PCKA_ECOLI
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 03-AUG-2022, entry version 192.
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; Proteobacteria; 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;
CC Evidence={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 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};
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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; P22259; -.
DR PRIDE; P22259; -.
DR EnsemblBacteria; AAC76428; AAC76428; b3403.
DR EnsemblBacteria; BAE77888; BAE77888; BAE77888.
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 PhylomeDB; P22259; -.
DR BioCyc; EcoCyc:PEPCARBOXYKIN-MON; -.
DR BioCyc; MetaCyc:PEPCARBOXYKIN-MON; -.
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; 3.40.449.10; -; 1.
DR Gene3D; 3.90.228.20; -; 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 PANTHER; PTHR30031; PTHR30031; 1.
DR Pfam; PF01293; PEPCK_ATP; 1.
DR PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR SUPFAM; SSF68923; SSF68923; 1.
DR TIGRFAMs; TIGR00224; pckA; 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
