Phosphoenolpyruvate synthase - Synechocystis sp. (strain PCC 6803 / Kazusa)

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Q55905 (PPSA_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. History...

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

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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)

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

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: 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 – 818

818

Phosphoenolpyruvate synthase

PRO_0000147039

Sites

Active site

442

Tele-phosphohistidine intermediate By similarity

Active site

774

Proton donor By similarity

Metal binding

703

Magnesium By similarity

Metal binding

727

Magnesium By similarity

Binding site

532

Substrate By similarity

Binding site

601

Substrate By similarity

Binding site

703

Substrate By similarity

Binding site

724

Substrate; via carbonyl oxygen By similarity

Binding site

725

Substrate; via amide nitrogen By similarity

Binding site

726

Substrate By similarity

Binding site

727

Substrate; via amide nitrogen By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q55905 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E6A93834607733F5
Show »

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

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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: 8590279] [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.

Tabata S.
DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27184 / PCC 6803 / N-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000022 Genomic DNA. Translation: BAA10668.1.
PIR	S76976.
RefSeq	NP_442597.1. NC_000911.1.
3D structure databases
ProteinModelPortal	Q55905.
SMR	Q55905. Positions 18-812.
ModBase	Search...
Protein-protein interaction databases
STRING	Q55905.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	952236.
GenomeReviews	Gene locus slr0301 in contig BA000022_GR.
KEGG	syn:slr0301.
NMPDR	fig\|1148.1.peg.2698.
PATRIC	23842926. VBISynSp132158_3001.
Phylogenomic databases
eggNOG	COG0574.
HOGENOM	HBG284863.
OMA	KNVEIMI.
PhylomeDB	Q55905.
ProtClustDB	PRK06464.
Enzyme and pathway databases
BioCyc	SSP1148:SLR0301-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. 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.
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:	January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents