P42850 (PPSA_PYRFU) Reviewed, UniProtKB/Swiss-Prot

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
Ordered Locus Names:	PF0043

Organism

Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

Taxonomic identifier

186497 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	817 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.4
Catalytic activity	ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate. Ref.4
Cofactor	Magnesium.
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Subunit structure	Homooctamer. Ref.4
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=0.11 mM for pyruvate Ref.4 KM=0.40 mM for phosphoenolpyruvate KM=0.39 mM for ATP KM=1.00 mM for AMP KM=38.4 mM for phosphate

Ontologies

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4
	Chain	2 – 817	816	Phosphoenolpyruvate synthase		PRO_0000147044
Regions
	Compositional bias	809 – 815	7	Poly-Glu
Sites
	Active site	442	1	Tele-phosphohistidine intermediate By similarity
	Active site	756	1	Proton donor By similarity
	Metal binding	684	1	Magnesium By similarity
	Metal binding	709	1	Magnesium By similarity
	Binding site	540	1	Substrate By similarity
	Binding site	587	1	Substrate By similarity
	Binding site	684	1	Substrate By similarity
	Binding site	706	1	Substrate; via carbonyl oxygen By similarity
	Binding site	707	1	Substrate; via amide nitrogen By similarity
	Binding site	708	1	Substrate By similarity
	Binding site	709	1	Substrate; via amide nitrogen By similarity
Experimental info
	Sequence conflict	8	1	W → G AA sequence Ref.4
	Sequence conflict	747	1	K → Q in AAA81512. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P42850 [UniParc]. Last modified April 3, 2002. Version 3. Checksum: DA3A7A3CF13C614F	FASTA	817	90,485
	10 20 30 40 50 60 MAYRFIKWFE ELSKNDVPLV GGKGANLGEM TNAGIPVPPG FCVTAEAYKY FVENVKVSKE 70 80 90 100 110 120 DVKRILGEKV NKGTISEVLA QAPDEPRPLQ DWIMDIISKT DVDDSKMLQE NTEAIRTLIK 130 140 150 160 170 180 SLDMPSEIAE EIKQAYKELS QRFGQEEVYV AVRSSATAED LPEASFAGQQ ETYLDVLGAD 190 200 210 220 230 240 DVIDKVKRCW ASLWTARATF YRAKQGFDHS KVYLSAVVQK MVNSEKSGVM FTANPVTNNR 250 260 270 280 290 300 NEIMINASWG LGEAVVSGAV TPDEYIVEKG TWKIKEKVIA KKEVMVIRNP ETGRGTVMVK 310 320 330 340 350 360 VAEYLGPEWV EKQVLTDEQI IEVAKMGQKI EDHYGWPQDI EWAYDKDDGK LYIVQSRPIT 370 380 390 400 410 420 TLKEEATAEE AEEVEEAEVI LKGLGASPGI GAGRVVVIFD ASEIDKVKEG DILVTTMTNP 430 440 450 460 470 480 DMVPAMKRAA AIVTDEGGRT SHAAIVSREL GIPCVVGTKE ATKKLKTGMY VTVDGTRGLV 490 500 510 520 530 540 YKGIVKSLVK KKEEAKAEGG QVVVAGAPLV TGTMVKVNVS MPEVAERAAA TGADGVGLLR 550 560 570 580 590 600 AEHMILSIGQ HPIKFIKEGK EEELVEKLAE GIEKVAAAFY PRPVWYRTLD APTNEFREMP 610 620 630 640 650 660 GGEDEPEERN PMLGWRGIRR GLDQPELLRA EFKAIKKVVE KGYNNIGVML PLVSHPEQIR 670 680 690 700 710 720 EAKRIAREVG LEPHKDVAWG VMIEVPAAAI IIEDLIKEGI DFVSFGTNDL TQYTLAIDRD 730 740 750 760 770 780 NERVAKLYDE THPAVLKLIK HVIKVCKRYG VETSICGQAG SDPKMARILV RLGIDSISAN 790 800 810 PDAVQLIRQV VAQEERKLML EAARKQLFEE EEEEELF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation, sequence and characterization of the maltose-regulated mlrA gene from the hyperthermophilic archaeum Pyrococcus furiosus." Robinson K.A., Schreier H.J. Gene 151:173-176(1994) [PubMed: 7828869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]	"Cloning and sequencing of a gene from the archaeon Pyrococcus furiosus with high homology to a gene encoding phosphoenolpyruvate synthetase from Escherichia coli." Jones C.E., Fleming T.M., Piper P.W., Littlechild J.A., Cowan D.A. Gene 160:101-103(1995) [PubMed: 7628701] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[3]	"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences." Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T. Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[4]	"Phosphoenolpyruvate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus." Hutchins A.M., Holden J.F., Adams M.W.W. J. Bacteriol. 183:709-715(2001) [PubMed: 11133966] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U08376 Genomic DNA. Translation: AAA81512.1. X80819 Genomic DNA. Translation: CAA56785.1. AE009950 Genomic DNA. Translation: AAL80167.1.
PIR	JC4176.
RefSeq	NP_577772.1. NC_003413.1.
3D structure databases
ProteinModelPortal	P42850.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBPYRT00000005738; EBPYRP00000005599; EBPYRG00000005737.
GeneID	1467872.
GenomeReviews	Gene locus PF0043 in contig AE009950_GR.
KEGG	pfu:PF0043.
NMPDR	fig|186497.1.peg.43.
Phylogenomic databases
GeneTree	EBGT00050000022475.
HOGENOM	HBG284863.
OMA	LLRAEHM.
PhylomeDB	P42850.
ProtClustDB	PRK06464.
Family and domain databases
InterPro	IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR008279. PEP-util_enz_mobile_dom. IPR006319. PEP_synth. IPR018274. PEP_util_AS. IPR000121. PEP_util_C. IPR023151. PEP_util_CS. IPR006318. PEP_util_enz. IPR002192. PPDK_PEP-bd. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 2 hits. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.50.30.10. PEP_mobile. 1 hit. G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KO	K01007.
Pfam	PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. PF01326. PPDK_N. 1 hit. [Graphical view]
PRINTS	PR01736. PHPHTRNFRASE.
SUPFAM	SSF52009. PEP_mobile. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
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_PYRFU

Accession

Primary (citable) accession number: P42850
Secondary accession number(s): Q59672

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	April 3, 2002
Last modified:	December 14, 2011
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program