Phosphoenolpyruvate synthase - Pyrococcus furiosus

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P42850 (PPSA_PYRFU)

Last modified November 3, 2009. Version 70. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

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 [Complete proteome] [HAMAP]

Taxonomic identifier

2261 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Hide | Top

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.

Hide | Top

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: K_M=0.11 mM for pyruvate K_M=0.40 mM for phosphoenolpyruvate K_M=0.39 mM for ATP K_M=1.00 mM for AMP K_M=38.4 mM for phosphate

Hide | Top

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 pyruvate, water dikinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 817

816

Phosphoenolpyruvate synthase

PRO_0000147044

Regions

Compositional bias

809 – 815

Poly-Glu

Sites

Active site

442

Tele-phosphohistidine intermediate By similarity

Active site

756

Proton donor By similarity

Metal binding

684

Magnesium By similarity

Metal binding

709

Magnesium By similarity

Binding site

540

Substrate By similarity

Binding site

587

Substrate By similarity

Binding site

684

Substrate By similarity

Binding site

706

Substrate; via carbonyl oxygen By similarity

Binding site

707

Substrate; via amide nitrogen By similarity

Binding site

708

Substrate By similarity

Binding site

709

Substrate; via amide nitrogen By similarity

Experimental info

Sequence conflict

W → G AA sequence Ref.4

Sequence conflict

747

K → Q in AAA81512. Ref.1

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P42850-1 [UniParc].

Last modified April 3, 2002. Version 3.
Checksum: DA3A7A3CF13C614F
Show »

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

« Hide

Hide | Top

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]	"The complete sequence of the Pyrococcus furiosus genome." Weiss R.B., Dunn D.M., Robb F.T., Brown J.R. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases 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.

Hide | Top

Cross-references

Sequence databases
	U08376 Genomic DNA. Translation: AAA81512.1. X80819 Genomic DNA. Translation: CAA56785.1. AE009950 Genomic DNA. Translation: AAL80167.1.
PIR	JC4176.
RefSeq	NP_577772.1.
3D structure databases
HSSP	HSSP built from PDB template 1H6Z based on UniProtKB O76283.
ModBase	Search...
Genome annotation databases
GeneID	1467872.
GenomeReviews	Gene locus PF0043 in contig AE009950_GR.
KEGG	pfu:PF0043.
NMPDR	fig\|186497.1.peg.43.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P42850.
OMA	RAEHMIL.
Enzyme and pathway databases
BRENDA	2.7.9.2. 321.
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...

Hide | Top

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:	November 3, 2009
This is version 70 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents