ACEK_ECOLI
ID ACEK_ECOLI Reviewed; 578 AA.
AC P11071; P11070; Q2M6T8;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Isocitrate dehydrogenase kinase/phosphatase {ECO:0000255|HAMAP-Rule:MF_00747};
DE Short=IDH kinase/phosphatase {ECO:0000255|HAMAP-Rule:MF_00747};
DE Short=IDHK/P {ECO:0000255|HAMAP-Rule:MF_00747};
DE EC=2.7.11.5 {ECO:0000255|HAMAP-Rule:MF_00747};
DE EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_00747};
GN Name=aceK {ECO:0000255|HAMAP-Rule:MF_00747};
GN OrderedLocusNames=b4016, JW3976;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2836370; DOI=10.1128/jb.170.6.2763-2769.1988;
RA Klumpp D.J., Plank D.W., Bowdin L.J., Stueland C.S., Chung T.,
RA Laporte D.C.;
RT "Nucleotide sequence of aceK, the gene encoding isocitrate dehydrogenase
RT kinase/phosphatase.";
RL J. Bacteriol. 170:2763-2769(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2826408; DOI=10.1128/jb.170.1.89-97.1988;
RA Cortay J.-C., Bleicher F., Rieul C., Reeves H.C., Cozzone A.J.;
RT "Nucleotide sequence and expression of the aceK gene coding for isocitrate
RT dehydrogenase kinase/phosphatase in Escherichia coli.";
RL J. Bacteriol. 170:89-97(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
RX PubMed=3049537; DOI=10.1128/jb.170.10.4528-4536.1988;
RA Matsuoka M., McFadden B.A.;
RT "Isolation, hyperexpression, and sequencing of the aceA gene encoding
RT isocitrate lyase in Escherichia coli.";
RL J. Bacteriol. 170:4528-4536(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 552-578.
RX PubMed=1995429; DOI=10.1016/0378-1119(91)90024-6;
RA Galinier A., Bleicher F., Negre D., Perriere G., Duclos B., Cozzone A.J.,
RA Cortay J.-C.;
RT "Primary structure of the intergenic region between aceK and iclR in the
RT Escherichia coli chromosome.";
RL Gene 97:149-150(1991).
RN [8]
RP REVIEW, AND MUTAGENESIS OF LYS-336.
RX PubMed=2557093; DOI=10.1016/0300-9084(89)90110-7;
RA Laporte D.C., Stueland C.S., Ikeda T.P.;
RT "Isocitrate dehydrogenase kinase/phosphatase.";
RL Biochimie 71:1051-1057(1989).
RN [9]
RP MUTAGENESIS OF ASP-371; ASN-377; ASP-403 AND GLU-439.
RX PubMed=11258918; DOI=10.1021/bi001713x;
RA Oudot C., Cortay J.-C., Blanchet C., Laporte D.C., Di Pietro A.,
RA Cozzone A.J., Jault J.-M.;
RT "The 'catalytic' triad of isocitrate dehydrogenase kinase/phosphatase from
RT E. coli and its relationship with that found in eukaryotic protein
RT kinases.";
RL Biochemistry 40:3047-3055(2001).
CC -!- FUNCTION: Bifunctional enzyme which can phosphorylate or
CC dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine
CC residue. This is a regulatory mechanism which enables bacteria to
CC bypass the Krebs cycle via the glyoxylate shunt in response to the
CC source of carbon. When bacteria are grown on glucose, IDH is fully
CC active and unphosphorylated, but when grown on acetate or ethanol, the
CC activity of IDH declines drastically concomitant with its
CC phosphorylation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-
CC phospho-L-seryl-[isocitrate dehydrogenase]; Xref=Rhea:RHEA:43540,
CC Rhea:RHEA-COMP:10605, Rhea:RHEA-COMP:10606, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC ChEBI:CHEBI:456216; EC=2.7.11.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00747};
CC -!- INTERACTION:
CC P11071; P08200: icd; NbExp=5; IntAct=EBI-1112800, EBI-369069;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the AceK family. {ECO:0000255|HAMAP-
CC Rule:MF_00747}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24007.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M20714; AAA24010.1; -; Genomic_DNA.
DR EMBL; M18974; AAA24007.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00006; AAC43110.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76986.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78018.1; -; Genomic_DNA.
DR EMBL; M22621; AAC13651.1; -; Genomic_DNA.
DR EMBL; M63497; AAA73005.1; -; Genomic_DNA.
DR PIR; G65208; KIECID.
DR RefSeq; NP_418440.1; NC_000913.3.
DR RefSeq; WP_001137220.1; NZ_SSZK01000049.1.
DR PDB; 6K5L; X-ray; 2.55 A; A/B=1-578.
DR PDBsum; 6K5L; -.
DR AlphaFoldDB; P11071; -.
DR SMR; P11071; -.
DR BioGRID; 4261467; 11.
DR BioGRID; 849198; 7.
DR DIP; DIP-9041N; -.
DR IntAct; P11071; 12.
DR STRING; 511145.b4016; -.
DR jPOST; P11071; -.
DR PaxDb; P11071; -.
DR PRIDE; P11071; -.
DR DNASU; 944797; -.
DR EnsemblBacteria; AAC76986; AAC76986; b4016.
DR EnsemblBacteria; BAE78018; BAE78018; BAE78018.
DR GeneID; 944797; -.
DR KEGG; ecj:JW3976; -.
DR KEGG; eco:b4016; -.
DR PATRIC; fig|1411691.4.peg.2697; -.
DR EchoBASE; EB0025; -.
DR eggNOG; COG4579; Bacteria.
DR HOGENOM; CLU_033804_1_1_6; -.
DR InParanoid; P11071; -.
DR OMA; EPWYSVG; -.
DR PhylomeDB; P11071; -.
DR BioCyc; EcoCyc:ICITDEHASE-KIN-PHOSPHA; -.
DR BioCyc; MetaCyc:ICITDEHASE-KIN-PHOSPHA; -.
DR BRENDA; 2.7.11.5; 2026.
DR SABIO-RK; P11071; -.
DR PRO; PR:P11071; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IC:EcoliWiki.
DR GO; GO:0008772; F:[isocitrate dehydrogenase (NADP+)] kinase activity; IDA:EcoCyc.
DR GO; GO:0016208; F:AMP binding; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IDA:EcoliWiki.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:EcoCyc.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:EcoCyc.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006097; P:glyoxylate cycle; IC:EcoliWiki.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; IDA:EcoCyc.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:EcoCyc.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0050790; P:regulation of catalytic activity; IDA:EcoCyc.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IC:EcoliWiki.
DR HAMAP; MF_00747; AceK; 1.
DR InterPro; IPR010452; Isocitrate_DH_AceK.
DR PANTHER; PTHR39559; PTHR39559; 1.
DR Pfam; PF06315; AceK; 1.
DR PIRSF; PIRSF000719; AceK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Glyoxylate bypass; Hydrolase; Kinase; Nucleotide-binding;
KW Protein phosphatase; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..578
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_0000057898"
FT ACT_SITE 371
FT /evidence="ECO:0000305"
FT BINDING 315..321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT MUTAGEN 336
FT /note="K->M: Inhibits enzyme."
FT /evidence="ECO:0000269|PubMed:2557093"
FT MUTAGEN 371
FT /note="D->A,E,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11258918"
FT MUTAGEN 377
FT /note="N->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:11258918"
FT MUTAGEN 403
FT /note="D->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:11258918"
FT MUTAGEN 439
FT /note="E->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:11258918"
FT CONFLICT 140
FT /note="A -> G (in Ref. 2; AAA24007)"
FT /evidence="ECO:0000305"
FT CONFLICT 416..417
FT /note="ER -> DG (in Ref. 1; AAA24010)"
FT /evidence="ECO:0000305"
FT HELIX 2..29
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 40..69
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:6K5L"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:6K5L"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:6K5L"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:6K5L"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 169..184
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 206..215
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 264..272
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 280..286
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 290..307
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 321..327
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 372..381
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 387..396
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 407..417
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 422..425
FT /evidence="ECO:0007829|PDB:6K5L"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 431..450
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:6K5L"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 518..522
FT /evidence="ECO:0007829|PDB:6K5L"
FT TURN 526..528
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 529..536
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 537..540
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 542..553
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:6K5L"
FT HELIX 569..572
FT /evidence="ECO:0007829|PDB:6K5L"
SQ SEQUENCE 578 AA; 67699 MW; 5ABD5FB5FA1D9B29 CRC64;
MPRGLELLIA QTILQGFDAQ YGRFLEVTSG AQQRFEQADW HAVQQAMKNR IHLYDHHVGL
VVEQLRCITN GQSTDAAFLL RVKEHYTRLL PDYPRFEIAE SFFNSVYCRL FDHRSLTPER
LFIFSSQPER RFRTIPRPLA KDFHPDHGWE SLLMRVISDL PLRLRWQNKS RDIHYIIRHL
TETLGTDNLA ESHLQVANEL FYRNKAAWLV GKLITPSGTL PFLLPIHQTD DGELFIDTCL
TTTAEASIVF GFARSYFMVY APLPAALVEW LREILPGKTT AELYMAIGCQ KHAKTESYRE
YLVYLQGCNE QFIEAPGIRG MVMLVFTLPG FDRVFKVIKD RFAPQKEMSA AHVRACYQLV
KEHDRVGRMA DTQEFENFVL EKRHISPALM ELLLQEAAEK ITDLGEQIVI RHLYIERRMV
PLNIWLEQVE GQQLRDAIEE YGNAIRQLAA ANIFPGDMLF KNFGVTRHGR VVFYDYDEIC
YMTEVNFRDI PPPRYPEDEL ASEPWYSVSP GDVFPEEFRH WLCADPRIGP LFEEMHADLF
RADYWRALQN RIREGHVEDV YAYRRRQRFS VRYGEMLF
