ID   PCKG_BORA1              Reviewed;         621 AA.
AC   Q2L1L0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP];
DE            Short=PEP carboxykinase;
DE            Short=PEPCK;
DE            EC=4.1.1.32;
DE   AltName: Full=Phosphoenolpyruvate carboxylase;
GN   Name=pckG; OrderedLocusNames=BAV1626;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: GTP + oxaloacetate = GDP + phosphoenolpyruvate
CC       + CO(2).
CC   -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family.
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DR   EMBL; AM167904; CAJ49235.1; -; Genomic_DNA.
DR   RefSeq; YP_786146.1; -.
DR   GeneID; 6265530; -.
DR   GenomeReviews; AM167904_GR; BAV1626.
DR   KEGG; bav:BAV1626; -.
DR   NMPDR; fig|521.1.peg.1777; -.
DR   HOGENOM; Q2L1L0; -.
DR   OMA; Q2L1L0; SHPNARF.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) act...; IEA:HAMAP.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:HAMAP.
DR   HAMAP; MF_00452; -; 1.
DR   InterPro; IPR018091; PEP_carboxykin_GTP_CS.
DR   InterPro; IPR013035; PEP_carboxykinase_C.
DR   InterPro; IPR008209; PEP_carboxykinase_GTP.
DR   InterPro; IPR008210; PEP_carboxykinase_N.
DR   Gene3D; G3DSA:3.90.228.20; PEP_carboxykinase_C; 1.
DR   Gene3D; G3DSA:3.40.449.10; PEP_carboxykinase_N; 1.
DR   PANTHER; PTHR11561; PEP_carboxykin; 1.
DR   Pfam; PF00821; PEPCK; 1.
DR   PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR   ProDom; PD004738; PEPCK_N; 1.
DR   PROSITE; PS00505; PEPCK_GTP; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Decarboxylase; Gluconeogenesis;
KW   GTP-binding; Lyase; Manganese; Metal-binding; Nucleotide-binding.
FT   CHAIN         1    621       Phosphoenolpyruvate carboxykinase [GTP].
FT                                /FTId=PRO_1000060287.
FT   NP_BIND     276    281       GTP (By similarity).
FT   NP_BIND     526    529       GTP (By similarity).
FT   REGION      396    398       Substrate binding (By similarity).
FT   ACT_SITE    277    277       By similarity.
FT   METAL       233    233       Manganese (By similarity).
FT   METAL       253    253       Manganese (By similarity).
FT   METAL       302    302       Manganese (By similarity).
FT   BINDING      85     85       Substrate (By similarity).
FT   BINDING     226    226       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     233    233       Substrate (By similarity).
FT   BINDING     275    275       Substrate (By similarity).
FT   BINDING     398    398       GTP (By similarity).
FT   BINDING     429    429       GTP (By similarity).
SQ   SEQUENCE   621 AA;  67910 MW;  70C191E3B587F43F CRC64;
     MTQAAEATLP PLNVPSYVKH ARLIDWVQGV VALTKPARVV WCDGSQEEAD RLCEQMVQAG
     TMRRLNPAKR PNSYLAWSDP SDVARVEDRT FICSQREEDA GPTNNWAAPA EMRNTLQGLF
     DGAMRGRTLY VVPFSMGPLG SPIAHIGVEL SDSPYVAVNM RIMTRMGRAV WDVLGADGEF
     VPCVHSVGMP LAEGQADVAW PCNPVKYIVH YPETREIWSF GSGYGGNALL GKKCFALRIA
     STMGRDEGWL AEHMLILGVT TPKGRKFHVA AAFPSACGKT NFAMLIPPSG MDGWKVSTIG
     DDIAWIKPGQ DGRLRAINPE AGYFGVAPGT SEKTNPNAMA TLKANVIFTN VALTDDGDVW
     WEGMTDTPPA HLIDWQGKDW TPEIARETGR KAAHPNARFT APASQCPSID PEWENPQGVA
     IDAFIFGGRR STTIPLVTEA RDWVQGVYMA ATMGSETTAA AVGQQGVVRR DPFAMLPFCG
     YNMADYFNHW LAVGQRLADA GATLPRIYCV NWFRKGPNGK FVWPGFGENM RVLKWMLGRL
     SGEAGGQEQV FGISPSYGDV DWTGLEFTPD QFQQVISVEA PAWREELALH GELFEQLAQG
     LPPALSRAKA DIEHRLAAVQ A
//