ID PCKG_MYCBP Reviewed; 606 AA. AC A1KF31; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 93. DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000303|PubMed:12855734}; DE Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000303|PubMed:12855734}; DE Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000303|PubMed:12855734}; DE EC=4.1.1.32 {ECO:0000255|HAMAP-Rule:MF_00452}; DE AltName: Full=GTP-dependent phosphoenolpyruvate carboxykinase {ECO:0000255|HAMAP-Rule:MF_00452}; DE Short=GTP-PEPCK {ECO:0000255|HAMAP-Rule:MF_00452}; GN Name=pckG {ECO:0000255|HAMAP-Rule:MF_00452}; GN OrderedLocusNames=BCG_0248; OS Mycobacterium bovis (strain BCG / Pasteur 1173P2). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=410289; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BCG / Pasteur 1173P2; RX PubMed=17372194; DOI=10.1073/pnas.0700869104; RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., RA Barrell B.G., Parkhill J., Cole S.T.; RT "Genome plasticity of BCG and impact on vaccine efficacy."; RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007). RN [2] RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION. RX PubMed=12855734; DOI=10.1099/mic.0.26234-0; RA Liu K., Yu J., Russell D.G.; RT "pckA-deficient Mycobacterium bovis BCG shows attenuated virulence in mice RT and in macrophages."; RL Microbiology 149:1829-1835(2003). CC -!- FUNCTION: Involved in the gluconeogenesis, in growth on fatty acids and CC is important for initiation of infection in the macrophages. Catalyzes CC the GTP-dependent 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:0000269|PubMed:12855734}. 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 -!- INDUCTION: Up-regulated by acetate or palmitate but down-regulated by CC glucose. {ECO:0000269|PubMed:12855734}. CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a reduction in the CC capacity to infect and survive in macrophages. Moreover, mice infected CC with this mutant are able to reduce the bacterial load much more CC effectively than mice infected with the parental wild-type bacteria. CC {ECO:0000269|PubMed:12855734}. 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; AM408590; CAL70232.1; -; Genomic_DNA. DR RefSeq; WP_003401212.1; NC_008769.1. DR AlphaFoldDB; A1KF31; -. DR SMR; A1KF31; -. DR KEGG; mbb:BCG_0248; -. DR HOGENOM; CLU_028872_1_1_11; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000001472; 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 2: Evidence at transcript level; KW Cytoplasm; Decarboxylase; Gluconeogenesis; GTP-binding; Lyase; Manganese; KW Metal-binding; Nucleotide-binding. FT CHAIN 1..606 FT /note="Phosphoenolpyruvate carboxykinase [GTP]" FT /id="PRO_1000060291" 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 606 AA; 67253 MW; AEE29412E6BCCAE3 CRC64; MTSATIPGLD TAPTNHQGLL SWVEEVAELT QPDRVVFTDG SEEEFQRLCD QLVEAGTFIR LNPEKHKNSY LALSDPSDVA RVESRTYICS AKEIDAGPTN NWMDPGEMRS IMKDLYRGCM RGRTMYVVPF CMGPLGAEDP KLGVEITDSE YVVVSMRTMT RMGKAALEKM GDDGFFVKAL HSVGAPLEPG QKDVAWPCSE TKYITHFPET REIWSYGSGY GGNALLGKKC YSLRIASAMA HDEGWLAEHM LILKLISPEN KAYYFAAAFP SACGKTNLAM LQPTIPGWRA ETLGDDIAWM RFGKDGRLYA VNPEFGFFGV APGTNWKSNP NAMRTIAAGN TVFTNVALTD DGDVWWEGLE GDPQHLIDWK GNDWYFRETE TNAAHPNSRY CTPMSQCPIL APEWDDPQGV PISGILFGGR RKTTVPLVTE ARDWQHGVFI GATLGSEQTA AAEGKVGNVR RDPMAMLPFL GYNVGDYFQH WINLGKHADE SKLPKVFFVN WFRRGDDGRF LWPGFGENSR VLKWIVDRIE HKAGGATTPI GTVPAVEDLD LDGLDVDAAD VAAALAVDAD EWRQELPLIE EWLQFVGEKL PTGVKDEFDA LKERLG //