ID   PCKG_SULAC              Reviewed;         604 AA.
AC   Q4J9S8;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=Saci_1100;
OS   Sulfolobus acidocaldarius.
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=2285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / IFO 15157 / JCM 8929 / NCIB 11770;
RX   PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family.
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DR   EMBL; CP000077; AAY80452.1; -; Genomic_DNA.
DR   RefSeq; YP_255745.1; -.
DR   GeneID; 3474134; -.
DR   GenomeReviews; CP000077_GR; Saci_1100.
DR   KEGG; sai:Saci_1100; -.
DR   NMPDR; fig|330779.3.peg.1575; -.
DR   HOGENOM; Q4J9S8; -.
DR   OMA; Q4J9S8; SHPNARF.
DR   BioCyc; SACI330779:SACI_1100-MON; -.
DR   BRENDA; 4.1.1.32; 434.
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; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Decarboxylase; Gluconeogenesis;
KW   GTP-binding; Lyase; Manganese; Metal-binding; Nucleotide-binding.
FT   CHAIN         1    604       Phosphoenolpyruvate carboxykinase [GTP].
FT                                /FTId=PRO_0000103621.
FT   REGION      365    367       Substrate binding (By similarity).
FT   ACT_SITE    260    260       By similarity.
FT   METAL       218    218       Manganese (By similarity).
FT   METAL       237    237       Manganese (By similarity).
FT   METAL       275    275       Manganese (By similarity).
FT   BINDING      87     87       Substrate (By similarity).
FT   BINDING     211    211       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     218    218       Substrate (By similarity).
FT   BINDING     258    258       Substrate (By similarity).
FT   BINDING     367    367       GTP (By similarity).
FT   BINDING     398    398       GTP (By similarity).
SQ   SEQUENCE   604 AA;  68720 MW;  FFEA81938BF49096 CRC64;
     MKVDLSPLNG IISDKAFQKL KSINNPSLVH FLSKTIELTT PDRVYVSFGE EKDREYVKKR
     ALETKEEIKL KMEGHTIHFD HPLDQARARE DTFILTDEKI PFVNTKPRDE GLREMLSLLK
     GSMKGREMYV GFYSLGPRNS KFSILAVQIT DSPYVIHSEN ILYRNAFEDF YGDKPFLKFI
     HSKGQLDIKK RRIMIDVKEN TVYSVNTTYA GNSVGLKKLA LRLTVTKAVN EGWLSEHMAI
     VGFEGNRGTH YFTASFPSGS GKTSTSMLGS LISDDLAFIK EIDGVCRAVN PEIGIFGIIQ
     GINERDDPVI WDVLHKPGEV IFSNVLMTDD GGVYWEGSEV EKPEKGYNYE GAWTKESGKP
     ASHPNARFTS PLTSFSNLDK DYDNPQGVVI DGIIFGVRDY STLVPVTEAF SWEHGVITIG
     ASMESSRTSA VIGKADVLEF NPMAILDFMP LSLGKYLNNY LTFGRNLKYV PKIFSFNYFL
     KDENNKFLNS KEDKRVWVKW AVKRVESETD AIYTPVGFIP YYEDLSKLFN STLGKQYTKE
     AYELQFTLKL SKYLEKTERI MKIYSEIADT PIEVINELKA QKDRLLDYIN RYGDKVSPFQ
     LVKS
//