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Protein

Phosphoenolpyruvate synthase

Gene

ppsA

Organism
Neisseria meningitidis serogroup B (strain MC58)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.By similarity

Catalytic activityi

ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate.

Cofactori

Mg2+By similarity

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei422 – 4221Tele-phosphohistidine intermediateBy similarity
Binding sitei512 – 5121SubstrateBy similarity
Binding sitei579 – 5791SubstrateBy similarity
Metal bindingi681 – 6811MagnesiumBy similarity
Binding sitei681 – 6811SubstrateBy similarity
Binding sitei702 – 7021Substrate; via carbonyl oxygenBy similarity
Binding sitei703 – 7031Substrate; via amide nitrogenBy similarity
Binding sitei704 – 7041SubstrateBy similarity
Metal bindingi705 – 7051MagnesiumBy similarity
Binding sitei705 – 7051Substrate; via amide nitrogenBy similarity
Active sitei752 – 7521Proton donorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciNMEN122586:GHGG-644-MONOMER.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate synthase (EC:2.7.9.2)
Short name:
PEP synthase
Alternative name(s):
Pyruvate, water dikinase
Gene namesi
Name:ppsA
Ordered Locus Names:NMB0618
OrganismiNeisseria meningitidis serogroup B (strain MC58)
Taxonomic identifieri122586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
Proteomesi
  • UP000000425 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 794794Phosphoenolpyruvate synthasePRO_0000320270Add
BLAST

Proteomic databases

PaxDbiQ9K0I2.
PRIDEiQ9K0I2.

Interactioni

Protein-protein interaction databases

STRINGi122586.NMB0618.

Structurei

Secondary structure

1
794
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi9 – 113Combined sources
Helixi14 – 163Combined sources
Helixi17 – 3418Combined sources
Helixi35 – 373Combined sources
Beta strandi44 – 474Combined sources
Helixi49 – 568Combined sources
Helixi58 – 603Combined sources
Helixi61 – 7010Combined sources
Helixi77 – 9216Combined sources
Helixi98 – 11417Combined sources
Beta strandi122 – 1287Combined sources
Beta strandi144 – 1485Combined sources
Helixi151 – 16414Combined sources
Helixi168 – 17710Combined sources
Beta strandi186 – 1927Combined sources
Beta strandi198 – 20710Combined sources
Turni209 – 2113Combined sources
Beta strandi215 – 22410Combined sources
Helixi227 – 2304Combined sources
Beta strandi237 – 2426Combined sources
Helixi243 – 2475Combined sources
Beta strandi253 – 2575Combined sources
Beta strandi263 – 2675Combined sources
Beta strandi272 – 2743Combined sources
Beta strandi277 – 2815Combined sources
Helixi284 – 2874Combined sources
Helixi294 – 31118Combined sources
Beta strandi315 – 3217Combined sources
Turni323 – 3253Combined sources
Beta strandi328 – 3358Combined sources
Beta strandi392 – 3965Combined sources
Helixi400 – 4023Combined sources
Helixi404 – 4074Combined sources
Beta strandi410 – 4167Combined sources
Helixi422 – 4265Combined sources
Beta strandi434 – 4363Combined sources
Helixi441 – 4444Combined sources
Beta strandi484 – 4918Combined sources
Helixi494 – 4963Combined sources
Helixi497 – 5015Combined sources
Beta strandi506 – 5116Combined sources
Helixi514 – 5196Combined sources
Helixi525 – 5295Combined sources
Helixi531 – 5333Combined sources
Helixi536 – 54510Combined sources
Turni546 – 5483Combined sources
Beta strandi549 – 5513Combined sources
Helixi552 – 57120Combined sources
Beta strandi574 – 5796Combined sources
Helixi585 – 5895Combined sources
Helixi595 – 5973Combined sources
Helixi604 – 6063Combined sources
Helixi611 – 6155Combined sources
Turni617 – 6193Combined sources
Helixi620 – 63516Combined sources
Beta strandi642 – 6465Combined sources
Helixi652 – 66413Combined sources
Helixi671 – 6733Combined sources
Beta strandi676 – 6805Combined sources
Helixi683 – 6875Combined sources
Helixi689 – 6935Combined sources
Beta strandi696 – 7027Combined sources
Helixi703 – 7119Combined sources
Turni718 – 7203Combined sources
Helixi721 – 7233Combined sources
Helixi729 – 74315Combined sources
Turni744 – 7463Combined sources
Beta strandi748 – 7547Combined sources
Helixi755 – 7584Combined sources
Helixi760 – 76910Combined sources
Beta strandi773 – 7764Combined sources
Helixi778 – 7803Combined sources
Helixi781 – 79111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OLSX-ray2.40A1-794[»]
ProteinModelPortaliQ9K0I2.
SMRiQ9K0I2. Positions 4-792.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9K0I2.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the PEP-utilizing enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4108HRN. Bacteria.
COG0574. LUCA.
HOGENOMiHOG000230913.
KOiK01007.
OMAiDELHTAC.
OrthoDBiEOG632CZ4.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR013815. 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-like_dom.
[Graphical view]
PfamiPF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
PF01326. PPDK_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000854. PEP_synthase. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
TIGRFAMsiTIGR01418. PEP_synth. 1 hit.
PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9K0I2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADNYVIWFE NLRMTDVERV GGKNASLGEM ISQLTEKGVR VPGGFATTAE
60 70 80 90 100
AYRAFLAHNG LSERISAALA KLDVEDVAEL ARVGKEIRQW ILDTPFPEQL
110 120 130 140 150
DAEIEAAWNK MVADAGGADI SVAVRSSATA EDLPDASFAG QQETFLNING
160 170 180 190 200
LDNVKEAMHH VFASLYNDRA ISYRVHKGFE HDIVALSAGV QRMVRSDSGA
210 220 230 240 250
SGVMFTLDTE SGYDQVVFVT SSYGLGENVV QGAVNPDEFY VFKPTLKAGK
260 270 280 290 300
PAILRKTMGS KHIKMIFTDK AEAGKSVTNV DVPEEDRNRF SITDEEITEL
310 320 330 340 350
AHYALTIEKH YGRPMDIEWG RDGLDGKLYI LQARPETVKS QEEGNRNLRR
360 370 380 390 400
FAINGDKTVL CEGRAIGQKV GQGKVRLIKD ASEMDSVEAG DVLVTDMTDP
410 420 430 440 450
DWEPVMKRAS AIVTNRGGRT CHAAIIAREL GIPAVVGCGN ATELLKNGQE
460 470 480 490 500
VTVSCAEGDT GFIYAGLLDV QITDVALDNM PKAPVKVMMN VGNPELAFSF
510 520 530 540 550
ANLPSEGIGL ARMEFIINRQ IGIHPKALLE FDKQDDELKA EITRRIAGYA
560 570 580 590 600
SPVDFYVDKI AEGVATLAAS VYPRKTIVRM SDFKSNEYAN LVGGNVYEPH
610 620 630 640 650
EENPMLGFRG AARYVADNFK DCFALECKAL KRVRDEMGLT NVEIMIPFVR
660 670 680 690 700
TLGEAEAVVK ALKENGLERG KNGLRLIMMC ELPSNAVLAE QFLQYFDGFS
710 720 730 740 750
IGSNDMTQLT LGLDRDSGLV SESFDERNPA VKVMLHLAIS ACRKQNKYVG
760 770 780 790
ICGQGPSDHP DFAKWLVEEG IESVSLNPDT VIETWLYLAN ELNK
Length:794
Mass (Da):87,170
Last modified:October 1, 2000 - v1
Checksum:i2165BDF3CFA67E56
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002098 Genomic DNA. Translation: AAF41044.1.
PIRiG81177.
RefSeqiNP_273662.1. NC_003112.2.
WP_002222834.1. NC_003112.2.

Genome annotation databases

EnsemblBacteriaiAAF41044; AAF41044; NMB0618.
GeneIDi902731.
KEGGinme:NMB0618.
PATRICi20356525. VBINeiMen85645_0782.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002098 Genomic DNA. Translation: AAF41044.1.
PIRiG81177.
RefSeqiNP_273662.1. NC_003112.2.
WP_002222834.1. NC_003112.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OLSX-ray2.40A1-794[»]
ProteinModelPortaliQ9K0I2.
SMRiQ9K0I2. Positions 4-792.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi122586.NMB0618.

Proteomic databases

PaxDbiQ9K0I2.
PRIDEiQ9K0I2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF41044; AAF41044; NMB0618.
GeneIDi902731.
KEGGinme:NMB0618.
PATRICi20356525. VBINeiMen85645_0782.

Phylogenomic databases

eggNOGiENOG4108HRN. Bacteria.
COG0574. LUCA.
HOGENOMiHOG000230913.
KOiK01007.
OMAiDELHTAC.
OrthoDBiEOG632CZ4.

Enzyme and pathway databases

UniPathwayiUPA00138.
BioCyciNMEN122586:GHGG-644-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9K0I2.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR013815. 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-like_dom.
[Graphical view]
PfamiPF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
PF01326. PPDK_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000854. PEP_synthase. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
TIGRFAMsiTIGR01418. PEP_synth. 1 hit.
PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MC58.
  2. "Characterization of the protein content of a meningococcal outer membrane vesicle vaccine by polyacrylamide gel electrophoresis and mass spectrometry."
    Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.
    Hum. Vaccin. 1:80-84(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPPSA_NEIMB
AccessioniPrimary (citable) accession number: Q9K0I2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 1, 2000
Last modified: March 16, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Present in outer membrane vesicle formulations which are used as vaccines in human.
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).By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.