ID PCKG_MYCUA Reviewed; 609 AA. AC A0PMX1; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, 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=MUL_1101; OS Mycobacterium ulcerans (strain Agy99). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium ulcerans group. OX NCBI_TaxID=362242; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Agy99; RX PubMed=17210928; DOI=10.1101/gr.5942807; RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M., RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.; RT "Reductive evolution and niche adaptation inferred from the genome of RT Mycobacterium ulcerans, the causative agent of Buruli ulcer."; RL Genome Res. 17:192-200(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; CP000325; ABL03690.1; -; Genomic_DNA. DR RefSeq; WP_011739312.1; NC_008611.1. DR AlphaFoldDB; A0PMX1; -. DR SMR; A0PMX1; -. DR KEGG; mul:MUL_1101; -. DR eggNOG; COG1274; Bacteria. DR HOGENOM; CLU_028872_1_1_11; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000765; 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..609 FT /note="Phosphoenolpyruvate carboxykinase [GTP]" FT /id="PRO_1000060297" 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; 67846 MW; 9D4A019065B6CF75 CRC64; MTSATIPGLD TAPTNHQGLL SWVQEVAELT QPDRVVFADG SDEEFHRLSA QLVDAGTFTR LNDEKFPNSY LALSDPSDVA RVESRTFICS EREIDAGPTN NWMNPSEMRT LMTDLYRGCM RGRTMYVVPF CMGPLGAEDP KLGVEITDSE YVVVSMKVMT RMGTAALEKM GQDGFFVKAL HSVGAPLEDG QADVPWPCSD TKYITHFPET REIWSYGSGY GGNALLGKKC YSLRIASAMA RDEGWLAEHM LILKLISPEN KAYYIAAAFP SACGKTNLAM LQPTIPGWRA ETLGDDIAWM RFGKDGRLYA VNPEFGFFGV APGTNWKSNP NAMRTIAAGN TVFTNVALTD DGEVWWEGLE GDPQHLVDWK GNEWYFRETE TTAAHPNSRY CTPMSQCPIL APEWDDPQGV PISAILFGGR RKTTVPLVTQ ARDWQHGVFI GATLGSEQTA AAEGKVGNVR RDPMAMLPFM GYNVGDYVQH WIDIGKNSDE SKLPQVFFVN WFRRGEDHRF LWPGFGENSR VMKWIVDRIE HKAGGKTTPI GTVPTVEDLD LEGLDANPAD VSEALAVNAQ EWREELPLIE EWLQFIGEKL PTGIKDEFDA LKERLRDAE //