(data stored in ACNUC1104 zone)

SWISSPROT: PCKG_BORPA

ID   PCKG_BORPA              Reviewed;         618 AA.
AC   Q7WAK8;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAY-2019, entry version 94.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000255|HAMAP-Rule:MF_00452};
DE            Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00452};
DE            Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00452};
DE            EC=4.1.1.32 {ECO:0000255|HAMAP-Rule:MF_00452};
GN   Name=pckG {ECO:0000255|HAMAP-Rule:MF_00452}; Synonyms=pck;
GN   OrderedLocusNames=BPP1368;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., 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 conversion of oxaloacetate (OAA) to
CC       phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic
CC       pathway that produces glucose from lactate and other precursors
CC       derived from the citric acid cycle. {ECO:0000255|HAMAP-
CC       Rule:MF_00452}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702;
CC         EC=4.1.1.32; Evidence={ECO:0000255|HAMAP-Rule:MF_00452};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00452};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00452};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00452}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00452}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00452}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family. {ECO:0000255|HAMAP-Rule:MF_00452}.
DR   EMBL; BX640427; CAE36670.1; -; Genomic_DNA.
DR   RefSeq; WP_010928001.1; NC_002928.3.
DR   SMR; Q7WAK8; -.
DR   EnsemblBacteria; CAE36670; CAE36670; BPP1368.
DR   KEGG; bpa:BPP1368; -.
DR   HOGENOM; HOG000191700; -.
DR   KO; K01596; -.
DR   OMA; GPTNNWV; -.
DR   BioCyc; BPAR257311:G1GSY-1407-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001421; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   CDD; cd00819; PEPCK_GTP; 1.
DR   Gene3D; 3.40.449.10; -; 1.
DR   Gene3D; 3.90.228.20; -; 1.
DR   HAMAP; MF_00452; PEPCK_GTP; 1.
DR   InterPro; IPR018091; PEP_carboxykin_GTP_CS.
DR   InterPro; IPR013035; PEP_carboxykinase_C.
DR   InterPro; IPR008209; PEP_carboxykinase_GTP.
DR   InterPro; IPR035077; PEP_carboxykinase_GTP_C.
DR   InterPro; IPR035078; PEP_carboxykinase_GTP_N.
DR   InterPro; IPR008210; PEP_carboxykinase_N.
DR   PANTHER; PTHR11561; PTHR11561; 1.
DR   Pfam; PF00821; PEPCK_GTP; 1.
DR   Pfam; PF17297; PEPCK_N; 1.
DR   PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR   SUPFAM; SSF68923; SSF68923; 1.
DR   PROSITE; PS00505; PEPCK_GTP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7WAK8.
DR   SWISS-2DPAGE; Q7WAK8.
KW   Complete proteome; Cytoplasm; Decarboxylase; Gluconeogenesis;
KW   GTP-binding; Lyase; Manganese; Metal-binding; Nucleotide-binding.
FT   CHAIN         1    618       Phosphoenolpyruvate carboxykinase [GTP].
FT                                /FTId=PRO_0000103591.
FT   NP_BIND     276    281       GTP. {ECO:0000255|HAMAP-Rule:MF_00452}.
FT   NP_BIND     526    529       GTP. {ECO:0000255|HAMAP-Rule:MF_00452}.
FT   REGION      224    226       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00452}.
FT   REGION      396    398       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00452}.
FT   ACT_SITE    277    277       {ECO:0000255|HAMAP-Rule:MF_00452}.
FT   METAL       233    233       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00452}.
FT   METAL       253    253       Manganese; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00452}.
FT   METAL       302    302       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00452}.
FT   BINDING      85     85       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00452}.
FT   BINDING     275    275       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00452}.
FT   BINDING     398    398       GTP. {ECO:0000255|HAMAP-Rule:MF_00452}.
FT   BINDING     429    429       GTP. {ECO:0000255|HAMAP-Rule:MF_00452}.
SQ   SEQUENCE   618 AA;  67985 MW;  7E073BF41021D83E CRC64;
     MNKPSEVKPV ALNVPDYVKH SGLIAWVERI AALTKPDRVV WCDGSQEEYD RLCEQMVQGG
     TMRRLNPAKR ANSYLACSDP SDVARVEDRT FICSEREEDA GPTNNWAAPQ AMRETLGGLF
     DGAMRGRTMY VVPFSMGPLG SPIAHIGVEL SDSPYVVVNM RIMTRMGRKV FDVLGSDGAF
     VPCVHSVGMP LAEGQQDVAW PCNPTKYIVH YPETREIWSF GSGYGGNALL GKKCFALRIA
     STMGRDEGWL AEHMLILGVT SPKGRKYHVA AAFPSACGKT NFAMLIPPHG MDGWKVTTIG
     DDIAWIKPGP DGRLHAINPE AGYFGVAPGT SEKTNFNAMA MLKANVIFTN VALTDDGDVW
     WEGMTDTPPA HLIDWQGQDW TPAIAAETGR KAAHPNARFT APAAQCPSID PEWENPKGVA
     IDAFIFGGRR STTVPLVTEA RNWVEGVYMA ATMGSETTAA AAGQQGVVRR DPFAMLPFCG
     YNMSDYFDHW LKLGRRLEET GATLPRIYCV NWFRKGPDGK FVWPGFGENM RVLRWMLGRL
     DGQAGGVDQV FGISPAYGDI DWTGLEFSPD KFEQVISVDL PAWRAELALH DELFTQLAAR
     LPEDLPLTRT AIERRMAA
//

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