. [Genome view]

GeneID

407608.

KEGG

ssc:407608.

Organism-specific databases

CTD

407608.

Phylogenomic databases

HOVERGEN

Q7SIB7.

Enzyme and pathway databases

BRENDA

2.7.2.3. 249.

Family and domain databases

InterPro

IPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]

Gene3D

G3DSA:3.40.50.1270. Phosphoglycerate_kinase_C. 1 hit.
G3DSA:3.40.50.1260. Phosphoglycerate_kinase_N. 1 hit.

PANTHER

PTHR11406. PGK. 1 hit.

Pfam

PF00162. PGK. 1 hit.
[Graphical view]

PRINTS

PR00477. PHGLYCKINASE.

PROSITE

PS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

PGK1_PIG

Accession

Primary (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:	November 24, 2009
This is version 47 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families