ID PCKG_COREF Reviewed; 612 AA. AC Q8FM16; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 2. DT 27-MAR-2024, entry version 120. 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=pck; GN OrderedLocusNames=CE2691; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 OS / NBRC 100395). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). 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 -!- SEQUENCE CAUTION: CC Sequence=BAC19501.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; BA000035; BAC19501.1; ALT_INIT; Genomic_DNA. DR AlphaFoldDB; Q8FM16; -. DR SMR; Q8FM16; -. DR STRING; 196164.gene:10743139; -. DR KEGG; cef:CE2691; -. DR eggNOG; COG1274; Bacteria. DR HOGENOM; CLU_028872_1_1_11; -. DR OrthoDB; 9758871at2; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000001409; 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..612 FT /note="Phosphoenolpyruvate carboxykinase [GTP]" FT /id="PRO_0000103602" FT ACT_SITE 274 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 82 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 221..223 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 230 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 250 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 272 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 273..278 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 297 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 388..390 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 390 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 421 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 516..519 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" SQ SEQUENCE 612 AA; 67642 MW; D9A27B4ED0521148 CRC64; MTTAAIPGLQ GEAPTNNQEL LNWIAEAVEL FQPEAVVFAD GSQEEWDRMA EELVEAGTLI RLNEEKRPNS FLARSNPSDV ARVESRTFIC SENQEDAGPT NNWAPPQAMK EEMTEVYRGS MKGRTMYVVP FCMGPITDPE PKLGVQLTDS AYVVMSMRIM TRMGKDALDK IGENGSFVRC LHSVGAPLEE GQEDVAWPCN DTKYITQFPE TKEIWSYGSG YGGNAILAKK CYALRIASVM AREEGWMAEH MLILKLTNPE GQAYHIAAAF PSACGKTNLA MITPTIPGWK AEVVGDDIAW LKFREDGHLY AVNPENGFFG VAPGTNYASN PIAMQTMEPG NTLFTNVALT DDGDIWWEGM DGDAPEHLID WKGNDWTPES NQPAAHPNSR YCVAIEQCPT AAPEFNDWKG VKVDAILFGG RRPDTVPLVT QTHDWEHGTM VGALLASGQT AASAEAKVGT LRHDPMAMLP FMGYNAGEYL QNWIDMGNKG GDKMPSIFLV NWFRRGEDGR FLWPGFGENS RVLKWVIDRI EGRVGAEETV VGYTARAEDL DLEGLDTPIE DIREALTAPA EQWAADLEDN AEYLTFLGPK VPTEVHEQFE ALKKRIQAAQ AS //