Q55905 (PPSA_SYNY3) 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:	slr0301

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › Synechocystis sp. PCC 6803

Protein attributes

Sequence length	818 AA.
Sequence status	Complete.
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 Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-UniPathway pyruvate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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
	Chain	1 – 818	818	Phosphoenolpyruvate synthase		PRO_0000147039
Sites
	Active site	442	1	Tele-phosphohistidine intermediate By similarity
	Active site	774	1	Proton donor By similarity
	Metal binding	703	1	Magnesium By similarity
	Metal binding	727	1	Magnesium By similarity
	Binding site	532	1	Substrate By similarity
	Binding site	601	1	Substrate By similarity
	Binding site	703	1	Substrate By similarity
	Binding site	724	1	Substrate; via carbonyl oxygen By similarity
	Binding site	725	1	Substrate; via amide nitrogen By similarity
	Binding site	726	1	Substrate By similarity
	Binding site	727	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55905 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E6A93834607733F5	FASTA	818	89,929
	10 20 30 40 50 60 MVSSVVEKTS VAHKETALIL WFEEVGTHDV GLVGGKNSSL GEMIQQLTNK GVNVPSGFAT 70 80 90 100 110 120 TAYAYRYFIQ EAGLEQKLRD LFTDLDVNDM ANLQERGHLA RQLILDTPFP QNLQTAIAEA 130 140 150 160 170 180 YGAMCERYGQ KMGRTGVDVA VRSSATAEDL PEASFAGQQE TYLNVHSLSC VLESCHKCFA 190 200 210 220 230 240 SLFTDRAISY RHHNGFDHFA VALSVGVQKM VRSDLATSGV MFSIDTETGF KNAALITAAY 250 260 270 280 290 300 GLGENVVQGA VNPDEYFVFK PTLKEGFKPI LEKRLGSKAI KMVYDVGGSK LTKNVEVAEP 310 320 330 340 350 360 EREKYCINDE EILQLARWAC IIEDHYSGVR GVYTPMDIEW AKDGQTGELF IVQARPETVQ 370 380 390 400 410 420 SQKSANVIKT YELKDHSQVL ATGRSVGAAI GQGKAQVIRN VSQINQFRPG EVLITNRTDP 430 440 450 460 470 480 DWEPIMKQAS AIVTNQGGKT CHAAIIAREM GIPAIVGCGD ATDTIKTGED VTICCSEGDE 490 500 510 520 530 540 GSVYSGILNY EVHETELSNL PRTKTQILMN VGNPEQAFGF ASYPADGVGL ARLEFIIANH 550 560 570 580 590 600 IKAHPLALMK FDELEDPLAK AEIAELTKLY AGDRPRFFVD KLAHGIAMIA AAFYPKPVVV 610 620 630 640 650 660 RMSDFKSNEY ANLLGGRQFE PKEENPMIGW RGASRYYDPN YREAYALECQ ALKRVRDEMG 670 680 690 700 710 720 LTNVIPMIPF CRTPDEGRKV IAEMAKHGLK QGKNGLEIYV MCELPSNVIL ADEFSEVFDG 730 740 750 760 770 780 FSIGSNDLTQ LTLGLDRDSS LVAHLFDERN LGVKRMVKMA IETAKANGRK IGICGQAPSD 790 800 810 YPEFAEFLVE LGIDSISLNP DSVLKTVLRI AEVEKALG

References

[1]

"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome." Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S. DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27184 / PCC 6803 / N-1.

[2]

"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000022 Genomic DNA. Translation: BAA10668.1.
PIR	S76976.
RefSeq	NP_442597.1. NC_000911.1. YP_005652658.1. NC_017277.1. YP_007452473.1. NC_020286.1.
3D structure databases
ProteinModelPortal	Q55905.
SMR	Q55905. Positions 18-812.
ModBase	Search...
Protein-protein interaction databases
STRING	1148.slr0301.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAA10668; BAA10668; BAA10668.
GeneID	12254772. 14618155. 952236.
KEGG	syn:slr0301. syy:SYNGTS_2705.
PATRIC	23842926. VBISynSp132158_3001.
Phylogenomic databases
eggNOG	COG0574.
HOGENOM	HOG000230912.
KO	K01007.
OMA	NVMERYL.
ProtClustDB	PRK06464.
Enzyme and pathway databases
UniPathway	UPA00138.
Family and domain databases
Gene3D	3.20.20.60. 1 hit. 3.30.1490.20. 1 hit. 3.30.470.20. 1 hit.
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. IPR002192. PPDK_PEP-bd. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view]
Pfam	PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. PF01326. PPDK_N. 1 hit. [Graphical view]
PIRSF	PIRSF000854. PEP_synthase. 1 hit.
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_SYNY3

Accession

Primary (citable) accession number: Q55905

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program