ID PCKG_ARTS2 Reviewed; 611 AA. AC A0JSP6; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 97. 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}; GN OrderedLocusNames=Arth_0667; OS Arthrobacter sp. (strain FB24). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Arthrobacter. OX NCBI_TaxID=290399; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FB24; RX PubMed=24501649; DOI=10.4056/sigs.4438185; RA Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T., RA Han C., Beasley F., Chen W., Konopka A., Xie G.; RT "Complete genome sequence of Arthrobacter sp. strain FB24."; RL Stand. Genomic Sci. 9:106-116(2013). 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000454; ABK02066.1; -; Genomic_DNA. DR RefSeq; WP_011690534.1; NC_008541.1. DR AlphaFoldDB; A0JSP6; -. DR SMR; A0JSP6; -. DR STRING; 290399.Arth_0667; -. DR KEGG; art:Arth_0667; -. DR eggNOG; COG1274; Bacteria. DR HOGENOM; CLU_028872_1_1_11; -. DR OrthoDB; 9758871at2; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000754; 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; 3.90.228.20; -; 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 (GTP)-RELATED; 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; Decarboxylase; Gluconeogenesis; GTP-binding; Lyase; Manganese; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1..611 FT /note="Phosphoenolpyruvate carboxykinase [GTP]" FT /id="PRO_1000072370" FT ACT_SITE 275 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 82 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 222..224 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 231 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 251 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 273 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 274..279 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 298 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 389..391 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 391 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 422 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 517..520 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" SQ SEQUENCE 611 AA; 67176 MW; 13FC3189846C263D CRC64; MGDLARLPLL EKAPTTHAGL LAWVEEVAEL TQPDRIHWVD GTEEEYTRLT GELVEAGTLT RLNPELFPNS FAAFSDPADV ARVEEQTFIC SENQRDAGFT NNWMAPAEMK QKLRGLFAGS MRGRTMYVIP FVMGHLDAED PKFGVEITDS AYVVASMRIM ANIGTEVLDK ITATNAFFVP ALHSLGAPLA PGQADVAWPC NPDKWIVHFP EERSIWSFGS GYGGNALLGK KCYALRIASV MARDEGWLAE HMLILKLTSP EKKSYYMSAA FPSACGKTNL ALLDPTIEGW EVETLGDDIT WMRIGKEGEL RATNPEAGLF GVAPGTGWGT NPNAMRAIAK GHSIFTNVAL TDDGGVWWEG MTEETPAHLT DWQGNSWTPD SDKPAAHPNS RFCTPISQID MLAEEYYSPE GVELSAILFG GRRKTTVPLV TQARSWTNGI FMGSTLSSET TAAAAGQVGV LRRDPMAMLP FIGYDAGDYL KHWISVSGKA NPERLPHIFL VNWFRRTADG DFAWPGFGDN ARVLKWAIER IEGKADAIET PIGFVPAGHA LDLTGLDLTH AHVEDAVRVD REEWDAELAS IEEWYAKFGD SLPEALRAEL DALKERMADH S //