PCKG_RALSO
ID PCKG_RALSO Reviewed; 622 AA.
AC Q8Y3G3;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=pckA;
GN OrderedLocusNames=RSc0017; ORFNames=RS01839;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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 derived
CC from the citric acid cycle. {ECO:0000255|HAMAP-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; EC=4.1.1.32;
CC 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-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}.
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DR EMBL; AL646052; CAD13545.1; -; Genomic_DNA.
DR RefSeq; WP_010999984.1; NC_003295.1.
DR AlphaFoldDB; Q8Y3G3; -.
DR SMR; Q8Y3G3; -.
DR STRING; 267608.RSc0017; -.
DR EnsemblBacteria; CAD13545; CAD13545; RSc0017.
DR GeneID; 60499525; -.
DR KEGG; rso:RSc0017; -.
DR eggNOG; COG1274; Bacteria.
DR HOGENOM; CLU_028872_1_1_4; -.
DR OMA; GPTNNWV; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001436; 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;
KW Cytoplasm; Decarboxylase; Gluconeogenesis; GTP-binding; Lyase; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..622
FT /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT /id="PRO_0000103613"
FT REGION 395..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 277
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 224..226
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 233
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 276..281
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 302
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 400..402
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 402
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 433
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 530..533
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
SQ SEQUENCE 622 AA; 68462 MW; 6E6E16F6E90A61FE CRC64;
MNQPVMQGVP ALNVPAYVKH ARLVAWVSEI AALTKPERVV WCDGSQEEYD RLCAEMVAAG
TLKQLNPAKR KNSYLALSDP SDVARVEDRT FICSQKQEDA GPTNNWTAPA EMRQTLNGLF
DGCMRGRTLY VVPFSMGPLG SPIAHIGVEL SDSPYVAVNM RIMTRMGRAV YDVLGADGEF
VPCVHTVGKP LAAGEQDVPW PCNPTKYIVH FPETREIWSF GSGYGGNALL GKKCFALRIA
STMGRDQGWL AEHMLILGVT SPEGKTYHVA AAFPSACGKT NFAMLIPPAG FDGWKVTTIG
DDIAWIKPRQ DANGQTRLYA INPEAGFFGV APGTGEKTNF NAMATLKENV IFTNVALTDD
GDVWWEGMTD TPPAHLTDWQ GQDWTPAIAK ETGRKAAHPN SRFTAPAAQC PSIDPEWDNP
AGVAIDAFIF GGRRSTTVPL VTEARDWTEG VYMAATMGSE TTAAAVGQQG VVRRDPFAML
PFCGYNMADY FAHWLKLGDQ LAKSGAELPK IFCVNWFRKD EQGRFVWPGF GENMRVLKWM
IDRIEGQARG DEHVFGVSPR YEELRWDGLD FSAEQFAKVI SLDAQAWQQE LTLHAELFAQ
LAHHLPQALP EAKARLEARL QG
