O83026 (PPSA_DEIRA) 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:	DR_1727

Organism

Deinococcus radiodurans

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	780 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: 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
	Chain	1 – 780	780	Phosphoenolpyruvate synthase		PRO_0000147033
Sites
	Active site	409	1	Tele-phosphohistidine intermediate By similarity
	Metal binding	668	1	Magnesium By similarity
	Metal binding	692	1	Magnesium By similarity
	Binding site	499	1	Substrate By similarity
	Binding site	566	1	Substrate By similarity
	Binding site	668	1	Substrate By similarity
	Binding site	689	1	Substrate; via carbonyl oxygen By similarity
	Binding site	690	1	Substrate; via amide nitrogen By similarity
	Binding site	691	1	Substrate By similarity
	Binding site	692	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	O83026 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: AD555076324ADA47	FASTA	780	84,895
	10 20 30 40 50 60 MDMIRPFGTL RMTDVEIVGG KNASIGEMIQ GLAQADVRVP GGFATTADAF RLFLRENQIE 70 80 90 100 110 120 EKINAKLQAL DVNDVNALVA AGKEIRGWVE EARLPAALED AIRQAYGEMG DDPDVAVRSS 130 140 150 160 170 180 ATAEDLPEAS FAGQQETFLN VRGIEEVLNH VKLVFASLYN DRAISYRVHH NFEHSEVALS 190 200 210 220 230 240 AGVQRMVRTD LGVSGVAFTL DTESGFRDAV FVTSSYGLGE MVVQGAVNPD EFFVYKPALE 250 260 270 280 290 300 QGKKAVLRRT RGSKQKKMIY AEAGGVKTVD VDEAEQRAFS LSDDDLTELA RQCVTIEKHY 310 320 330 340 350 360 GRPMDIEWGK DGRDVQIYIL QARPETVQSR AGRTLERFEL TGKGDVLVEG RAVGSRIGAG 370 380 390 400 410 420 VVRVVKSLDQ MDSVQDGDIL VADMTDPDWE PVMKRASAIV TNRGGRTCHA AIIARELGIP 430 440 450 460 470 480 AVVGTGNATR ELHNGDEVTV SCAEGDTGYV YAGRLDFHVN RVELDAMPEV GMKIMMNVAS 490 500 510 520 530 540 PDRAFSFAAL PNEGVGLARV EFIISNVIGI HPRALLDYPD VPADVKAQIE EKTAGYASPR 550 560 570 580 590 600 DFFREKLAEG VASIAAAFAP KPVIVRLSDF KSNEYHHLIG GPAYEPTEEN PMIGFRGASR 610 620 630 640 650 660 YRSADFAEAF ALECQAMKQV RDDMGLTNVQ LMIPFVRTVA EGQRILEILA ANGLTQREND 670 680 690 700 710 720 LKVIMMCEVP SNALLADQFL DLFDGFSIGS NDLTQLTLAL DRDSGLVADM FDEQNEAVLA 730 740 750 760 770 780 LMGMAIKAAK AKGKYVGICG QGPSDHPALA QWLMDQGIDS VSLNPDSVLS TWLHLAGEQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[2]	"IS8301: the second insertion sequence element from Deinococcus radiodurans." Narumi I., Islam S., Cherdchu K., Kikuchi M., Watanabe H., Kitayama S., Yamamoto K. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-780.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000513 Genomic DNA. Translation: AAF11283.1. AB016803 Genomic DNA. Translation: BAA32387.1.
PIR	D75361. T44369.
RefSeq	NP_295450.1. NC_001263.1.
3D structure databases
ProteinModelPortal	O83026.
SMR	O83026. Positions 2-778.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1797452.
GenomeReviews	Gene locus DR_1727 in contig AE000513_GR.
KEGG	dra:DR_1727.
NMPDR	fig|243230.1.peg.1909.
PATRIC	21631082. VBIDeiRad64572_1936.
TIGR	DR_1727.
Phylogenomic databases
HOGENOM	HBG284863.
OMA	ALAQWLM.
PhylomeDB	O83026.
ProtClustDB	PRK06464.
Enzyme and pathway databases
BioCyc	DRAD243230:DR_1727-MONOMER.
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. 1 hit. 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]
PIRSF	PIRSF000854. PEP_synthase. 1 hit.
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_DEIRA

Accession

Primary (citable) accession number: O83026

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	January 25, 2012
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program