Q9GPM4 (PGK_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglycerate kinase
EC=2.7.2.3

Gene names

Name:	pgkA
ORF Names:	DDB_G0287595

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. UniProtKB P00558
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. UniProtKB P00558
Subunit structure	Monomer. Interacts with calmodulin in the presence of Ca2+. Ref.1 UniProtKB P00558
Subcellular location	Cytoplasm By similarity UniProtKB P00558.
Developmental stage	Expressed during development. Expression levels decrease steadily from the initiation of development until culmination. Levels increase after 18 hours of development and peak at 22 hours, after which they decrease again. Ref.3 Ref.4
Sequence similarities	Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from sequence or structural similarity Ref.1. Source: dictyBase glycolysis Inferred from sequence or structural similarity Ref.1. Source: dictyBase
Cellular_component	phagocytic vesicle Inferred from direct assay Ref.5PubMed 19482547. Source: dictyBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin binding Inferred from direct assay Ref.1. Source: dictyBase phosphoglycerate kinase activity Inferred from sequence or structural similarity Ref.1. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 420	420	Phosphoglycerate kinase		PRO_0000293630
Regions
	Nucleotide binding	376 – 379	4	ATP By similarity UniProtKB P00558
	Region	27 – 29	3	Substrate binding By similarity UniProtKB P00558
	Region	67 – 70	4	Substrate binding By similarity UniProtKB P00558
	Region	209 – 228	20	Calmodulin binding Ref.1
Sites
	Binding site	43	1	Substrate By similarity UniProtKB P00558
	Binding site	126	1	Substrate By similarity UniProtKB P00558
	Binding site	174	1	Substrate By similarity UniProtKB P00558
	Binding site	223	1	ATP By similarity UniProtKB P00558
	Binding site	316	1	ATP; via carbonyl oxygen By similarity UniProtKB P00558
	Binding site	347	1	ATP By similarity UniProtKB P00558
Amino acid modifications
	Modified residue	199	1	Phosphotyrosine By similarity UniProtKB P00558
	Modified residue	206	1	Phosphoserine By similarity UniProtKB P00558 UniProtKB P09411
	Modified residue	393	1	Phosphoserine By similarity UniProtKB P09411

Sequences

	Sequence		Length	Mass (Da)
	Q9GPM4 [UniParc]. Last modified October 1, 2002. Version 2. Checksum: 6FEA000CF9B5F83E	FASTA	420	45,709
	10 20 30 40 50 60 MSSNKIGNKL SLDKVDVKGK RVLIRVDYNV PLDKNNNITS TQRIDASIPT LEYCLKNGAK 70 80 90 100 110 120 SIVLMSHLGR PDGLVKPEYS LKPVVKVLED QLKRPIKFLS DCVGEQVEKE CANPEEGTVI 130 140 150 160 170 180 LLENLRFHIE EEGSGVDAEG KKVKANPEKV KEFRESLTKL GDVYVNDAFG TAHRAHSSMV 190 200 210 220 230 240 GINLPQKAAG FLMKKELEYF AKALESPSKP FLAILGGAKV SDKIKLIENL LYKVDEMIIG 250 260 270 280 290 300 GGMAFTFKKF IDNKEIGSSL FEKTAEQITK DIIAKAAKNN VKLHFPVDYV IADKFDNDAN 310 320 330 340 350 360 IKTVTQDQGI PEGWMGLDCG PETIKENRDT ISRAKTIVWN GPMGVFEKSN FEAGTKAAMD 370 380 390 400 410 420 DVVNATTNGA ITIIGGGDTA TCAAKYNTED KVSHVSTGGG ASLELLEGKE LPGVTALSDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Calmodulin binds to and inhibits the activity of phosphoglycerate kinase." Myre M.A., O'Day D.H. Biochim. Biophys. Acta 1693:177-183(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CALMODULIN.
[2]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	"A transcriptional profile of multicellular development in Dictyostelium discoideum." Van Driessche N., Shaw C., Katoh M., Morio T., Sucgang R., Ibarra M., Kuwayama H., Saito T., Urushihara H., Maeda M., Takeuchi I., Ochiai H., Eaton W., Tollett J., Halter J., Kuspa A., Tanaka Y., Shaulsky G. Development 129:1543-1552(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[4]	"Genome-wide expression analyses of gene regulation during early development of Dictyostelium discoideum." Iranfar N., Fuller D., Loomis W.F. Eukaryot. Cell 2:664-670(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[5]	"Proteomics fingerprinting of phagosome maturation and evidence for the role of a Galpha during uptake." Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M., Soldati T. Mol. Cell. Proteomics 5:2228-2243(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: AX2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF316577 mRNA. Translation: AAG34561.2. AAFI02000103 Genomic DNA. Translation: EAL63606.1.
RefSeq	XP_637130.1. XM_632038.1.
3D structure databases
HSSP	HSSP built from PDB template 1VJD based on UniProtKB Q7SIB7.
ProteinModelPortal	Q9GPM4.
SMR	Q9GPM4. Positions 6-420.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0191349.
Proteomic databases
PRIDE	Q9GPM4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0191349; DDB0191349; DDB_G0287595.
GeneID	8626225.
KEGG	ddi:DDB_G0287595.
Organism-specific databases
dictyBase	DDB_G0287595. pgkA.
Phylogenomic databases
eggNOG	COG0126.
KO	K00927.
OMA	LENCRAN.
ProtClustDB	PTZ00005.
Enzyme and pathway databases
UniPathway	UPA00109; UER00185.
Family and domain databases
Gene3D	3.40.50.1260. 1 hit. 3.40.50.1270. 1 hit.
InterPro	IPR001576. Phosphoglycerate_kinase. IPR015901. Phosphoglycerate_kinase_C. IPR015911. Phosphoglycerate_kinase_CS. IPR015824. Phosphoglycerate_kinase_N. [Graphical view]
PANTHER	PTHR11406. PTHR11406. 1 hit.
Pfam	PF00162. PGK. 1 hit. [Graphical view]
PIRSF	PIRSF000724. Pgk. 1 hit.
PRINTS	PR00477. PHGLYCKINASE.
SUPFAM	SSF53748. PGK. 1 hit.
PROSITE	PS00111. PGLYCERATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGK_DICDI

Accession

Primary (citable) accession number: Q9GPM4
Secondary accession number(s): Q54K34

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)