ACEK_ECO57
ID ACEK_ECO57 Reviewed; 578 AA.
AC Q8X607;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=Z5602, ECs4934;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(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. {ECO:0000255|HAMAP-Rule:MF_00747}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00747}.
CC -!- SIMILARITY: Belongs to the AceK family. {ECO:0000255|HAMAP-
CC Rule:MF_00747}.
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DR EMBL; AE005174; AAG59208.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38357.1; -; Genomic_DNA.
DR PIR; D86093; D86093.
DR PIR; F91245; F91245.
DR RefSeq; NP_312961.1; NC_002695.1.
DR RefSeq; WP_001137245.1; NZ_SWKA01000005.1.
DR PDB; 3EPS; X-ray; 2.80 A; A/B=2-578.
DR PDB; 3LC6; X-ray; 3.10 A; A/B=1-578.
DR PDB; 3LCB; X-ray; 2.90 A; A/B=1-578.
DR PDB; 4P69; X-ray; 3.30 A; A/B=4-571.
DR PDBsum; 3EPS; -.
DR PDBsum; 3LC6; -.
DR PDBsum; 3LCB; -.
DR PDBsum; 4P69; -.
DR AlphaFoldDB; Q8X607; -.
DR SMR; Q8X607; -.
DR STRING; 155864.EDL933_5343; -.
DR EnsemblBacteria; AAG59208; AAG59208; Z5602.
DR EnsemblBacteria; BAB38357; BAB38357; ECs_4934.
DR GeneID; 914849; -.
DR KEGG; ece:Z5602; -.
DR KEGG; ecs:ECs_4934; -.
DR PATRIC; fig|386585.9.peg.5161; -.
DR eggNOG; COG4579; Bacteria.
DR HOGENOM; CLU_033804_1_1_6; -.
DR OMA; EPWYSVG; -.
DR BRENDA; 2.7.11.5; 2026.
DR EvolutionaryTrace; Q8X607; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008772; F:[isocitrate dehydrogenase (NADP+)] kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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; Glyoxylate bypass; Hydrolase; Kinase;
KW Nucleotide-binding; Protein phosphatase; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..578
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_0000057900"
FT ACT_SITE 371
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
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 HELIX 3..28
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 40..67
FT /evidence="ECO:0007829|PDB:3EPS"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:3EPS"
FT TURN 88..92
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:3EPS"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3EPS"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 169..184
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 206..215
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 290..306
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:3LCB"
FT STRAND 321..327
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:3EPS"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 373..381
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 387..396
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 407..417
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 422..428
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 432..450
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:3EPS"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 496..500
FT /evidence="ECO:0007829|PDB:3LCB"
FT HELIX 517..522
FT /evidence="ECO:0007829|PDB:3EPS"
FT TURN 526..528
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 529..535
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 537..540
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 542..553
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:3EPS"
FT HELIX 569..572
FT /evidence="ECO:0007829|PDB:3EPS"
SQ SEQUENCE 578 AA; 67735 MW; B6C1AF54D272685A CRC64;
MPRGLELLIA QTILQGFDAQ YGRFLEVTSG AQQRFEQADW HAVQQAMKNR IHLYDHHVGL
VVEQLRCITN GQSTDAEFLL RVKEHYTRLL PDYPRFEIAE SFFNSVYCRL FDHRSLTPER
LFIFSSQPER RFRTIPRPLA KDFHPDHGWE SLLMRVISDL PLRLHWQNKS RDIHYIIRHL
TETLGPENLS KSHLQVANEL FYRNKAAWLV GKLITPSGTL PFLLPIHQTD DGELFIDTCL
TTTAEASIVF GFARSYFMVY APLPAALVEW LREILPGKTT AELYMAIGCQ KHAKTESYRE
YLVYLQGCNE QFIEAPGIRG MVMLVFTLPG FDRVFKVIKD KFAPQKEMSA AHVRACYQLV
KEHDRVGRMA DTQEFENFVL EKRHISPALM ELLLQEAAEK ITDLGEQIVI RHLYIERRMV
PLNIWLEQVE GQQLRDAIEE YGNAIRQLAA ANIFPGDMLF KNFGVTRHGR VVFYDYDEIC
YMTEVNFRDI PPPRYPEDEL ASEPWYSVSP GDVFPEEFRH WLCADPRIGP LFEEMHADLF
RADYWRALQN RIREGHVEDV YAYRRRQRFS VRYGEMLF
