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P22259

- PCKA_ECOLI

UniProt

P22259 - PCKA_ECOLI

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Protein
Phosphoenolpyruvate carboxykinase [ATP]
Gene
pckA, pck, b3403, JW3366
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.3 Publications

Catalytic activityi

ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2.1 Publication

Cofactori

Binds 1 manganese ion per subunit.5 Publications

Enzyme regulationi

Allosterically activated by calcium. It may represent the only case of a monomeric, allosteric enzyme.4 Publications

Kineticsi

  1. KM=3.8 µM for manganese (at 31 degrees Celsius and pH 7.5)2 Publications
  2. KM=0.11 mM for calcium (at 31 degrees Celsius and pH 7.5)
  3. KM=0.31 mM for OAA (at 31 degrees Celsius and pH 7.5)
  4. KM=0.51 mM for OAA (at pH 7.5)
  5. KM=1.4 mM for magnesium (at 31 degrees Celsius and pH 7.5)
  6. KM=11 mM for PEP (at pH 7.5)

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei65 – 651Substrate
Metal bindingi149 – 1491Calcium; via carbonyl oxygen By similarity
Metal bindingi150 – 1501Calcium; via carbonyl oxygen By similarity
Metal bindingi152 – 1521Calcium; via carbonyl oxygen By similarity
Binding sitei207 – 2071Substrate
Metal bindingi213 – 2131Manganese
Binding sitei213 – 2131ATP
Binding sitei213 – 2131Substrate
Metal bindingi232 – 2321Manganese; via tele nitrogen
Binding sitei232 – 2321ATP
Metal bindingi269 – 2691Manganese
Metal bindingi283 – 2831Calcium; via carbonyl oxygen By similarity
Binding sitei297 – 2971ATP
Binding sitei333 – 3331ATP
Binding sitei333 – 3331Substrate
Binding sitei455 – 4551ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi248 – 2569ATPUniRule annotation
Nucleotide bindingi449 – 4502ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. calcium ion binding Source: EcoCyc
  3. magnesium ion binding Source: EcoCyc
  4. phosphoenolpyruvate carboxykinase (ATP) activity Source: EcoCyc
Complete GO annotation...

GO - Biological processi

  1. gluconeogenesis Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Gluconeogenesis

Keywords - Ligandi

ATP-binding, Calcium, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PEPCARBOXYKIN-MONOMER.
ECOL316407:JW3366-MONOMER.
MetaCyc:PEPCARBOXYKIN-MONOMER.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate carboxykinase [ATP] (EC:4.1.1.49)
Short name:
PCK
Short name:
PEP carboxykinase
Short name:
PEPCK
Gene namesi
Name:pckA
Synonyms:pck
Ordered Locus Names:b3403, JW3366
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10688. pck.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651R → Q: Slightly lower catalytic efficiency compared to wild-type and the affinity binding for OAA is 330-fold higher than for wild-type. 1 Publication
Mutagenesisi268 – 2681D → N in PCK51; altered-activity mutant that catalyzes the conversion from oxaloacetate to pyruvate (OAA decarboxylase activity). 1 Publication
Mutagenesisi284 – 2841G → S in PCK53; shows reduced-activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 540540Phosphoenolpyruvate carboxykinase [ATP]UniRule annotation
PRO_0000203818Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871N6-acetyllysine1 Publication
Modified residuei523 – 5231N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP22259.
PRIDEiP22259.

PTM databases

PhosSiteiP0809417.

Expressioni

Inductioni

Induced upon entry into stationary phase and by cyclic AMP (cAMP). Repressed by glucose (catabolite repression) and by CsrA.6 Publications

Gene expression databases

GenevestigatoriP22259.

Interactioni

Subunit structurei

Monomer.4 Publications

Protein-protein interaction databases

IntActiP22259. 4 interactions.
STRINGi511145.b3403.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni5 – 73
Helixi9 – 146
Beta strandi23 – 264
Helixi29 – 379
Helixi43 – 453
Beta strandi47 – 493
Beta strandi55 – 573
Helixi67 – 693
Beta strandi70 – 734
Turni76 – 816
Beta strandi87 – 904
Beta strandi95 – 973
Helixi99 – 11315
Beta strandi118 – 12811
Turni129 – 1313
Beta strandi133 – 1408
Helixi142 – 15110
Helixi157 – 1615
Beta strandi166 – 1727
Turni178 – 1847
Beta strandi186 – 1883
Beta strandi190 – 1945
Turni195 – 1984
Beta strandi199 – 2046
Helixi209 – 22214
Helixi224 – 2263
Beta strandi229 – 2313
Beta strandi233 – 2375
Beta strandi243 – 2475
Helixi254 – 2585
Beta strandi263 – 2697
Beta strandi271 – 2744
Beta strandi277 – 2815
Beta strandi283 – 2886
Turni294 – 2963
Helixi298 – 3025
Beta strandi309 – 3124
Beta strandi314 – 3163
Turni317 – 3193
Beta strandi320 – 3223
Beta strandi333 – 3375
Helixi338 – 3403
Beta strandi341 – 3444
Beta strandi347 – 3526
Beta strandi354 – 3618
Beta strandi370 – 3734
Helixi376 – 38510
Beta strandi387 – 3915
Helixi394 – 3963
Beta strandi401 – 4055
Helixi407 – 4093
Helixi411 – 4133
Helixi418 – 43215
Beta strandi435 – 4406
Beta strandi447 – 4493
Helixi452 – 46312
Helixi466 – 4694
Beta strandi472 – 4754
Turni476 – 4794
Beta strandi480 – 4845
Helixi491 – 4944
Helixi496 – 4994
Beta strandi500 – 5023
Helixi503 – 52119
Helixi522 – 5243
Helixi528 – 5336
Helixi534 – 5363

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQ2X-ray1.90A1-540[»]
1AYLX-ray1.80A1-540[»]
1K3CX-ray2.00A1-540[»]
1K3DX-ray2.00A1-540[»]
1OENX-ray1.90A1-538[»]
1OS1X-ray1.80A1-540[»]
2OLQX-ray1.94A1-540[»]
2OLRX-ray1.60A1-540[»]
2PXZX-ray2.23X1-540[»]
2PY7X-ray2.20X1-540[»]
ProteinModelPortaliP22259.
SMRiP22259. Positions 6-540.

Miscellaneous databases

EvolutionaryTraceiP22259.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1866.
HOGENOMiHOG000271471.
KOiK01610.
OMAiGADPEHY.
OrthoDBiEOG6DG2RK.
PhylomeDBiP22259.

Family and domain databases

Gene3Di3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPiMF_00453. PEPCK_ATP.
InterProiIPR001272. PEP_carboxykinase_ATP.
IPR013035. PEP_carboxykinase_C.
IPR008210. PEP_carboxykinase_N.
IPR015994. PEPCK_ATP_CS.
[Graphical view]
PfamiPF01293. PEPCK_ATP. 1 hit.
[Graphical view]
PIRSFiPIRSF006294. PEP_crbxkin. 1 hit.
SUPFAMiSSF68923. SSF68923. 1 hit.
TIGRFAMsiTIGR00224. pckA. 1 hit.
PROSITEiPS00532. PEPCK_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22259-1 [UniParc]FASTAAdd to Basket

« Hide

MRVNNGLTPQ ELEAYGISDV HDIVYNPSYD LLYQEELDPS LTGYERGVLT    50
NLGAVAVDTG IFTGRSPKDK YIVRDDTTRD TFWWADKGKG KNDNKPLSPE 100
TWQHLKGLVT RQLSGKRLFV VDAFCGANPD TRLSVRFITE VAWQAHFVKN 150
MFIRPSDEEL AGFKPDFIVM NGAKCTNPQW KEQGLNSENF VAFNLTERMQ 200
LIGGTWYGGE MKKGMFSMMN YLLPLKGIAS MHCSANVGEK GDVAVFFGLS 250
GTGKTTLSTD PKRRLIGDDE HGWDDDGVFN FEGGCYAKTI KLSKEAEPEI 300
YNAIRRDALL ENVTVREDGT IDFDDGSKTE NTRVSYPIYH IDNIVKPVSK 350
AGHATKVIFL TADAFGVLPP VSRLTADQTQ YHFLSGFTAK LAGTERGITE 400
PTPTFSACFG AAFLSLHPTQ YAEVLVKRMQ AAGAQAYLVN TGWNGTGKRI 450
SIKDTRAIID AILNGSLDNA ETFTLPMFNL AIPTELPGVD TKILDPRNTY 500
ASPEQWQEKA ETLAKLFIDN FDKYTDTPAG AALVAAGPKL 540
Length:540
Mass (Da):59,643
Last modified:November 1, 1995 - v2
Checksum:iA744D90899F6A8A5
GO

Sequence cautioni

The sequence AAA24301.1 differs from that shown. Reason: Frameshift at position 456. Translation N-terminally extended.

Mass spectrometryi

Molecular mass is 59656 Da from positions 1 - 540. Determined by ESI. 1 Publication

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 726PKDKYI → QKISIS in AAA24301. 1 Publication
Sequence conflicti192 – 1943AFN → R AA sequence 1 Publication
Sequence conflicti197 – 2037ERMQLIG → DRAHAADC AA sequence 1 Publication
Sequence conflicti233 – 2331C → S in AAA24301. 1 Publication
Sequence conflicti252 – 2521T → N in AAA24301. 1 Publication
Sequence conflicti256 – 2605TLSTD → AFPR in AAA24301. 1 Publication
Sequence conflicti281 – 2855FEGGC → LKAAG in AAA24301. 1 Publication
Sequence conflicti302 – 3076NAIRRD → KLSVVM in AAA24301. 1 Publication
Sequence conflicti346 – 3461K → R in AAA24301. 1 Publication
Sequence conflicti354 – 3596ATKVIF → GRRLSL in AAA24301. 1 Publication
Sequence conflicti363 – 3631D → H in AAA24301. 1 Publication
Sequence conflicti446 – 4461T → S in AAA24301. 1 Publication
Sequence conflicti449 – 4491R → S in AAA24301. 1 Publication
Sequence conflicti460 – 4678DAILNGSL → RRHPQRFV1 Publication
Sequence conflicti499 – 4991T → R1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M59823 Genomic DNA. Translation: AAA24301.1. Frameshift.
U18997 Genomic DNA. Translation: AAA58200.1.
U00096 Genomic DNA. Translation: AAC76428.1.
AP009048 Genomic DNA. Translation: BAE77888.1.
J01656 Unassigned RNA. No translation available.
S76268 Genomic DNA. Translation: AAB33745.2.
S76269 Genomic DNA. Translation: AAB33746.2.
U21325 Genomic DNA. Translation: AAA95999.1.
PIRiF65135.
RefSeqiNP_417862.1. NC_000913.3.
YP_492029.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76428; AAC76428; b3403.
BAE77888; BAE77888; BAE77888.
GeneIDi12933187.
945667.
KEGGiecj:Y75_p3773.
eco:b3403.
PATRICi32122242. VBIEscCol129921_3498.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M59823 Genomic DNA. Translation: AAA24301.1 . Frameshift.
U18997 Genomic DNA. Translation: AAA58200.1 .
U00096 Genomic DNA. Translation: AAC76428.1 .
AP009048 Genomic DNA. Translation: BAE77888.1 .
J01656 Unassigned RNA. No translation available.
S76268 Genomic DNA. Translation: AAB33745.2 .
S76269 Genomic DNA. Translation: AAB33746.2 .
U21325 Genomic DNA. Translation: AAA95999.1 .
PIRi F65135.
RefSeqi NP_417862.1. NC_000913.3.
YP_492029.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AQ2 X-ray 1.90 A 1-540 [» ]
1AYL X-ray 1.80 A 1-540 [» ]
1K3C X-ray 2.00 A 1-540 [» ]
1K3D X-ray 2.00 A 1-540 [» ]
1OEN X-ray 1.90 A 1-538 [» ]
1OS1 X-ray 1.80 A 1-540 [» ]
2OLQ X-ray 1.94 A 1-540 [» ]
2OLR X-ray 1.60 A 1-540 [» ]
2PXZ X-ray 2.23 X 1-540 [» ]
2PY7 X-ray 2.20 X 1-540 [» ]
ProteinModelPortali P22259.
SMRi P22259. Positions 6-540.
ModBasei Search...

Protein-protein interaction databases

IntActi P22259. 4 interactions.
STRINGi 511145.b3403.

PTM databases

PhosSitei P0809417.

Proteomic databases

PaxDbi P22259.
PRIDEi P22259.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76428 ; AAC76428 ; b3403 .
BAE77888 ; BAE77888 ; BAE77888 .
GeneIDi 12933187.
945667.
KEGGi ecj:Y75_p3773.
eco:b3403.
PATRICi 32122242. VBIEscCol129921_3498.

Organism-specific databases

EchoBASEi EB0682.
EcoGenei EG10688. pck.

Phylogenomic databases

eggNOGi COG1866.
HOGENOMi HOG000271471.
KOi K01610.
OMAi GADPEHY.
OrthoDBi EOG6DG2RK.
PhylomeDBi P22259.

Enzyme and pathway databases

UniPathwayi UPA00138 .
BioCyci EcoCyc:PEPCARBOXYKIN-MONOMER.
ECOL316407:JW3366-MONOMER.
MetaCyc:PEPCARBOXYKIN-MONOMER.

Miscellaneous databases

EvolutionaryTracei P22259.
PROi P22259.

Gene expression databases

Genevestigatori P22259.

Family and domain databases

Gene3Di 3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPi MF_00453. PEPCK_ATP.
InterProi IPR001272. PEP_carboxykinase_ATP.
IPR013035. PEP_carboxykinase_C.
IPR008210. PEP_carboxykinase_N.
IPR015994. PEPCK_ATP_CS.
[Graphical view ]
Pfami PF01293. PEPCK_ATP. 1 hit.
[Graphical view ]
PIRSFi PIRSF006294. PEP_crbxkin. 1 hit.
SUPFAMi SSF68923. SSF68923. 1 hit.
TIGRFAMsi TIGR00224. pckA. 1 hit.
PROSITEi PS00532. PEPCK_ATP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the pckA gene of Escherichia coli K-12: relevance to genetic and allosteric regulation and homology of E. coli phosphoenolpyruvate carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces cerevisiae."
    Medina V., Pontarollo R., Glaeske D., Tabel H., Goldie H.
    J. Bacteriol. 172:7151-7156(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, ENZYME REGULATION, COFACTOR, SUBUNIT.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Osmoregulation of gene expression. II. DNA sequence of the envZ gene of the ompB operon of Escherichia coli and characterization of its gene product."
    Mizuno T., Wurtzel E.T., Inouye M.
    J. Biol. Chem. 257:13692-13698(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 439-540.
  5. "The global regulatory protein FruR modulates the direction of carbon flow in Escherichia coli."
    Ramseier T.M., Bledig S., Michotey V., Feghali R., Saier M.H. Jr.
    Mol. Microbiol. 16:1157-1169(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
    Strain: K12.
  6. "A mutant phosphoenolpyruvate carboxykinase in Escherichia coli conferring oxaloacetate decarboxylase activity."
    Hou S.-Y., Chao Y.-P., Liao J.C.
    J. Bacteriol. 177:1620-1623(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 242-290, MUTAGENESIS OF ASP-268 AND GLY-284.
  7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  8. "Allosteric control by calcium and mechanism of desensitization of phosphoenolpyruvate carboxykinase of Escherichia coli."
    Goldie A.H., Sanwal B.D.
    J. Biol. Chem. 255:1399-1405(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  9. "Regulation of transcription of the Escherichia coli phosphoenolpyruvate carboxykinase locus: studies with pck-lacZ operon fusions."
    Goldie H.
    J. Bacteriol. 159:832-836(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "Control of gluconeogenic growth by pps and pck in Escherichia coli."
    Chao Y.P., Patnaik R., Roof W.D., Young R.F., Liao J.C.
    J. Bacteriol. 175:6939-6944(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GLUCONEOGENESIS.
  11. "Identification and molecular characterization of csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties."
    Romeo T., Gong M., Liu M.-Y., Brun-Zinkernagel A.-M.
    J. Bacteriol. 175:4744-4755(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  12. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  13. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87 AND LYS-523, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  14. "Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold."
    Matte A., Goldie H., Sweet R.M., Delbaere L.T.J.
    J. Mol. Biol. 256:126-143(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-538, ENZYME REGULATION, MASS SPECTROMETRY.
  15. "Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase."
    Tari L.W., Matte A., Pugazhenthi U., Goldie H., Delbaere L.T.J.
    Nat. Struct. Biol. 3:355-363(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ATP AND SUBSTRATE ANALOGS, REACTION MECHANISM.
  16. "Mg(2+)-Mn(2+) clusters in enzyme-catalyzed phosphoryl-transfer reactions."
    Tari L.W., Matte A., Goldie H., Delbaere L.T.
    Nat. Struct. Biol. 4:990-994(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ATP, MANGANESE AND SUBSTRATE, COFACTOR, SUBUNIT.
  17. "The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF(3)."
    Sudom A.M., Prasad L., Goldie H., Delbaere L.T.
    J. Mol. Biol. 314:83-92(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ATP ANALOGS AND SUBSTRATE, REACTION MECHANISM.
  18. "Mechanisms of activation of phosphoenolpyruvate carboxykinase from Escherichia coli by Ca2+ and of desensitization by trypsin."
    Sudom A., Walters R., Pastushok L., Goldie D., Prasad L., Delbaere L.T., Goldie H.
    J. Bacteriol. 185:4233-4242(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ATP, CALCIUM AND SUBSTRATE, ENZYME REGULATION, REACTION MECHANISM, SUBUNIT.
  19. Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ATP, MANGANESE AND SUBSTRATE ANALOGS, MUTAGENESIS OF ARG-65, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
  20. "Crystal structure of E. coli phosphoenolpyruvate carboxykinase (PEPCK) complexed with ATP, Mg2+, Mn2+, carbon dioxide and oxaloacetate."
    Delbaere L.T.J., Cotelesage J.J.H., Goldie H.
    Submitted (MAY-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEX WITH ATP, MANGANESE AND SUBSTRATE ANALOGS, COFACTOR.
  21. "Crystal structure of E. coli phosphoenolpyruvate carboxykinase mutant Lys213Ser."
    Delbaere L.T.J., Cotelesage J.J.H., Goldie H.
    Submitted (MAY-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ATP AND MANGANESE, COFACTOR.

Entry informationi

Entry nameiPCKA_ECOLI
AccessioniPrimary (citable) accession number: P22259
Secondary accession number(s): Q2M768
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1995
Last modified: May 14, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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