ID PCKG_CORGB Reviewed; 610 AA. AC A4QHQ4; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 90. 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=cgR_2751; OS Corynebacterium glutamicum (strain R). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=340322; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R; RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0; RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.; RT "Comparative analysis of the Corynebacterium glutamicum group and complete RT genome sequence of strain R."; RL Microbiology 153:1042-1058(2007). 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; AP009044; BAF55770.1; -; Genomic_DNA. DR RefSeq; WP_003857887.1; NC_009342.1. DR AlphaFoldDB; A4QHQ4; -. DR SMR; A4QHQ4; -. DR GeneID; 69623143; -. DR KEGG; cgt:cgR_2751; -. DR HOGENOM; CLU_028872_1_1_11; -. DR PhylomeDB; A4QHQ4; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000006698; 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. FT CHAIN 1..610 FT /note="Phosphoenolpyruvate carboxykinase [GTP]" FT /id="PRO_1000060288" 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 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 610 AA; 66861 MW; 7958DBA2E99B0F30 CRC64; MTTAAIRGLQ GEAPTKNKEL LNWIADAVEL FQPEAVVFVD GSQAEWDRMA EDLVEAGTLI KLNEEKRPNS YLARSNPSDV ARVESRTFIC SEKEEDAGPT NNWAPPQAMK DEMSKHYAGS MKGRTMYVVP FCMGPISDPD PKLGVQLTDS EYVVMSMRIM TRMGIEALDK IGANGSFVKC LHSVGAPLEP GQEDVAWPCN DTKYITQFPE TKEIWSYGSG YGGNAILAKK CYALRIASVM AREEGWMAEH MLILKLINPE GKAYHIAAAF PSACGKTNLA MITPTIPGWT AQVVGDDIAW LKLREDGLYA VNPENGFFGV APGTNYASNP IAMKTMEPGN TLFTNVALTD DGDIWWEGMD GDAPAHLIDW KGNDWTPESD ENAAHPNSRY CVAIDQSPAA APEFNDWEGV KIDAILFGGR RADTVPLVTQ TYDWEHGTMV GALLASGQTA ASAEAKVGTL RHDPMAMLPF IGYNAGEYLQ NWIDMGNKGG DKMPSIFLVN WFRRGEDGRF LWPGFGDNSR VLKWVIDRIE GRVGADETVV GHTAKAEDLD LDGLDTPIED VKEALTAPAE QWANDVQDNA EYLTFLGPRV PAEVHSQFDA LKARISAAHA //