ID PCKA_BACLD Reviewed; 527 AA. AC Q65FV7; Q62RB5; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 111. 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=BLi03197, BL00839; OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=279010; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46; RX PubMed=15383718; DOI=10.1159/000079829; RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.; RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism RT with great industrial potential."; RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46; RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77; RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.; RT "Complete genome sequence of the industrial bacterium Bacillus RT licheniformis and comparisons with closely related Bacillus species."; RL Genome Biol. 5:R77.1-R77.12(2004). 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 -!- 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; AE017333; AAU42057.1; -; Genomic_DNA. DR EMBL; CP000002; AAU24695.1; -; Genomic_DNA. DR RefSeq; WP_003184588.1; NC_006322.1. DR AlphaFoldDB; Q65FV7; -. DR SMR; Q65FV7; -. DR STRING; 279010.BL00839; -. DR GeneID; 66214830; -. DR KEGG; bld:BLi03197; -. DR KEGG; bli:BL00839; -. DR eggNOG; COG1866; Bacteria. DR HOGENOM; CLU_018247_0_1_9; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000606; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; IEA:UniProtKB-UniRule. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule. 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 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. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Decarboxylase; Gluconeogenesis; Lyase; Manganese; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1..527 FT /note="Phosphoenolpyruvate carboxykinase (ATP)" FT /id="PRO_0000236919" FT BINDING 56 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 192 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 198 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 198 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 198 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 217 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 217 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 233..241 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 254 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 282 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 319 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 319 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" FT BINDING 444 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453" SQ SEQUENCE 527 AA; 58167 MW; BE2002BCB9FF58C0 CRC64; MNSVDLTTDL QTLLTGENVQ MNLSVPHLVE KILERKEGVL TSSGAVRATT GTYTGRSPKD KFIVEEASTK DKIDWGAVNQ PISEAAFDRL YAKVLGYLKE RDELYVFEGF AGADEKYRLP ITVVNEFAWH NLFARQLFIR PEEHDKKPEE QPFTILSAPH FKADPLVDGT RSETFIIVSF EKRTILIGGT EYAGEMKKSI FSIMNFLLPE QNILPMHCSA NIGEEGGTAL FFGLSGTGKT TLSADPKRKL IGDDEHGWSS TGVFNIEGGC YAKCINLSEE KEPQIYNAIR FGSVLENVVV DSKTGEPDYS DSFYTENTRA AYPIDAIDNI VKPSIAAHPQ TIVFLTADAF GVLPPISKLT KEQAMYHFLS GYTSKLAGTE RGITTPEATF STCFGSPFLP LPAHVYAEML GRKIDEHGVG VFLVNTGWTG GGYGTGERMS LAYTRAMVQA AIEGELDKAE MRTDRIFGLH SPVHVPGVPD QVLDPAKTWT DENEYEEKAI HLAKAFKQNF KKFSNTENIE KAGGPLV //