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Entry: A0A345ZHX0_9GAMM
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ID   A0A345ZHX0_9GAMM        Unreviewed;       600 AA.
AC   A0A345ZHX0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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   ORFNames=DWG18_02930 {ECO:0000313|EMBL:AXK71345.1};
OS   Lysobacter sp. TY2-98.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=2290922 {ECO:0000313|EMBL:AXK71345.1, ECO:0000313|Proteomes:UP000254438};
RN   [1] {ECO:0000313|EMBL:AXK71345.1, ECO:0000313|Proteomes:UP000254438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TY2-98 {ECO:0000313|EMBL:AXK71345.1,
RC   ECO:0000313|Proteomes:UP000254438};
RA   Kim S.-G., Park A.-Y., Lee Y.-J.;
RT   "Lysobacter sp. nov. isolated from a farm soil.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00452};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00452};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00452};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00452}.
CC   -!- SUBUNIT: Monomer. {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|ARBA:ARBA00005796, ECO:0000256|HAMAP-
CC       Rule:MF_00452}.
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DR   EMBL; CP031413; AXK71345.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A345ZHX0; -.
DR   KEGG; lyt:DWG18_02930; -.
DR   OrthoDB; 9758871at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000254438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00819; PEPCK_GTP; 1.
DR   Gene3D; 3.90.228.20; -; 1.
DR   Gene3D; 3.40.449.10; Phosphoenolpyruvate Carboxykinase, domain 1; 1.
DR   Gene3D; 2.170.8.10; Phosphoenolpyruvate Carboxykinase, domain 2; 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; PHOSPHOENOLPYRUVATE CARBOXYKINASE; 1.
DR   PANTHER; PTHR11561:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE, CYTOSOLIC [GTP]; 1.
DR   Pfam; PF00821; PEPCK_GTP; 1.
DR   Pfam; PF17297; PEPCK_N; 1.
DR   PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR   SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR   SUPFAM; SSF53795; PEP carboxykinase-like; 1.
DR   PROSITE; PS00505; PEPCK_GTP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00452};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00452}; Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00452};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00452}; Kinase {ECO:0000313|EMBL:AXK71345.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00452};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00452};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00452};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00452}; Pyruvate {ECO:0000313|EMBL:AXK71345.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000254438};
KW   Transferase {ECO:0000313|EMBL:AXK71345.1}.
FT   DOMAIN          27..236
FT                   /note="Phosphoenolpyruvate carboxykinase GTP-utilising N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17297"
FT   DOMAIN          240..594
FT                   /note="Phosphoenolpyruvate carboxykinase C-terminal P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF00821"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         215..217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         224
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         244
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         267..272
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         295
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         382..384
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         384
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         415
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         508..511
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
SQ   SEQUENCE   600 AA;  66237 MW;  BFC01757F6818087 CRC64;
     MNALVQDVDK RTPEVQGRGT TLDSLRRWVD DVAALTRPDA IHWCDGSDAE NAALVAKMEK
     DGTLIRLNEQ TNPGSWLHRS HPDDVARVEH LTFVCTSNQD DAGPNNHWMA PADGHAQMDA
     LFDGCMEGRT LYVIPYCMGP IDSPISRCGV EITDSPYVVA NMRIMTRMGE AALQRIEREG
     TFVRGLHSTG ELDPNRRFIM HFPEELTIKS YGSGYGGNAL LGKKCHALRI ASHQARQEGW
     LAEHMLILGI ENPQGETHYI AAAFPSACGK TNLAMLIPPE GYRQDGWKVW TIGDDICWMR
     PGPDGRLYAI NPEAGFFGVA PGTSAKSNPN ALATIRKNTI FTNVGLTADG QPWWEGLDEG
     TPAFDWRGND YDFNKGPAAH PNARFTVSAK QCPSYSEHAE DPTGVPISAI VFGGRRASLV
     PLVFEARDWT HGVLVGAAMG SETTAAATGA VGVMRRDPMA MKPFCGYNFA DYFAHWLSFD
     NGQNKLPKVF HVNWFRKGDD GKFLWPGFGD NLRVLEWMIK RVEGQADATE TPIGALPREQ
     DLNLDGVQLS DESRAKLFGF DHAGWTTEFT SIGNYLREYG PRMPQALHEE QQRIAAMLGG
//
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