Reviewed, UniProtKB/Swiss-Prot Q9V2H7 (PPSA_PYRAB)

Names and origin

Protein names

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

Gene names

Name:	ppsA
Ordered Locus Names:	PYRAB00970
ORF Names:	PAB0057

Organism

Pyrococcus abyssi [Complete proteome] [HAMAP]

Taxonomic identifier

29292 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	819 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate By similarity.
Catalytic activity	ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate.
Cofactor	Magnesium By similarity.
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
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.

Ontologies

Keywords
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
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 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
	Chain	1 – 819	819	Probable phosphoenolpyruvate synthase		PRO_0000147043
Regions
	Compositional bias	809 – 816	8	Poly-Glu
Sites
	Active site	441	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

Sequences

	Sequence		Length	Mass (Da)
	Q9V2H7-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: E09486ABB527C6EA	FASTA	819	90,653
	10 20 30 40 50 60 MAYRFIKWFE ELRKEDVPLV GGKGANLGEM TNAGIPVPPG FCVTAEAYKY FVENVKISKE 70 80 90 100 110 120 DVKRILGEKA NKGTIAEVLA QAPDEPRPLQ EWIMDIINRT NVDDSKQLQE NTAVIRELIK 130 140 150 160 170 180 SLDMPAEIAD EIKQAYKELS QRFGKDEIYV 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 ETGKGTVTVK 310 320 330 340 350 360 VAEYLGPEWV EKQVLTDEQI IEVAKMGQKI EEHYGWPQDI EWAYDKDDGK LYIVQSRPVT 370 380 390 400 410 420 TLKETTTEEV EEVEEAEVIL KGLGASPGIG AGRVVVIFDA SEIDKVKEGD VLVTTMTNPD 430 440 450 460 470 480 MVPAMKRAAA IITDEGGRTS HAAIVSRELG IPAVVGTKEA TKKLKTGDYV TVDGTRGLVY 490 500 510 520 530 540 KGIVKSLVEK KKKEEAAAAP GAAVAAAPLV TGTLVKVNVS MPEVAERAAA TGADGVGLLR 550 560 570 580 590 600 AEHMILSIGQ HPVKFIKEGK EEELVEKLAE GIEKVAAAFY PRPVWYRTLD APTNEFREMP 610 620 630 640 650 660 GGEDEPEERN PMLGWRGIRR GLDQPELLRA EFKAIKKVVE KGYNNIGVML PLVSHPEQIR 670 680 690 700 710 720 KAKEIARSVG LEPHKDVAWG IMIEVPAAAI IIEDLIKEGI DFVSFGTNDL TQYTLAIDRD 730 740 750 760 770 780 NERVAKLYDE THPAVLKLIK HVIKVCKRYG VETSICGQAG SDPKMARILV RLGIDSISAN 790 800 810 PDAVQLIRQV VAQEERKLML EAARKRLFEE EEEEEEFLF

References

[1]

"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi." Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P. Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GE5 / Orsay.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ248283 Genomic DNA. Translation: CAB49021.1.
PIR	F75196.
RefSeq	NP_125790.1.
3D structure databases
HSSP	HSSP built from PDB template 1H6Z based on UniProtKB O76283.
ModBase	Search...
Genome annotation databases
GeneID	1494984.
GenomeReviews	Gene locus PYRAB00970 in contig AL096836_GR.
KEGG	pab:PAB0057.
NMPDR	fig|272844.1.peg.108.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9V2H7.
OMA	RAEHMIL.
Enzyme and pathway databases
BioCyc	PABY272844:PAB0057-MON.
BRENDA	2.7.9.2. 262861.
Family and domain databases
InterPro	IPR013815. ATP_grasp_subdomain_1. IPR008279. PEP_mobile. IPR018274. PEP_mobile_CS. IPR006318. PEP_P_trans. 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]
PRINTS	PR01736. PHPHTRNFRASE.
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_PYRAB

Accession

Primary (citable) accession number: Q9V2H7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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