ID PCKG_ACIBT Reviewed; 611 AA. AC A3M840; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 2. DT 27-MAR-2024, entry version 89. 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=A1S_2668; OS Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC OS KC755 / 5377). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=400667; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377; RX PubMed=17344419; DOI=10.1101/gad.1510307; RA Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., RA Gerstein M., Snyder M.; RT "New insights into Acinetobacter baumannii pathogenesis revealed by high- RT density pyrosequencing and transposon mutagenesis."; RL Genes Dev. 21:601-614(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; CP000521; ABO13084.2; -; Genomic_DNA. DR AlphaFoldDB; A3M840; -. DR SMR; A3M840; -. DR KEGG; acb:A1S_2668; -. DR HOGENOM; CLU_028872_1_1_6; -. DR UniPathway; UPA00138; -. 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..611 FT /note="Phosphoenolpyruvate carboxykinase [GTP]" FT /id="PRO_1000125041" FT ACT_SITE 269 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 77 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 216..218 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 225 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 245 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 267 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 268..273 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 294 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 382..384 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 384 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452" FT BINDING 415 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 611 AA; 67530 MW; 35BAC9B5834E03C9 CRC64; MTTVNAPEFV RHPKLIAWVE EIANLTKPAK IEWCDGSEEE YQRLIDLMIA NGTMQKLNQE KHPGSYLANS DPSDVARVED RTYICSQNKE DAGATNNWED PAVMREKLNG LFEGSMKGRT MYVVPFSMGP LGSHIAHIGI ELTDSPYVAV SMRKMARMGK AVYDVLGTDG EFVPCVHTVG TPLAEGQKDV AWPCNPEKYI VHYPETREIW SFGSGYGGNA LLGKKCLALR IASVMGREQG WLAEHMLILG VTNPQGEKHY IAAAFPSACG KTNFAMLIPP AGYEGWKIET VGDDIAWIKP GEDGRLYAIN PEAGFFGVAP GTNTKTNPNC MATLHKDVIY TNVAVTDDGQ VWWEGLSKEV PANLTNWKGQ PHVNGEKAAH PNARFTVAAG QCPSIDADWE NPAGVPISAF IFGGRRADTV PLVSEAFDWV DGVYKAATMG SETTAAAVGQ QGIVRRDPFA MLPFAGYNMA DYFDHWLNLG AKVSEKAEAS GNKLPKIFNV NWFRRDAEGN FVWPGFGQNM RVLEWIIDRC EGRANAVETP IGFVPTYEDL NWEGTEFTKE QFDLITNQDK DQWVTEIESH TELFNKLGER LPKALKERQA ALLEAVKLAS N //