ID PCKA_VIBCH Reviewed; 542 AA. AC Q9KNK0; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2003, sequence version 3. DT 27-MAR-2024, entry version 124. DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000255|HAMAP-Rule:MF_00453}; DE Short=PCK {ECO:0000255|HAMAP-Rule:MF_00453}; DE Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00453}; DE Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00453}; DE EC=4.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00453}; GN Name=pckA {ECO:0000255|HAMAP-Rule:MF_00453}; GN OrderedLocusNames=VC_2738; OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=243277; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39315 / El Tor Inaba N16961; RX PubMed=10952301; DOI=10.1038/35020000; RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A., RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.; RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio RT cholerae."; RL Nature 406:477-483(2000). CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the conversion of CC oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct CC phosphoryl transfer between the nucleoside triphosphate and OAA. CC {ECO:0000255|HAMAP-Rule:MF_00453}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate; CC Xref=Rhea:RHEA:18617, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; CC EC=4.1.1.49; Evidence={ECO:0000255|HAMAP-Rule:MF_00453}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00453}; CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00453}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|HAMAP-Rule:MF_00453}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00453}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00453}. CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP) CC family. {ECO:0000255|HAMAP-Rule:MF_00453}. 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; AE003852; AAF95877.1; -; Genomic_DNA. DR PIR; B82039; B82039. DR RefSeq; NP_232364.1; NC_002505.1. DR RefSeq; WP_000217613.1; NZ_LT906614.1. DR AlphaFoldDB; Q9KNK0; -. DR SMR; Q9KNK0; -. DR STRING; 243277.VC_2738; -. DR DNASU; 2614901; -. DR EnsemblBacteria; AAF95877; AAF95877; VC_2738. DR GeneID; 69718668; -. DR KEGG; vch:VC_2738; -. DR PATRIC; fig|243277.26.peg.2613; -. DR eggNOG; COG1866; Bacteria. DR HOGENOM; CLU_018247_0_1_6; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000584; Chromosome 1. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IBA:GO_Central. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR CDD; cd00484; PEPCK_ATP; 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_00453; PEPCK_ATP; 1. DR InterPro; IPR001272; PEP_carboxykinase_ATP. DR InterPro; IPR013035; PEP_carboxykinase_C. DR InterPro; IPR008210; PEP_carboxykinase_N. DR InterPro; IPR015994; PEPCK_ATP_CS. DR NCBIfam; TIGR00224; pckA; 1. DR PANTHER; PTHR30031:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE (ATP); 1. DR PANTHER; PTHR30031; PHOSPHOENOLPYRUVATE CARBOXYKINASE ATP; 1. DR Pfam; PF01293; PEPCK_ATP; 1. DR PIRSF; PIRSF006294; PEP_crbxkin; 1. DR SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1. DR SUPFAM; SSF53795; PEP carboxykinase-like; 1. DR PROSITE; PS00532; PEPCK_ATP; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Decarboxylase; Gluconeogenesis; Lyase; Manganese; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1..542 FT /note="Phosphoenolpyruvate carboxykinase (ATP)" FT /id="PRO_0000203854" FT BINDING 67 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 208 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 214 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 214 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 214 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 233 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 233 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 249..257 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 270 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 298 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 334 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 334 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 450..451 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 456 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" SQ SEQUENCE 542 AA; 59844 MW; 3162609A820D8D14 CRC64; MTVMEHTKAA QIDLAQYGIT GVTELVRNPS YEMLFAEETR SDLEGYERGV VTELGAVAVD TGIFTGRSPK DKFIVKDDTT RDTLWWTSDK AKNDNKPINQ EVWNDLKALV TKQLSGKRVF VLDGYCGANA DTRLSVRFIT EVAWQAHFVK NMFIRPSEEE LAHFKPDFVV MNGAKCTNAK WKEHGLNSEN FTVFNLTERM QLIGGTWYGG EMKKGMFAMM NYFLPLQGIA SMHCSANMGK AGDVAIFFGL SGTGKTTLST DPKRALIGDD EHGWDDDGVF NFEGGCYAKT IKLSKEAEPD IYNAIRRDAL LENVTVRSDG SIDFDDGSKT ENTRVSYPIY HIDNIVKPVS KGGHATKVIF LSADAFGVLP PVSKLTPEQT KYHFLSGFTA KLAGTERGIT EPTPTFSACF GAAFLTLHPT QYAEVLVKRM EAAGAEAYLV NTGWNGSGKR ISIKDTRGII DAILDGSIEK AETKHIPIFN LQVPTALPGV DPMILDPRDT YVDPLQWESK AKDLATRFIN NFDKYTDNAE GKALVAAGPK LD //