Reviewed, UniProtKB/Swiss-Prot P23538 (PPSA_ECOLI)

Names and origin

Protein names

Recommended name:
    Phosphoenolpyruvate synthase
      Short name=PEP synthase
    EC=2.7.9.2
Alternative name(s):
    Pyruvate, water dikinase

Gene names

Name:	ppsA
Synonyms:	pps
Ordered Locus Names:	b1702, JW1692

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	792 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate. Ref.7
Catalytic activity	ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate. Ref.7 Ref.6
Cofactor	Magnesium. Ref.7
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Subunit structure	Homodimer. Ref.8
Domain	The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site By similarity.
Miscellaneous	The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain By similarity.
Sequence similarities	Belongs to the PEP-utilizing enzyme family.
Biophysicochemical properties	Kinetic parameters: KM=0.083 mM for pyruvate KM=0.028 mM for ATP KM=10.4 mM for phosphate

Ontologies

Keywords
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from electronic annotation. Source: InterPro phosphorylation Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct pyruvate, water dikinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
rplB	P60422	1	EBI-1114517,EBI-543515

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 792	791	Phosphoenolpyruvate synthase		PRO_0000147034
Sites
	Active site	421	1	Tele-phosphohistidine intermediate By similarity
	Active site	751	1	Proton donor By similarity
	Metal binding	680	1	Magnesium By similarity
	Metal binding	704	1	Magnesium By similarity
	Binding site	511	1	Substrate By similarity
	Binding site	578	1	Substrate By similarity
	Binding site	680	1	Substrate By similarity
	Binding site	701	1	Substrate; via carbonyl oxygen By similarity
	Binding site	702	1	Substrate; via amide nitrogen By similarity
	Binding site	703	1	Substrate By similarity
	Binding site	704	1	Substrate; via amide nitrogen By similarity
Experimental info
	Sequence conflict	194 – 195	2	RM → AGL in AAA24319. Ref.1
	Sequence conflict	341 – 360	20	RSRGQ…GKIIA → AHAVRSWSVIRCIHRVRLSP in AAA24319. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P23538-1 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: DBBAB0BA9B9F7DD9	FASTA	792	87,435
	10 20 30 40 50 60 MSNNGSSPLV LWYNQLGMND VDRVGGKNAS LGEMITNLSG MGVSVPNGFA TTADAFNQFL 70 80 90 100 110 120 DQSGVNQRIY ELLDKTDIDD VTQLAKAGAQ IRQWIIDTPF QPELENAIRE AYAQLSADDE 130 140 150 160 170 180 NASFAVRSSA TAEDMPDASF AGQQETFLNV QGFDAVLVAV KHVFASLFND RAISYRVHQG 190 200 210 220 230 240 YDHRGVALSA GVQRMVRSDL ASSGVMFSID TESGFDQVVF ITSAWGLGEM VVQGAVNPDE 250 260 270 280 290 300 FYVHKPTLAA NRPAIVRRTM GSKKIRMVYA PTQEHGKQVK IEDVPQEQRD IFSLTNEEVQ 310 320 330 340 350 360 ELAKQAVQIE KHYGRPMDIE WAKDGHTGKL FIVQARPETV RSRGQVMERY TLHSQGKIIA 370 380 390 400 410 420 EGRAIGHRIG AGPVKVIHDI SEMNRIEPGD VLVTDMTDPD WEPIMKKASA IVTNRGGRTC 430 440 450 460 470 480 HAAIIARELG IPAVVGCGDA TERMKDGENV TVSCAEGDTG YVYAELLEFS VKSSSVETMP 490 500 510 520 530 540 DLPLKVMMNV GNPDRAFDFA CLPNEGVGLA RLEFIINRMI GVHPRALLEF DDQEPQLQNE 550 560 570 580 590 600 IREMMKGFDS PREFYVGRLT EGIATLGAAF YPKRVIVRLS DFKSNEYANL VGGERYEPDE 610 620 630 640 650 660 ENPMLGFRGA GRYVSDSFRD CFALECEAVK RVRNDMGLTN VEIMIPFVRT VDQAKAVVEE 670 680 690 700 710 720 LARQGLKRGE NGLKIIMMCE IPSNALLAEQ FLEYFDGFSI GSNDMTQLAL GLDRDSGVVS 730 740 750 760 770 780 ELFDERNDAV KALLSMAIRA AKKQGKYVGI CGQGPSDHED FAAWLMEEGI DSLSLNPDTV 790 VQTWLSLAEL KK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The cloning and sequence of the E. coli pps gene." Holzschu D.L., McElver J.A., Liao C.C., Berry A. Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Cloning and nucleotide sequence of the Escherichia coli K-12 ppsA gene, encoding PEP synthase." Niersbach M., Kreuzaler F., Geerse R.H., Postma P.W., Hirsch H.J. Mol. Gen. Genet. 231:332-336(1992) [PubMed: 1310524] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE OF 2-21. Strain: K12.
[3]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The mechanism of the phosphoenolpyruvate synthase reaction." Cooper R.A., Kornberg H.L. Biochim. Biophys. Acta 141:211-213(1967) [PubMed: 4293109] [Abstract] Cited for: CATALYTIC ACTIVITY.
[7]	"Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent metal ions." Berman K.M., Cohn M. J. Biol. Chem. 245:5309-5318(1970) [PubMed: 4319237] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[8]	"Phosphoenolypyruvate synthetase of Escherichia coli: molecular weight, subunit composition, and identification of phosphohistidine in phosphoenzyme intermediate." Narindrasorasak S., Bridger W.A. J. Biol. Chem. 252:3121-3127(1977) [PubMed: 16880] [Abstract] Cited for: PHOSPHOINTERMEDIATE OF REACTION, SUBUNIT, AMINO-ACID COMPOSITION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M69116 Genomic DNA. Translation: AAA24319.1. X59381 Genomic DNA. Translation: CAA42024.1. U00096 Genomic DNA. Translation: AAC74772.1. AP009048 Genomic DNA. Translation: BAA15471.1.
PIR	S20554.
RefSeq	AP_002322.1. NP_416217.1.
3D structure databases
HSSP	HSSP built from PDB template 1H6Z based on UniProtKB O76283.
ModBase	Search...
Protein-protein interaction databases
IntAct	P23538. 6 interactions.
STRING	P23538.
PTM databases
PhosSite	P23538.
2-D gel databases
SWISS-2DPAGE	P23538.
ECO2DBASE	B083.0. 6TH EDITION.
Proteomic databases
PRIDE	P23538.
Genome annotation databases
GeneID	946209.
GenomeReviews	Gene locus JW1692 in contig AP009048_GR. Gene locus b1702 in contig U00096_GR.
KEGG	ecj:JW1692. eco:b1702.
Organism-specific databases
EchoBASE	EB0752.
EcoGene	EG10759. pps.
CMR	Search...
Phylogenomic databases
HOGENOM	P23538.
OMA	NKYVGIC.
Enzyme and pathway databases
BioCyc	EcoCyc:PEPSYNTH-MON. MetaCyc:PEPSYNTH-MON.
BRENDA	2.7.9.2. 246.
Gene expression databases
Genevestigator	P23538.
Family and domain databases
InterPro	IPR013815. ATP_grasp_subdomain_1. IPR008279. PEP_mobile. IPR018274. PEP_mobile_CS. IPR006319. PEP_synth. IPR000121. PEP_utilizers. IPR002192. PPDK_PEP_bd. IPR015813. Pyrv/PenolPyrv_Kinase_cat. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.50.30.10. PEP_mobile. 1 hit. G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
Pfam	PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. PF01326. PPDK_N. 1 hit. [Graphical view]
ProDom	PD000940. PEP_utilizers. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01418. PEP_synth. 1 hit.
PROSITE	PS00742. PEP_ENZYMES_2. 1 hit. PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPSA_ECOLI

Accession

Primary (citable) accession number: P23538

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 84 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)