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Phosphoenolpyruvate carboxykinase [GTP] (PEP carboxykinase) (PEPCK) (EC 4.1.1.32) (GTP-dependent phosphoenolpyruvate carboxykinase) (GTP-PEPCK)

 B7R284_9EURY            Unreviewed;       625 AA.
B7R284;
10-FEB-2009, integrated into UniProtKB/TrEMBL.
10-FEB-2009, sequence version 1.
28-FEB-2018, entry version 49.
RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000256|HAMAP-Rule:MF_00452};
Short=PEP carboxykinase {ECO:0000256|HAMAP-Rule:MF_00452};
Short=PEPCK {ECO:0000256|HAMAP-Rule:MF_00452};
EC=4.1.1.32 {ECO:0000256|HAMAP-Rule:MF_00452};
AltName: Full=GTP-dependent phosphoenolpyruvate carboxykinase {ECO:0000256|HAMAP-Rule:MF_00452};
Short=GTP-PEPCK {ECO:0000256|HAMAP-Rule:MF_00452};
Name=pckG {ECO:0000256|HAMAP-Rule:MF_00452};
ORFNames=TAM4_1562 {ECO:0000313|EMBL:EEB74195.1};
Thermococcus sp. AM4.
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Thermococcus.
NCBI_TaxID=246969 {ECO:0000313|EMBL:EEB74195.1, ECO:0000313|Proteomes:UP000009277};
[1] {ECO:0000313|EMBL:EEB74195.1, ECO:0000313|Proteomes:UP000009277}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AM4 {ECO:0000313|EMBL:EEB74195.1};
PubMed=22123768; DOI=10.1128/JB.06259-11;
Oger P., Sokolova T.G., Kozhevnikova D.A., Chernyh N.A.,
Bartlett D.H., Bonch-Osmolovskaya E.A., Lebedinsky A.V.;
"Complete Genome Sequence of the Hyperthermophilic Archaeon
Thermococcus sp. Strain AM4, Capable of Organotrophic Growth and
Growth at the Expense of Hydrogenogenic or Sulfidogenic Oxidation of
Carbon Monoxide.";
J. Bacteriol. 193:7019-7020(2011).
-!- FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to
phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic
pathway that produces glucose from lactate and other precursors
derived from the citric acid cycle. {ECO:0000256|HAMAP-
Rule:MF_00452}.
-!- CATALYTIC ACTIVITY: GTP + oxaloacetate = GDP + phosphoenolpyruvate
+ CO(2). {ECO:0000256|HAMAP-Rule:MF_00452}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|HAMAP-Rule:MF_00452};
Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_00452};
-!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
{ECO:0000256|HAMAP-Rule:MF_00452}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00452}.
-!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
family. {ECO:0000256|HAMAP-Rule:MF_00452}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00452}.
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EMBL; CP002952; EEB74195.1; -; Genomic_DNA.
RefSeq; WP_014122308.1; NC_016051.1.
STRING; 246969.TAM4_1562; -.
EnsemblBacteria; EEB74195; EEB74195; TAM4_1562.
GeneID; 7418920; -.
KEGG; tha:TAM4_1562; -.
eggNOG; arCOG05865; Archaea.
eggNOG; COG1274; LUCA.
KO; K01596; -.
OrthoDB; POG093Z01SN; -.
BioCyc; TSP246969:G1GNJ-1154-MONOMER; -.
UniPathway; UPA00138; -.
Proteomes; UP000009277; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:UniProtKB-UniRule.
GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
CDD; cd00819; PEPCK_GTP; 1.
Gene3D; 3.40.449.10; -; 2.
Gene3D; 3.90.228.20; -; 2.
HAMAP; MF_00452; PEPCK_GTP; 1.
InterPro; IPR018091; PEP_carboxykin_GTP_CS.
InterPro; IPR013035; PEP_carboxykinase_C.
InterPro; IPR008209; PEP_carboxykinase_GTP.
InterPro; IPR035077; PEP_carboxykinase_GTP_C.
InterPro; IPR035078; PEP_carboxykinase_GTP_N.
InterPro; IPR008210; PEP_carboxykinase_N.
PANTHER; PTHR11561; PTHR11561; 1.
Pfam; PF00821; PEPCK_C; 1.
Pfam; PF17297; PEPCK_N; 1.
PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
SUPFAM; SSF68923; SSF68923; 1.
PROSITE; PS00505; PEPCK_GTP; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000009277};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00452};
Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00452};
Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00452};
GTP-binding {ECO:0000256|HAMAP-Rule:MF_00452};
Kinase {ECO:0000313|EMBL:EEB74195.1};
Lyase {ECO:0000256|HAMAP-Rule:MF_00452};
Manganese {ECO:0000256|HAMAP-Rule:MF_00452};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00452};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00452};
Pyruvate {ECO:0000313|EMBL:EEB74195.1};
Transferase {ECO:0000313|EMBL:EEB74195.1}.
DOMAIN 30 239 PEPCK_N. {ECO:0000259|Pfam:PF17297}.
DOMAIN 244 606 PEPCK_C. {ECO:0000259|Pfam:PF00821}.
NP_BIND 271 276 GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
REGION 220 222 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00452}.
REGION 384 386 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00452}.
ACT_SITE 272 272 {ECO:0000256|HAMAP-Rule:MF_00452}.
METAL 229 229 Manganese. {ECO:0000256|HAMAP-
Rule:MF_00452}.
METAL 248 248 Manganese; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00452}.
METAL 289 289 Manganese. {ECO:0000256|HAMAP-
Rule:MF_00452}.
BINDING 86 86 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00452}.
BINDING 270 270 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00452}.
BINDING 386 386 GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
BINDING 418 418 GTP. {ECO:0000256|HAMAP-Rule:MF_00452}.
SEQUENCE 625 AA; 72255 MW; 9E3ACCE8D9042EA0 CRC64;
MEALDKLKEL LPEEQFEKVK AIDNPELHAF LAEWIEWLEP SKVFVCTDSE EDEHYVRWKA
LYYGEEKMLE TPNHTVHYDN YYDQARDKAN TKLLVPGGKE IPFLNTKDRD EGLKEIRELM
RGVMRGKELF ICFFVLGPKN SIFTIPAVQL TDSAYVAHSE FILYRKGYEE FKRLGRNAKF
FRFVHSAGEL DERKTSKNLD KRRIYIDLVD DTVYSVNTQY GGNTIGLKKL AFRLTIQKAV
KEGWLSEHMF LMRVNGPNGR KTYFTGAYPS MCGKTSTAMI PWENIVGDDL TFILPVNGVA
RGANVEKGVF GIIQGVNPED DPIIWKVLHS PVEIIFSNVL IKDGKPYWNE MGVEIPEEGE
NHSGKWWKGK TDKEGNEIPP SHKNARFTVS LEHFPNVDLE ALHNPCGVEV GGMIFGGRDK
DTWPPVREAF DWKHGVITMG ASLESETTAA TLGKEGVRAF NPMAILDFMS VPLGEYIENY
LRFGEKLRKT PKIFAVNYFL RDENGNWLNH KLDKAVWLKW MELRVHGDVD AIETPIGYIP
KYEDLARLFK EVLNKDYSRE AYEKQFTIRV PELLAKIERI EKIYREKVKE VPEELFRVLE
EERKRLLEAR EKYGDYISPF AFEGS


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