Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Active sitei422Tele-phosphohistidine intermediateBy similarity1
Binding sitei512SubstrateBy similarity1
Binding sitei579SubstrateBy similarity1
Metal bindingi681MagnesiumBy similarity1
Binding sitei681SubstrateBy similarity1
Binding sitei702Substrate; via carbonyl oxygenBy similarity1
Binding sitei703Substrate; via amide nitrogenBy similarity1
Binding sitei704SubstrateBy similarity1
Metal bindingi705MagnesiumBy similarity1
Binding sitei705Substrate; via amide nitrogenBy similarity1
Active sitei752Proton donorBy similarity1

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

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)DescriptionActionsGraphical viewLength
ChainiPRO_00003202701 – 794Phosphoenolpyruvate synthaseAdd BLAST794

Proteomic databases

PaxDbiQ9K0I2.
PRIDEiQ9K0I2.

Interactioni

Protein-protein interaction databases

STRINGi122586.NMB0618.

Structurei

Secondary structure

1794
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Helixi9 – 11Combined sources3
Helixi14 – 16Combined sources3
Helixi17 – 34Combined sources18
Helixi35 – 37Combined sources3
Beta strandi44 – 47Combined sources4
Helixi49 – 56Combined sources8
Helixi58 – 60Combined sources3
Helixi61 – 70Combined sources10
Helixi77 – 92Combined sources16
Helixi98 – 114Combined sources17
Beta strandi122 – 128Combined sources7
Beta strandi144 – 148Combined sources5
Helixi151 – 164Combined sources14
Helixi168 – 177Combined sources10
Beta strandi186 – 192Combined sources7
Beta strandi198 – 207Combined sources10
Turni209 – 211Combined sources3
Beta strandi215 – 224Combined sources10
Helixi227 – 230Combined sources4
Beta strandi237 – 242Combined sources6
Helixi243 – 247Combined sources5
Beta strandi253 – 257Combined sources5
Beta strandi263 – 267Combined sources5
Beta strandi272 – 274Combined sources3
Beta strandi277 – 281Combined sources5
Helixi284 – 287Combined sources4
Helixi294 – 311Combined sources18
Beta strandi315 – 321Combined sources7
Turni323 – 325Combined sources3
Beta strandi328 – 335Combined sources8
Beta strandi392 – 396Combined sources5
Helixi400 – 402Combined sources3
Helixi404 – 407Combined sources4
Beta strandi410 – 416Combined sources7
Helixi422 – 426Combined sources5
Beta strandi434 – 436Combined sources3
Helixi441 – 444Combined sources4
Beta strandi484 – 491Combined sources8
Helixi494 – 496Combined sources3
Helixi497 – 501Combined sources5
Beta strandi506 – 511Combined sources6
Helixi514 – 519Combined sources6
Helixi525 – 529Combined sources5
Helixi531 – 533Combined sources3
Helixi536 – 545Combined sources10
Turni546 – 548Combined sources3
Beta strandi549 – 551Combined sources3
Helixi552 – 571Combined sources20
Beta strandi574 – 579Combined sources6
Helixi585 – 589Combined sources5
Helixi595 – 597Combined sources3
Helixi604 – 606Combined sources3
Helixi611 – 615Combined sources5
Turni617 – 619Combined sources3
Helixi620 – 635Combined sources16
Beta strandi642 – 646Combined sources5
Helixi652 – 664Combined sources13
Helixi671 – 673Combined sources3
Beta strandi676 – 680Combined sources5
Helixi683 – 687Combined sources5
Helixi689 – 693Combined sources5
Beta strandi696 – 702Combined sources7
Helixi703 – 711Combined sources9
Turni718 – 720Combined sources3
Helixi721 – 723Combined sources3
Helixi729 – 743Combined sources15
Turni744 – 746Combined sources3
Beta strandi748 – 754Combined sources7
Helixi755 – 758Combined sources4
Helixi760 – 769Combined sources10
Beta strandi773 – 776Combined sources4
Helixi778 – 780Combined sources3
Helixi781 – 791Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OLSX-ray2.40A1-794[»]
ProteinModelPortaliQ9K0I2.
SMRiQ9K0I2.
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.
OrthoDBiPOG091H013L.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OLSX-ray2.40A1-794[»]
ProteinModelPortaliQ9K0I2.
SMRiQ9K0I2.
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.
OrthoDBiPOG091H013L.

Enzyme and pathway databases

UniPathwayiUPA00138.

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...

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: November 2, 2016
This is version 95 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.