(data stored in ACNUC1104 zone)

SWISSPROT: Q7WA43_BORPA

ID   Q7WA43_BORPA            Unreviewed;       787 AA.
AC   Q7WA43;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAY-2019, entry version 103.
DE   RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|PIRNR:PIRNR000854};
DE            Short=PEP synthase {ECO:0000256|PIRNR:PIRNR000854};
DE            EC=2.7.9.2 {ECO:0000256|PIRNR:PIRNR000854};
DE   AltName: Full=Pyruvate, water dikinase {ECO:0000256|PIRNR:PIRNR000854};
GN   Name=ppsA {ECO:0000313|EMBL:CAE36846.1};
GN   OrderedLocusNames=BPP1544 {ECO:0000313|EMBL:CAE36846.1};
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311 {ECO:0000313|Proteomes:UP000001421};
RN   [1] {ECO:0000313|Proteomes:UP000001421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253
RC   {ECO:0000313|Proteomes:UP000001421};
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.,
RA   Harris D.E., Holden M.T., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.M., Temple L., James K., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC       phosphoenolpyruvate. {ECO:0000256|PIRNR:PIRNR000854}.
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;
CC         EC=2.7.9.2; Evidence={ECO:0000256|PIRNR:PIRNR000854};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000854};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|PIRNR:PIRNR000854}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|PIRNR:PIRNR000854}.
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DR   EMBL; BX640427; CAE36846.1; -; Genomic_DNA.
DR   RefSeq; WP_010928087.1; NC_002928.3.
DR   EnsemblBacteria; CAE36846; CAE36846; BPP1544.
DR   KEGG; bpa:BPP1544; -.
DR   HOGENOM; HOG000230913; -.
DR   KO; K01007; -.
DR   OMA; LETWFFL; -.
DR   BioCyc; BPAR257311:G1GSY-1584-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001421; 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: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_PEP-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   3: Inferred from homology;
DR   PRODOM; Q7WA43.
DR   SWISS-2DPAGE; Q7WA43.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000854};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001421};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000854};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR000854};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000854};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000854};
KW   Pyruvate {ECO:0000313|EMBL:CAE36846.1};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000854,
KW   ECO:0000313|EMBL:CAE36846.1}.
FT   DOMAIN       16    347       PPDK_N. {ECO:0000259|Pfam:PF01326}.
FT   DOMAIN      382    453       PEP-utilizers. {ECO:0000259|Pfam:
FT                                PF00391}.
FT   DOMAIN      479    786       PEP-utilizers_C. {ECO:0000259|Pfam:
FT                                PF02896}.
SQ   SEQUENCE   787 AA;  86270 MW;  DFDEB5EE6020C1F1 CRC64;
     MSYVVSFEQL RMTDVDSVGG KNASLGEMIS QLAGAGVRVP GGFATTAQAF RDFLQASGLD
     KRIADRLATL NPEDVRELAS AGAQIRQWVI DAPFSPEFEQ AIRTAFAELD ADGKGSFAVR
     SSATAEDLPD ASFAGQQETF LNVVGVDDVL DKIRHVFASL YNDRAISYRV HKGYAHAEVA
     LSAGIQRMVR SDKGSAGVMF TIDTESGFQD VVFITSSYGL GETVVQGAVN PDEFYVFKPS
     LERGNYPIVS RRIGSKLIKM EFDPERPEGR AVRTVDVPVS ERNRYSLTDD EVIELARYAV
     IIEKHYQRPM DIEWGRDGVD GKIYILQARP ETVKSQQGVN DVQQRYRLKA TGQVLVTGRA
     IGQKIGAGKV RVVADISEMD KVQAGDVLVT DMTDPNWEPV MKRASAIITN RGGRTCHAAI
     IARELGIPAV VGCGDATDLL KDGQAVTASC AEGDEGRIYD GLIETEVEEV RRGEMPPIDV
     KIMMNVGNPQ LAFDFAQIPN AGVGLARLEF IINNNIGIHP KAVLDYPNVD GELKKAVESA
     ARGHASPRAF FVEKLAEGVA TIGAAFWPKP VIVRMSDFKS NEYRKLVGGS RYEPEEENPM
     LGFRGASRYI AADFEECFRM ECEALKKVRD EMGLTNVEIM VPFVRTLGQA RKVVELLAAH
     GLARGENGLK LIMMCEVPSN AILAEQFLEY FDGFSIGSND MTQLTLGLDR DSGMELLAAD
     FDERDDAVKF MLRRAIKACL AANKYVGICG QGPSDHPDFA QWLKDEGILS MSLNPDTVVE
     TWQQLAK
//

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