Q8XD03 (PGK_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglycerate kinase
EC=2.7.2.3

Gene names

Name:	pgk
Ordered Locus Names:	Z4265, ECs3797

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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 By similarity.
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00145.
Sequence similarities	Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglycerate kinase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 387	386	Phosphoglycerate kinase HAMAP-Rule MF_00145		PRO_0000145943
Regions
	Nucleotide binding	340 – 343	4	ATP By similarity
	Region	21 – 23	3	Substrate binding By similarity
	Region	59 – 62	4	Substrate binding By similarity
Sites
	Binding site	36	1	Substrate By similarity
	Binding site	113	1	Substrate By similarity
	Binding site	146	1	Substrate By similarity
	Binding site	197	1	ATP By similarity
	Binding site	314	1	ATP By similarity
Amino acid modifications
	Modified residue	84	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8XD03 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C21AD662E33514B6	FASTA	387	41,130
	10 20 30 40 50 60 MSVIKMTDLD LAGKRVFIRA DLNVPVKDGK VTSDARIRAS LPTIELALKQ GAKVMVTSHL 70 80 90 100 110 120 GRPTEGEYNE EFSLLPVVNY LKDKLSNPVR LVKDYLDGVD VAEGELVVLE NVRFNKGEKK 130 140 150 160 170 180 DDEILSKKYA ALCDVFVMDA FGTAHRAQAS THGIGKFADV ACAGPLLAAE LDALGKALKE 190 200 210 220 230 240 PARPMVAIVG GSKVSTKLTV LDSLSKIADQ LIVGGGIANT FIAAQGHDVG KSLYEADLVD 250 260 270 280 290 300 EAKRLLTTCN IPVPSDVRVA TEFSETAPAT LKSVNDVKAD EQILDIGDAS AQELAEILKN 310 320 330 340 350 360 AKTILWNGPV GVFEFPNFRK GTEIVANAIA DSEAFSIAGG GDTLAAIDLF GIADKISYIS 370 380 TGGGAFLEFV EGKVLPAVAM LEERAKK

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG58052.1. BA000007 Genomic DNA. Translation: BAB37220.1.
PIR	E91103. H85948.
RefSeq	NP_289493.1. NC_002655.2. NP_311824.1. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8XD03.
SMR	Q8XD03. Positions 2-387.
ModBase	Search...
Protein-protein interaction databases
STRING	155864.Z4265.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG58052; AAG58052; Z4265. BAB37220; BAB37220; BAB37220.
GeneID	916382. 957143.
KEGG	ece:Z4265. ecs:ECs3797.
PATRIC	18357083. VBIEscCol44059_3720.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0126.
HOGENOM	HOG000227107.
KO	K00927.
OMA	EKKNDEA.
ProtClustDB	PRK00073.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-3764-MONOMER.
UniPathway	UPA00109; UER00185.
Family and domain databases
Gene3D	3.40.50.1260. 1 hit. 3.40.50.1270. 1 hit.
HAMAP	MF_00145. Phosphoglyc_kinase.
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_ECO57

Accession

Primary (citable) accession number: Q8XD03

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 27, 2002
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 68 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program