Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoglycerate kinase

Gene

PGK

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Pathwayi: glycolysis

This protein is involved in step 2 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (KLLA0_F09141g), Glyceraldehyde-3-phosphate dehydrogenase 1 (GAP1), Glyceraldehyde-3-phosphate dehydrogenase 2 (GAP2)
  2. Phosphoglycerate kinase (PGK)
  3. Phosphoglycerate mutase (KLLA0_E11859g), Phosphoglycerate mutase (KLLA0_C04081g)
  4. Enolase (ENO)
  5. Pyruvate kinase (PYK1)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei39SubstrateBy similarity1
Binding sitei122SubstrateBy similarity1
Binding sitei169SubstrateBy similarity1
Binding sitei218ATPBy similarity1
Binding sitei311ATP; via carbonyl oxygenBy similarity1
Binding sitei342ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi371 – 374ATPBy similarity4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00109; UER00185.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate kinase (EC:2.7.2.3)
Gene namesi
Name:PGK
Ordered Locus Names:KLLA0A11011g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
Proteomesi
  • UP000000598 Componenti: Chromosome A

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001458821 – 416Phosphoglycerate kinaseAdd BLAST416

Proteomic databases

PRIDEiP14828.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi284590.XP_451479.1.

Structurei

3D structure databases

ProteinModelPortaliP14828.
SMRiP14828.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni24 – 26Substrate bindingBy similarity3
Regioni63 – 66Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the phosphoglycerate kinase family.Curated

Phylogenomic databases

eggNOGiKOG1367. Eukaryota.
COG0126. LUCA.
HOGENOMiHOG000227107.
InParanoidiP14828.
KOiK00927.
OMAiFPVDYVT.
OrthoDBiEOG092C2GKC.

Family and domain databases

CDDicd00318. Phosphoglycerate_kinase. 1 hit.
Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase. 1 hit.
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.

P14828-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSSKLTVK DLDVTGKRVF IRVDFNVPLD GKKITSNQRI VAALPTIQYV
60 70 80 90 100
LEKKPKAIVL ASHLGRPNGE VNDKYSLAPV ADELSRLLQK PVTFLHDCVG
110 120 130 140 150
EEVTNAVNNA KDGEVFLLEN LRFHIEEEGS RKVDGNKVKA DKAAVTKFRE
160 170 180 190 200
QLSSLADVYV NDAFGTAHRA HSSIVGFDLP NRAAGFLLSK ELQYFAKALE
210 220 230 240 250
NPTRPFLAIL GGAKVADKIQ LIDNLLDKVD SLIIGGGMAF TFKKVLENTE
260 270 280 290 300
IGDSIYDAAG AELVPKLVEK AKKNNVKIVL PTDFVIGDKF SADANTKVVT
310 320 330 340 350
DKEGIPSGWQ GLDNGPESRK AFAATVAEAK TIVWNGPPGV FEFAPFAKGT
360 370 380 390 400
EALLDAVVAS SQAGNTVIIG GGDTATVAKK YGVVDKISHV STGGGASLEL
410
LEGKELPGVT FLSNKQ
Length:416
Mass (Da):44,514
Last modified:September 27, 2004 - v2
Checksum:i9CFF5724C67AB850
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti366T → N in CAA35646 (PubMed:2326170).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17654 Genomic DNA. Translation: CAA35646.1.
CR382121 Genomic DNA. Translation: CAH03067.1.
PIRiS07878. KIVKGL.
RefSeqiXP_451479.1. XM_451479.1.

Genome annotation databases

EnsemblFungiiCAH03067; CAH03067; KLLA0_A11011g.
GeneIDi2896489.
KEGGikla:KLLA0A11011g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17654 Genomic DNA. Translation: CAA35646.1.
CR382121 Genomic DNA. Translation: CAH03067.1.
PIRiS07878. KIVKGL.
RefSeqiXP_451479.1. XM_451479.1.

3D structure databases

ProteinModelPortaliP14828.
SMRiP14828.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi284590.XP_451479.1.

Proteomic databases

PRIDEiP14828.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAH03067; CAH03067; KLLA0_A11011g.
GeneIDi2896489.
KEGGikla:KLLA0A11011g.

Phylogenomic databases

eggNOGiKOG1367. Eukaryota.
COG0126. LUCA.
HOGENOMiHOG000227107.
InParanoidiP14828.
KOiK00927.
OMAiFPVDYVT.
OrthoDBiEOG092C2GKC.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00185.

Family and domain databases

CDDicd00318. Phosphoglycerate_kinase. 1 hit.
Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiPGK_KLULA
AccessioniPrimary (citable) accession number: P14828
Secondary accession number(s): Q6CX60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: September 27, 2004
Last modified: November 2, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.