ID PCKG_MYCSJ Reviewed; 609 AA. AC A3PSV1; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 18-JUN-2025, entry version 103. 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=Mjls_0165; OS Mycobacterium sp. (strain JLS). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=164757; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JLS; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J., RA Sims R.C., Richardson P.; RT "Complete sequence of Mycobacterium sp. JLS."; RL Submitted (FEB-2007) 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:0000255|HAMAP-Rule:MF_00452}. CC -!- CATALYTIC ACTIVITY: CC Reaction=oxaloacetate + GTP = phosphoenolpyruvate + GDP + CO2; 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; CP000580; ABN95978.1; -; Genomic_DNA. DR AlphaFoldDB; A3PSV1; -. DR SMR; A3PSV1; -. DR KEGG; mjl:Mjls_0165; -. DR HOGENOM; CLU_028872_1_1_11; -. DR BioCyc; MSP164757:G1G8C-170-MONOMER; -. DR UniPathway; UPA00138; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0071333; P:cellular response to glucose stimulus; IEA:TreeGrafter. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule. DR GO; GO:0046327; P:glycerol biosynthetic process from pyruvate; IEA:TreeGrafter. DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:TreeGrafter. DR GO; GO:0019543; P:propionate catabolic process; IEA:TreeGrafter. DR GO; GO:0033993; P:response to lipid; IEA:TreeGrafter. DR GO; GO:0042594; P:response to starvation; IEA:TreeGrafter. DR CDD; cd00819; PEPCK_GTP; 1. DR FunFam; 3.40.449.10:FF:000005; Phosphoenolpyruvate carboxykinase [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 NCBIfam; NF003253; PRK04210.1; 1. 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. FT CHAIN 1..609 FT /note="Phosphoenolpyruvate carboxykinase [GTP]" FT /id="PRO_1000060293" FT ACT_SITE 273 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 81 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 220..222 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 229 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 249 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 271 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 272..277 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 296 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 387..389 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 389 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 420 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 515..518 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" SQ SEQUENCE 609 AA; 67822 MW; 9F7D9E191F37FA54 CRC64; MTSATIPGLD TAPTEHEGLL AWVREVAELT QPDRVVFTDG SEEECARLTE QLCEAGTFQK LNEEKKPNSY LALSDPSDVA RVESRTYICS EREIDAGPTN NWMDPAEMRG IMTDLYRGSM RGRTMYVVPF CMGPLEAEDP KLGVEITDSE YVVVSMRTMT RMGQAALDKM GTDGFFVKAL HSLGAPLEPG EKDVPWPCND TKYITHFPET REIWSYGSGY GGNALLGKKC YSLRIASAMA HDEGWLAEHM LILKLISPEN KAYFIAAAFP SACGKTNLAM LQPTIPGWRA ETVGDDIAWM RFGKDGRLYA VNPEFGFFGV APGTNWSSNP NAMKTIEAGN TVFTNVAKTD DGDVWWEGLE GEPDHLIDWK GNDYILRETE TKAAHPNSRY CTPISQCPTL APEWDDPQGV PISAILFGGR RKTTVPLITQ ARDWQHGVFI GATLGSEQTA AAEGKVGTVR RDPMAMLPFL GYNVGDYFQH WIDIGKNADE SKMPAVFFVN WFRRGDDGRF LWPGFGENSR VLKWAIERIE HKADGRSTPI GIVPTAQDLD LEGLDVDPED VDAALAVKPE EWRQELPLIE EWFEFVGEKL PTGIRDEFDA LKHRLAEEA //