ID PCKA_ECOLI Reviewed; 540 AA. AC P22259; Q2M768; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 24-JAN-2024, entry version 199. 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}; Synonyms=pck; GN OrderedLocusNames=b3403, JW3366; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, RP ACTIVITY REGULATION, COFACTOR, AND SUBUNIT. RC STRAIN=K12; RX PubMed=1701430; DOI=10.1128/jb.172.12.7151-7156.1990; RA Medina V., Pontarollo R., Glaeske D., Tabel H., Goldie H.; RT "Sequence of the pckA gene of Escherichia coli K-12: relevance to genetic RT and allosteric regulation and homology of E. coli phosphoenolpyruvate RT carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces RT cerevisiae."; RL J. Bacteriol. 172:7151-7156(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 439-540. RX PubMed=6292200; DOI=10.1016/s0021-9258(18)33502-6; RA Mizuno T., Wurtzel E.T., Inouye M.; RT "Osmoregulation of gene expression. II. DNA sequence of the envZ gene of RT the ompB operon of Escherichia coli and characterization of its gene RT product."; RL J. Biol. Chem. 257:13692-13698(1982). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39. RC STRAIN=K12; RX PubMed=8577250; DOI=10.1111/j.1365-2958.1995.tb02339.x; RA Ramseier T.M., Bledig S., Michotey V., Feghali R., Saier M.H. Jr.; RT "The global regulatory protein FruR modulates the direction of carbon flow RT in Escherichia coli."; RL Mol. Microbiol. 16:1157-1169(1995). RN [6] RP PROTEIN SEQUENCE OF 242-290, AND MUTAGENESIS OF ASP-268 AND GLY-284. RX PubMed=7883719; DOI=10.1128/jb.177.6.1620-1623.1995; RA Hou S.-Y., Chao Y.-P., Liao J.C.; RT "A mutant phosphoenolpyruvate carboxykinase in Escherichia coli conferring RT oxaloacetate decarboxylase activity."; RL J. Bacteriol. 177:1620-1623(1995). RN [7] RP PROTEIN SEQUENCE OF 1-12. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND SUBUNIT. RX PubMed=6986370; DOI=10.1016/s0021-9258(19)86044-1; RA Goldie A.H., Sanwal B.D.; RT "Allosteric control by calcium and mechanism of desensitization of RT phosphoenolpyruvate carboxykinase of Escherichia coli."; RL J. Biol. Chem. 255:1399-1405(1980). RN [9] RP INDUCTION. RX PubMed=6434512; DOI=10.1128/jb.159.3.832-836.1984; RA Goldie H.; RT "Regulation of transcription of the Escherichia coli phosphoenolpyruvate RT carboxykinase locus: studies with pck-lacZ operon fusions."; RL J. Bacteriol. 159:832-836(1984). RN [10] RP FUNCTION IN GLUCONEOGENESIS. RX PubMed=8226637; DOI=10.1128/jb.175.21.6939-6944.1993; RA Chao Y.P., Patnaik R., Roof W.D., Young R.F., Liao J.C.; RT "Control of gluconeogenic growth by pps and pck in Escherichia coli."; RL J. Bacteriol. 175:6939-6944(1993). RN [11] RP INDUCTION. RX PubMed=8393005; DOI=10.1128/jb.175.15.4744-4755.1993; RA Romeo T., Gong M., Liu M.-Y., Brun-Zinkernagel A.-M.; RT "Identification and molecular characterization of csrA, a pleiotropic gene RT from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, RT cell size, and surface properties."; RL J. Bacteriol. 175:4744-4755(1993). RN [12] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87 AND LYS-523, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076; RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200; RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., RA Grishin N.V., Zhao Y.; RT "Lysine acetylation is a highly abundant and evolutionarily conserved RT modification in Escherichia coli."; RL Mol. Cell. Proteomics 8:215-225(2009). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-538, ACTIVITY REGULATION, AND RP MASS SPECTROMETRY. RX PubMed=8609605; DOI=10.1006/jmbi.1996.0072; RA Matte A., Goldie H., Sweet R.M., Delbaere L.T.J.; RT "Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a RT new structural family with the P-loop nucleoside triphosphate hydrolase RT fold."; RL J. Mol. Biol. 256:126-143(1996). RN [15] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ATP AND SUBSTRATE RP ANALOGS, AND REACTION MECHANISM. RX PubMed=8599762; DOI=10.1038/nsb0496-355; RA Tari L.W., Matte A., Pugazhenthi U., Goldie H., Delbaere L.T.J.; RT "Snapshot of an enzyme reaction intermediate in the structure of the ATP- RT Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase."; RL Nat. Struct. Biol. 3:355-363(1996). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ATP, MANGANESE AND RP SUBSTRATE, COFACTOR, AND SUBUNIT. RX PubMed=9406547; DOI=10.1038/nsb1297-990; RA Tari L.W., Matte A., Goldie H., Delbaere L.T.; RT "Mg(2+)-Mn(2+) clusters in enzyme-catalyzed phosphoryl-transfer RT reactions."; RL Nat. Struct. Biol. 4:990-994(1997). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ATP ANALOGS AND RP SUBSTRATE, AND REACTION MECHANISM. RX PubMed=11724534; DOI=10.1006/jmbi.2001.5120; RA Sudom A.M., Prasad L., Goldie H., Delbaere L.T.; RT "The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate RT carboxykinase from the use of AlF(3)."; RL J. Mol. Biol. 314:83-92(2001). RN [18] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ATP, CALCIUM AND RP SUBSTRATE, ACTIVITY REGULATION, REACTION MECHANISM, AND SUBUNIT. RX PubMed=12837799; DOI=10.1128/jb.185.14.4233-4242.2003; RA Sudom A., Walters R., Pastushok L., Goldie D., Prasad L., Delbaere L.T., RA Goldie H.; RT "Mechanisms of activation of phosphoenolpyruvate carboxykinase from RT Escherichia coli by Ca2+ and of desensitization by trypsin."; RL J. Bacteriol. 185:4233-4242(2003). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ATP, MANGANESE AND RP SUBSTRATE ANALOGS, MUTAGENESIS OF ARG-65, COFACTOR, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=17475535; DOI=10.1016/j.biocel.2007.03.015; RA Cotelesage J.J., Puttick J., Goldie H., Rajabi B., Novakovski B., RA Delbaere L.T.; RT "How does an enzyme recognize CO2?"; RL Int. J. Biochem. Cell Biol. 39:1204-1210(2007). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEX WITH ATP, MANGANESE AND RP SUBSTRATE ANALOGS, AND COFACTOR. RA Delbaere L.T.J., Cotelesage J.J.H., Goldie H.; RT "Crystal structure of E. coli phosphoenolpyruvate carboxykinase (PEPCK) RT complexed with ATP, Mg2+, Mn2+, carbon dioxide and oxaloacetate."; RL Submitted (MAY-2007) to the PDB data bank. RN [21] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ATP AND MANGANESE, RP AND COFACTOR. RA Delbaere L.T.J., Cotelesage J.J.H., Goldie H.; RT "Crystal structure of E. coli phosphoenolpyruvate carboxykinase mutant RT Lys213Ser."; RL Submitted (MAY-2007) to the PDB data bank. 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, ECO:0000269|PubMed:1701430, CC ECO:0000269|PubMed:6986370, ECO:0000269|PubMed:8226637}. 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 ECO:0000269|PubMed:6986370}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00453, ECO:0000269|PubMed:1701430, CC ECO:0000269|PubMed:17475535, ECO:0000269|PubMed:9406547, CC ECO:0000269|Ref.20, ECO:0000269|Ref.21}; CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00453, CC ECO:0000269|PubMed:1701430, ECO:0000269|PubMed:17475535, CC ECO:0000269|PubMed:9406547, ECO:0000269|Ref.20, ECO:0000269|Ref.21}; CC -!- ACTIVITY REGULATION: Allosterically activated by calcium. It may CC represent the only case of a monomeric, allosteric enzyme. CC {ECO:0000269|PubMed:12837799, ECO:0000269|PubMed:1701430, CC ECO:0000269|PubMed:6986370, ECO:0000269|PubMed:8609605}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.8 uM for manganese (at 31 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:17475535, ECO:0000269|PubMed:6986370}; CC KM=0.11 mM for calcium (at 31 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:17475535, ECO:0000269|PubMed:6986370}; CC KM=0.31 mM for OAA (at 31 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:17475535, ECO:0000269|PubMed:6986370}; CC KM=0.51 mM for OAA (at pH 7.5) {ECO:0000269|PubMed:17475535, CC ECO:0000269|PubMed:6986370}; CC KM=1.4 mM for magnesium (at 31 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:17475535, ECO:0000269|PubMed:6986370}; CC KM=11 mM for PEP (at pH 7.5) {ECO:0000269|PubMed:17475535, CC ECO:0000269|PubMed:6986370}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|HAMAP-Rule:MF_00453}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00453, CC ECO:0000269|PubMed:11724534, ECO:0000269|PubMed:12837799, CC ECO:0000269|PubMed:1701430, ECO:0000269|PubMed:17475535, CC ECO:0000269|PubMed:6986370, ECO:0000269|PubMed:8599762, CC ECO:0000269|PubMed:9406547, ECO:0000269|Ref.20, ECO:0000269|Ref.21}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: Induced upon entry into stationary phase and by cyclic AMP CC (cAMP). Repressed by glucose (catabolite repression) and by CsrA. CC {ECO:0000269|PubMed:6434512, ECO:0000269|PubMed:8393005}. CC -!- MASS SPECTROMETRY: Mass=59656; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:8609605}; CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP) CC family. {ECO:0000255|HAMAP-Rule:MF_00453}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA24301.1; Type=Frameshift; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; 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; M59823; AAA24301.1; ALT_FRAME; Genomic_DNA. DR EMBL; U18997; AAA58200.1; -; Genomic_DNA. DR EMBL; U00096; AAC76428.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77888.1; -; Genomic_DNA. DR EMBL; J01656; -; NOT_ANNOTATED_CDS; Unassigned_RNA. DR EMBL; S76268; AAB33745.2; -; Genomic_DNA. DR EMBL; S76269; AAB33746.2; -; Genomic_DNA. DR EMBL; U21325; AAA95999.1; -; Genomic_DNA. DR PIR; F65135; F65135. DR RefSeq; NP_417862.1; NC_000913.3. DR RefSeq; WP_001265681.1; NZ_STEB01000004.1. DR PDB; 1AQ2; X-ray; 1.90 A; A=1-540. DR PDB; 1AYL; X-ray; 1.80 A; A=1-540. DR PDB; 1K3C; X-ray; 2.00 A; A=1-540. DR PDB; 1K3D; X-ray; 2.00 A; A=1-540. DR PDB; 1OEN; X-ray; 1.90 A; A=1-538. DR PDB; 1OS1; X-ray; 1.80 A; A=1-540. DR PDB; 2OLQ; X-ray; 1.94 A; A=1-540. DR PDB; 2OLR; X-ray; 1.60 A; A=1-540. DR PDB; 2PXZ; X-ray; 2.23 A; X=1-540. DR PDB; 2PY7; X-ray; 2.20 A; X=1-540. DR PDB; 6ASI; X-ray; 1.79 A; A=1-540. DR PDB; 6ASM; X-ray; 1.55 A; A=1-540. DR PDB; 6ASN; X-ray; 1.55 A; A=1-540. DR PDB; 6AT2; X-ray; 1.44 A; A=1-540. DR PDB; 6AT3; X-ray; 1.46 A; A/B=1-540. DR PDB; 6AT4; X-ray; 1.33 A; A/B=1-540. DR PDB; 6COM; X-ray; 2.30 A; A=1-540. DR PDB; 6CRT; X-ray; 2.00 A; A=1-540. DR PDB; 6V2L; X-ray; 1.70 A; A=1-540. DR PDB; 6V2M; X-ray; 1.66 A; A=1-540. DR PDB; 6V2N; X-ray; 1.65 A; A=1-540. DR PDBsum; 1AQ2; -. DR PDBsum; 1AYL; -. DR PDBsum; 1K3C; -. DR PDBsum; 1K3D; -. DR PDBsum; 1OEN; -. DR PDBsum; 1OS1; -. DR PDBsum; 2OLQ; -. DR PDBsum; 2OLR; -. DR PDBsum; 2PXZ; -. DR PDBsum; 2PY7; -. DR PDBsum; 6ASI; -. DR PDBsum; 6ASM; -. DR PDBsum; 6ASN; -. DR PDBsum; 6AT2; -. DR PDBsum; 6AT3; -. DR PDBsum; 6AT4; -. DR PDBsum; 6COM; -. DR PDBsum; 6CRT; -. DR PDBsum; 6V2L; -. DR PDBsum; 6V2M; -. DR PDBsum; 6V2N; -. DR AlphaFoldDB; P22259; -. DR SMR; P22259; -. DR BioGRID; 4262181; 19. DR IntAct; P22259; 4. DR STRING; 511145.b3403; -. DR iPTMnet; P22259; -. DR jPOST; P22259; -. DR PaxDb; 511145-b3403; -. DR EnsemblBacteria; AAC76428; AAC76428; b3403. DR GeneID; 66672717; -. DR GeneID; 945667; -. DR KEGG; ecj:JW3366; -. DR KEGG; eco:b3403; -. DR PATRIC; fig|1411691.4.peg.3326; -. DR EchoBASE; EB0682; -. DR eggNOG; COG1866; Bacteria. DR HOGENOM; CLU_018247_0_1_6; -. DR InParanoid; P22259; -. DR OMA; MRYAGEM; -. DR OrthoDB; 9806325at2; -. DR PhylomeDB; P22259; -. DR BioCyc; EcoCyc:PEPCARBOXYKIN-MONOMER; -. DR BioCyc; MetaCyc:PEPCARBOXYKIN-MONOMER; -. DR BRENDA; 4.1.1.49; 2026. DR SABIO-RK; P22259; -. DR UniPathway; UPA00138; -. DR EvolutionaryTrace; P22259; -. DR PRO; PR:P22259; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0005509; F:calcium ion binding; IDA:EcoCyc. DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc. DR GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IDA:EcoCyc. DR GO; GO:0006094; P:gluconeogenesis; IMP:EcoCyc. 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 1: Evidence at protein level; KW 3D-structure; Acetylation; Allosteric enzyme; ATP-binding; Calcium; KW Cytoplasm; Decarboxylase; Direct protein sequencing; Gluconeogenesis; KW Lyase; Magnesium; Manganese; Metal-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..540 FT /note="Phosphoenolpyruvate carboxykinase (ATP)" FT /id="PRO_0000203818" FT BINDING 65 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|PubMed:11724534" FT BINDING 149 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 150 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 152 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 207 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|PubMed:11724534" FT BINDING 213 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|PubMed:12837799, ECO:0000269|PubMed:17475535, FT ECO:0000269|PubMed:8599762, ECO:0000269|PubMed:9406547, FT ECO:0000269|Ref.20, ECO:0000269|Ref.21" FT BINDING 213 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|Ref.21" FT BINDING 213 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|PubMed:11724534" FT BINDING 232 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|PubMed:12837799, ECO:0000269|PubMed:17475535, FT ECO:0000269|PubMed:8599762, ECO:0000269|PubMed:9406547, FT ECO:0000269|Ref.20, ECO:0000269|Ref.21" FT BINDING 232 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|Ref.21" FT BINDING 248..256 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|PubMed:12837799, ECO:0000269|PubMed:17475535, FT ECO:0000269|PubMed:8599762, ECO:0000269|PubMed:9406547, FT ECO:0000269|Ref.20, ECO:0000269|Ref.21" FT BINDING 269 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|Ref.21" FT BINDING 283 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 297 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|PubMed:12837799, ECO:0000269|PubMed:17475535, FT ECO:0000269|PubMed:8599762, ECO:0000269|PubMed:9406547, FT ECO:0000269|Ref.20, ECO:0000269|Ref.21" FT BINDING 333 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|PubMed:12837799, ECO:0000269|PubMed:17475535, FT ECO:0000269|PubMed:8599762, ECO:0000269|PubMed:9406547, FT ECO:0000269|Ref.20, ECO:0000269|Ref.21" FT BINDING 333 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|PubMed:11724534" FT BINDING 449..450 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|PubMed:12837799, ECO:0000269|PubMed:17475535, FT ECO:0000269|PubMed:8599762, ECO:0000269|PubMed:9406547, FT ECO:0000269|Ref.20, ECO:0000269|Ref.21" FT BINDING 455 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|PubMed:12837799, ECO:0000269|PubMed:17475535, FT ECO:0000269|PubMed:8599762, ECO:0000269|PubMed:9406547, FT ECO:0000269|Ref.20, ECO:0000269|Ref.21" FT MOD_RES 87 FT /note="N6-acetyllysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|PubMed:18723842" FT MOD_RES 523 FT /note="N6-acetyllysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453, FT ECO:0000269|PubMed:18723842" FT MUTAGEN 65 FT /note="R->Q: Slightly lower catalytic efficiency compared FT to wild-type and the affinity binding for OAA is 330-fold FT higher than for wild-type." FT /evidence="ECO:0000269|PubMed:17475535" FT MUTAGEN 268 FT /note="D->N: In PCK51; altered-activity mutant that FT catalyzes the conversion from oxaloacetate to pyruvate (OAA FT decarboxylase activity)." FT /evidence="ECO:0000269|PubMed:7883719" FT MUTAGEN 284 FT /note="G->S: In PCK53; shows reduced-activity." FT /evidence="ECO:0000269|PubMed:7883719" FT CONFLICT 67..72 FT /note="PKDKYI -> QKISIS (in Ref. 1; AAA24301)" FT /evidence="ECO:0000305" FT CONFLICT 192..194 FT /note="AFN -> R (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 197..203 FT /note="ERMQLIG -> DRAHAADC (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 233 FT /note="C -> S (in Ref. 1; AAA24301)" FT /evidence="ECO:0000305" FT CONFLICT 252 FT /note="T -> N (in Ref. 1; AAA24301)" FT /evidence="ECO:0000305" FT CONFLICT 256..260 FT /note="TLSTD -> AFPR (in Ref. 1; AAA24301)" FT /evidence="ECO:0000305" FT CONFLICT 281..285 FT /note="FEGGC -> LKAAG (in Ref. 1; AAA24301)" FT /evidence="ECO:0000305" FT CONFLICT 302..307 FT /note="NAIRRD -> KLSVVM (in Ref. 1; AAA24301)" FT /evidence="ECO:0000305" FT CONFLICT 346 FT /note="K -> R (in Ref. 1; AAA24301)" FT /evidence="ECO:0000305" FT CONFLICT 354..359 FT /note="ATKVIF -> GRRLSL (in Ref. 1; AAA24301)" FT /evidence="ECO:0000305" FT CONFLICT 363 FT /note="D -> H (in Ref. 1; AAA24301)" FT /evidence="ECO:0000305" FT CONFLICT 446 FT /note="T -> S (in Ref. 1; AAA24301)" FT /evidence="ECO:0000305" FT CONFLICT 449 FT /note="R -> S (in Ref. 1; AAA24301)" FT /evidence="ECO:0000305" FT CONFLICT 460..467 FT /note="DAILNGSL -> RRHPQRFV (in Ref. 4)" FT /evidence="ECO:0000305" FT CONFLICT 499 FT /note="T -> R (in Ref. 4)" FT /evidence="ECO:0000305" FT TURN 5..7 FT /evidence="ECO:0007829|PDB:1AQ2" FT HELIX 9..13 FT /evidence="ECO:0007829|PDB:6AT4" FT TURN 14..16 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 23..26 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 29..36 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 43..45 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 67..69 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 70..73 FT /evidence="ECO:0007829|PDB:6AT4" FT TURN 76..81 FT /evidence="ECO:0007829|PDB:6AT4" FT TURN 85..87 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 99..113 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 118..128 FT /evidence="ECO:0007829|PDB:6AT4" FT TURN 129..131 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 133..141 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 142..151 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 157..161 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 166..172 FT /evidence="ECO:0007829|PDB:6AT4" FT TURN 178..184 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 186..188 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 190..194 FT /evidence="ECO:0007829|PDB:6AT4" FT TURN 195..198 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 199..204 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 210..222 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 233..237 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 243..247 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 254..258 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 263..269 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 271..273 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 278..281 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 283..288 FT /evidence="ECO:0007829|PDB:6AT4" FT TURN 294..296 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 298..302 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 309..312 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:1OEN" FT TURN 317..319 FT /evidence="ECO:0007829|PDB:1OEN" FT STRAND 320..322 FT /evidence="ECO:0007829|PDB:1OEN" FT STRAND 333..337 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 338..340 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 341..344 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 347..352 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 354..361 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 370..373 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 376..385 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 387..390 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 394..396 FT /evidence="ECO:0007829|PDB:6AT2" FT STRAND 402..405 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 407..409 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 411..413 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 418..432 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 435..440 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 447..449 FT /evidence="ECO:0007829|PDB:6AT2" FT HELIX 452..463 FT /evidence="ECO:0007829|PDB:6AT4" FT TURN 464..469 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 472..475 FT /evidence="ECO:0007829|PDB:6AT4" FT TURN 476..479 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 480..484 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 491..493 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 496..499 FT /evidence="ECO:0007829|PDB:6AT4" FT STRAND 500..502 FT /evidence="ECO:0007829|PDB:6AT2" FT HELIX 504..521 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 522..526 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 528..533 FT /evidence="ECO:0007829|PDB:6AT4" FT HELIX 534..536 FT /evidence="ECO:0007829|PDB:6AT4" SQ SEQUENCE 540 AA; 59643 MW; A744D90899F6A8A5 CRC64; MRVNNGLTPQ ELEAYGISDV HDIVYNPSYD LLYQEELDPS LTGYERGVLT NLGAVAVDTG IFTGRSPKDK YIVRDDTTRD TFWWADKGKG KNDNKPLSPE TWQHLKGLVT RQLSGKRLFV VDAFCGANPD TRLSVRFITE VAWQAHFVKN MFIRPSDEEL AGFKPDFIVM NGAKCTNPQW KEQGLNSENF VAFNLTERMQ LIGGTWYGGE MKKGMFSMMN YLLPLKGIAS MHCSANVGEK GDVAVFFGLS GTGKTTLSTD PKRRLIGDDE HGWDDDGVFN FEGGCYAKTI KLSKEAEPEI YNAIRRDALL ENVTVREDGT IDFDDGSKTE NTRVSYPIYH IDNIVKPVSK AGHATKVIFL TADAFGVLPP VSRLTADQTQ YHFLSGFTAK LAGTERGITE PTPTFSACFG AAFLSLHPTQ YAEVLVKRMQ AAGAQAYLVN TGWNGTGKRI SIKDTRAIID AILNGSLDNA ETFTLPMFNL AIPTELPGVD TKILDPRNTY ASPEQWQEKA ETLAKLFIDN FDKYTDTPAG AALVAAGPKL //