PPSA_NEIMB
ID PPSA_NEIMB Reviewed; 794 AA.
AC Q9K0I2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phosphoenolpyruvate synthase;
DE Short=PEP synthase;
DE EC=2.7.9.2;
DE AltName: Full=Pyruvate, water dikinase;
GN Name=ppsA; OrderedLocusNames=NMB0618;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17038831; DOI=10.4161/hv.1.2.1651;
RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.;
RT "Characterization of the protein content of a meningococcal outer membrane
RT vesicle vaccine by polyacrylamide gel electrophoresis and mass
RT spectrometry.";
RL Hum. Vaccin. 1:80-84(2005).
CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC phosphoenolpyruvate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:11364, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.2;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- DOMAIN: The N-terminal domain contains the ATP/Pi binding site, the
CC central domain the pyrophosphate/phosphate carrier histidine, and the
CC C-terminal domain the pyruvate binding site. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC used as vaccines in human.
CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated by a
CC phosphocarrier histidine residue located on the surface of the central
CC domain. The two first partial reactions are catalyzed at an active site
CC located on the N-terminal domain, and the third partial reaction is
CC catalyzed at an active site located on the C-terminal domain. For
CC catalytic turnover, the central domain swivels from the concave surface
CC of the N-terminal domain to that of the C-terminal domain (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
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DR EMBL; AE002098; AAF41044.1; -; Genomic_DNA.
DR PIR; G81177; G81177.
DR RefSeq; NP_273662.1; NC_003112.2.
DR RefSeq; WP_002222834.1; NC_003112.2.
DR PDB; 2OLS; X-ray; 2.40 A; A=1-794.
DR PDBsum; 2OLS; -.
DR AlphaFoldDB; Q9K0I2; -.
DR SMR; Q9K0I2; -.
DR STRING; 122586.NMB0618; -.
DR PaxDb; Q9K0I2; -.
DR PRIDE; Q9K0I2; -.
DR EnsemblBacteria; AAF41044; AAF41044; NMB0618.
DR KEGG; nme:NMB0618; -.
DR PATRIC; fig|122586.8.peg.782; -.
DR HOGENOM; CLU_007308_6_2_4; -.
DR OMA; LETWFFL; -.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; Q9K0I2; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR006319; PEP_synth.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR43030; PTHR43030; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR PIRSF; PIRSF000854; PEP_synthase; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR TIGRFAMs; TIGR01418; PEP_synth; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..794
FT /note="Phosphoenolpyruvate synthase"
FT /id="PRO_0000320270"
FT ACT_SITE 422
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 752
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 512
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 579
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 681
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 681
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 702
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 703
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 704
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 705
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 705
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 17..34
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 77..92
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:2OLS"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 215..224
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 294..311
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:2OLS"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 422..426
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 484..491
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 497..501
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 506..511
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 514..519
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 525..529
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 536..545
FT /evidence="ECO:0007829|PDB:2OLS"
FT TURN 546..548
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 552..571
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 574..579
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 585..589
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 595..597
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 611..615
FT /evidence="ECO:0007829|PDB:2OLS"
FT TURN 617..619
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 620..635
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 642..646
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 652..664
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 676..680
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 683..687
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 689..693
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 696..702
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 703..711
FT /evidence="ECO:0007829|PDB:2OLS"
FT TURN 718..720
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 721..723
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 729..743
FT /evidence="ECO:0007829|PDB:2OLS"
FT TURN 744..746
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 748..754
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 755..758
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 760..769
FT /evidence="ECO:0007829|PDB:2OLS"
FT STRAND 773..776
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 778..780
FT /evidence="ECO:0007829|PDB:2OLS"
FT HELIX 781..791
FT /evidence="ECO:0007829|PDB:2OLS"
SQ SEQUENCE 794 AA; 87170 MW; 2165BDF3CFA67E56 CRC64;
MADNYVIWFE NLRMTDVERV GGKNASLGEM ISQLTEKGVR VPGGFATTAE AYRAFLAHNG
LSERISAALA KLDVEDVAEL ARVGKEIRQW ILDTPFPEQL DAEIEAAWNK MVADAGGADI
SVAVRSSATA EDLPDASFAG QQETFLNING LDNVKEAMHH VFASLYNDRA ISYRVHKGFE
HDIVALSAGV QRMVRSDSGA SGVMFTLDTE SGYDQVVFVT SSYGLGENVV QGAVNPDEFY
VFKPTLKAGK PAILRKTMGS KHIKMIFTDK AEAGKSVTNV DVPEEDRNRF SITDEEITEL
AHYALTIEKH YGRPMDIEWG RDGLDGKLYI LQARPETVKS QEEGNRNLRR FAINGDKTVL
CEGRAIGQKV GQGKVRLIKD ASEMDSVEAG DVLVTDMTDP DWEPVMKRAS AIVTNRGGRT
CHAAIIAREL GIPAVVGCGN ATELLKNGQE VTVSCAEGDT GFIYAGLLDV QITDVALDNM
PKAPVKVMMN VGNPELAFSF ANLPSEGIGL ARMEFIINRQ IGIHPKALLE FDKQDDELKA
EITRRIAGYA SPVDFYVDKI AEGVATLAAS VYPRKTIVRM SDFKSNEYAN LVGGNVYEPH
EENPMLGFRG AARYVADNFK DCFALECKAL KRVRDEMGLT NVEIMIPFVR TLGEAEAVVK
ALKENGLERG KNGLRLIMMC ELPSNAVLAE QFLQYFDGFS IGSNDMTQLT LGLDRDSGLV
SESFDERNPA VKVMLHLAIS ACRKQNKYVG ICGQGPSDHP DFAKWLVEEG IESVSLNPDT
VIETWLYLAN ELNK
