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Database: UniProt
Entry: Q6AGS4
LinkDB: Q6AGS4
Original site: Q6AGS4 
ID   PCKG_LEIXX              Reviewed;         612 AA.
AC   Q6AGS4;
DT   02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   11-JUN-2014, entry version 65.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP];
DE            Short=PEP carboxykinase;
DE            Short=PEPCK;
DE            EC=4.1.1.32;
GN   Name=pckG; OrderedLocusNames=Lxx04240;
OS   Leifsonia xyli subsp. xyli (strain CTCB07).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Microbacteriaceae; Leifsonia.
OX   NCBI_TaxID=281090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTCB07;
RX   PubMed=15305603; DOI=10.1094/MPMI.2004.17.8.827;
RA   Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A.,
RA   Kitajima J.P., Truffi D., do Amaral A.M., Harakava R.,
RA   de Oliveira J.C.F., Wood D., de Oliveira M.C., Miyaki C.Y.,
RA   Takita M.A., da Silva A.C.R., Furlan L.R., Carraro D.M., Camarotte G.,
RA   Almeida N.F. Jr., Carrer H., Coutinho L.L., El-Dorry H.A.,
RA   Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S.,
RA   Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M.,
RA   Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F.,
RA   Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A.,
RA   Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
RT   "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia
RT   xyli subsp. xyli.";
RL   Mol. Plant Microbe Interact. 17:827-836(2004).
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; AE016822; AAT88421.1; -; Genomic_DNA.
DR   RefSeq; YP_061526.1; NC_006087.1.
DR   ProteinModelPortal; Q6AGS4; -.
DR   SMR; Q6AGS4; 17-610.
DR   STRING; 281090.Lxx04240; -.
DR   EnsemblBacteria; AAT88421; AAT88421; Lxx04240.
DR   GeneID; 2939161; -.
DR   KEGG; lxx:Lxx04240; -.
DR   PATRIC; 22334330; VBILeiXyl11655_0430.
DR   eggNOG; COG1274; -.
DR   HOGENOM; HOG000191700; -.
DR   KO; K01596; -.
DR   OMA; INTEGLG; -.
DR   OrthoDB; EOG6MPWQS; -.
DR   BioCyc; LXYL281090:GH0X-394-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.449.10; -; 1.
DR   Gene3D; 3.90.228.20; -; 2.
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; IPR008210; PEP_carboxykinase_N.
DR   PANTHER; PTHR11561; PTHR11561; 1.
DR   Pfam; PF00821; PEPCK; 1.
DR   PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR   SUPFAM; SSF68923; SSF68923; 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    612       Phosphoenolpyruvate carboxykinase [GTP].
FT                                /FTId=PRO_0000103606.
FT   NP_BIND     520    523       GTP (By similarity).
FT   REGION      393    395       Substrate binding (By similarity).
FT   ACT_SITE    280    280       By similarity.
FT   METAL       236    236       Manganese (By similarity).
FT   METAL       256    256       Manganese; via tele nitrogen (By
FT                                similarity).
FT   METAL       303    303       Manganese (By similarity).
FT   BINDING      84     84       Substrate (By similarity).
FT   BINDING     229    229       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     236    236       Substrate (By similarity).
FT   BINDING     278    278       Substrate (By similarity).
FT   BINDING     395    395       GTP (By similarity).
FT   BINDING     426    426       GTP (By similarity).
SQ   SEQUENCE   612 AA;  66419 MW;  BB6BD41B5049CE6A CRC64;
     MTAPPRPTAP PGAAALTGLA ALHAWVDELA ALLQPDGIVW CDGSRGQTDR LTKQLVAEGK
     LIRLNPEWRP NSFLSRTDPS DVARVEDRTF ICSLDEADAG PTNNWREPEG MRAELREAFA
     GSMRGRTLYV VPFSMGPIGG PLSQLGVQLT DSAYVAVSMG IMTRVASAVL DLIAAGQPWV
     PTVHSVGAPL VDEAGVRQED VAWPCNPVKY IVQFPETREI WSYGSGYGGN AILAKKCFAL
     RIASVMARDE GWLAEHMLIV KVTSPEGRVF HFAAAFPSSC GKTNLAMLKP SIPGWTVETV
     CDDIAWLRPG PDGRLRAINP EAGFFGVAPG TGELTNKTAV EALWGNTIFT NVALRDDGDV
     WWEGLTAEPP AHLIDWEGND WTPASGRPAA HPNSRFTVSA AQCPVIADEW DVVDGVPIDA
     ILFGGRRATN VPLVAQARDW KHGVFIGATI SSEQTAAAEG TVGELRRDPF AMLPFCGYNM
     ADYWAHWLRM GEKLGADAPA IFQVNWFRKG DDGRFLWPGF SENARVIEWI ARRVEGSAGA
     EETAIGRLPL ADELDLDGLG LPAEDLAALF DIDTERWLAE CALTEQYFAR FGPRVPPALT
     AELASLRDKL RA
//
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