(data stored in ACNUC7421 zone)

SWISSPROT: C4KDU0_SULIK

ID   C4KDU0_SULIK            Unreviewed;       604 AA.
AC   C4KDU0;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   05-JUL-2017, entry version 51.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000256|HAMAP-Rule:MF_00452};
DE            Short=PEP carboxykinase {ECO:0000256|HAMAP-Rule:MF_00452};
DE            Short=PEPCK {ECO:0000256|HAMAP-Rule:MF_00452};
DE            EC=4.1.1.32 {ECO:0000256|HAMAP-Rule:MF_00452};
DE   AltName: Full=GTP-dependent phosphoenolpyruvate carboxykinase {ECO:0000256|HAMAP-Rule:MF_00452};
DE            Short=GTP-PEPCK {ECO:0000256|HAMAP-Rule:MF_00452};
GN   Name=pckG {ECO:0000256|HAMAP-Rule:MF_00452};
GN   OrderedLocusNames=M164_0433 {ECO:0000313|EMBL:ACR41063.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR41063.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR41063.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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:0000256|HAMAP-
CC       Rule:MF_00452}.
CC   -!- CATALYTIC ACTIVITY: GTP + oxaloacetate = GDP + phosphoenolpyruvate
CC       + CO(2). {ECO:0000256|HAMAP-Rule:MF_00452}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00452};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00452};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00452}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00452}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family. {ECO:0000256|HAMAP-Rule:MF_00452}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00452}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001402; ACR41063.1; -; Genomic_DNA.
DR   RefSeq; WP_012718407.1; NC_012726.1.
DR   EnsemblBacteria; ACR41063; ACR41063; M164_0433.
DR   GeneID; 7812316; -.
DR   KEGG; sid:M164_0433; -.
DR   HOGENOM; HOG000191700; -.
DR   KO; K01596; -.
DR   OMA; GPTNNWV; -.
DR   OrthoDB; POG093Z01SN; -.
DR   BioCyc; SISL426118:GI01-438-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; -; 1.
DR   HAMAP; MF_00452; PEPCK_GTP; 1.
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_C; 1.
DR   Pfam; PF17297; PEPCK_N; 1.
DR   PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR   SUPFAM; SSF68923; SSF68923; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KDU0.
DR   SWISS-2DPAGE; C4KDU0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00452};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00452};
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00452};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00452};
KW   Kinase {ECO:0000313|EMBL:ACR41063.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00452, ECO:0000313|EMBL:ACR41063.1};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00452};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00452};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00452};
KW   Pyruvate {ECO:0000313|EMBL:ACR41063.1};
KW   Transferase {ECO:0000313|EMBL:ACR41063.1}.
FT   DOMAIN       30    228       PEPCK_N. {ECO:0000259|Pfam:PF17297}.
FT   DOMAIN      233    585       PEPCK_C. {ECO:0000259|Pfam:PF00821}.
FT   NP_BIND     259    264       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   REGION      209    211       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00452}.
FT   REGION      365    367       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00452}.
FT   ACT_SITE    260    260       {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   METAL       218    218       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   METAL       237    237       Manganese; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   METAL       275    275       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING      87     87       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING     258    258       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00452}.
FT   BINDING     367    367       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
FT   BINDING     398    398       GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
SQ   SEQUENCE   604 AA;  69144 MW;  663A7285AAA25241 CRC64;
     MKVSLDFLND LVNGDSVKKL ESLNNYRLIE FLSNVVKLCE PDSVYLITGR NEEKEYIRKK
     ALERGEEIKL KTSGHTIHFD HPLDQARARE DTFILTDSKI PYVNTKPRNE GLNEILGLLK
     GSMRGREMYV GFYSLGPRNS PFQILAVQVT DSPYVIHSEN ILYRNAFGDF NNNKQFLRFV
     HSKGELDIRK RRIMIDLADN TVYSINTTYA GNSVGLKKLA LRLTITKAAE EGWLSEHMAI
     IGFNGDKGIH YFTASFPSGS GKTSTSMIGS LISDDLAFIR EFDGFPKAVN PEIGVFGIIQ
     GINARDDPII WEVLHKSGEV IFSNVLMTED GDVYWEGSEL PKPERGYNYE GKWIRESGKP
     ASHPNARFTV PLTSFKNLDG NWDNPNGVVI DGIIFGVRDY STLIPVVEAF SWSHGVATIG
     ASMESARTSA VIGKSDELEF NPMAILDFMP ISLSRYLRNY LNFGKRLRRS PKIFGFNYFL
     KDENNKFLNS KEDKRIWVSW AVKRVEETTD AIYTPIGFIP FYEDLKALYK RVLGREYSKE
     EYEKQFKIKL KRYLEKTDRI IGIYLKFDDI PSEIISELEM QRKRIIDYIS KYGDSVSPFR
     LEKT
//

If you have problems or comments...

PBIL Back to PBIL home page