Reviewed, UniProtKB/Swiss-Prot P11071 (ACEK_ECOLI)

Names and origin

Protein names

Recommended name:
    Isocitrate dehydrogenase kinase/phosphatase
      Short name=IDH kinase/phosphatase
      Short name=IDHK/P
    EC=2.7.11.5
    EC=3.1.3.-

Gene names

Name:	aceK
Ordered Locus Names:	b4016, JW3976

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	578 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
Catalytic activity	ATP + [isocitrate dehydrogenase (NADP(+))] = ADP + [isocitrate dehydrogenase (NADP(+))] phosphate.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the aceK family.
Sequence caution	The sequence AAA24007.1 differs from that shown. Reason: Frameshift at positions 92, 137 and 166.

Ontologies

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase Kinase Protein phosphatase Transferase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: InterPro glyoxylate cycle Inferred from electronic annotation. Source: HAMAP tricarboxylic acid cycle Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP [isocitrate dehydrogenase (NADP+)] kinase activity Inferred from electronic annotation. Source: HAMAP phosphoprotein phosphatase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 578	578	Isocitrate dehydrogenase kinase/phosphatase		PRO_0000057898
Regions
	Nucleotide binding	315 – 321	7	ATP By similarity
Sites
	Active site	371	1	Probable
	Binding site	336	1	ATP By similarity
Experimental info
	Mutagenesis	336	1	K → M: Inhibits enzyme
	Mutagenesis	371	1	D → A, E or Q: Loss of activity
	Mutagenesis	377	1	N → A: No loss of activity
	Mutagenesis	403	1	D → A: No loss of activity
	Mutagenesis	439	1	E → A: No loss of activity
	Sequence conflict	140	1	A → G in AAA24007. Ref.2
	Sequence conflict	416 – 417	2	ER → DG in AAA24010. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P11071-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 5ABD5FB5FA1D9B29	FASTA	578	67,699
	10 20 30 40 50 60 MPRGLELLIA QTILQGFDAQ YGRFLEVTSG AQQRFEQADW HAVQQAMKNR IHLYDHHVGL 70 80 90 100 110 120 VVEQLRCITN GQSTDAAFLL RVKEHYTRLL PDYPRFEIAE SFFNSVYCRL FDHRSLTPER 130 140 150 160 170 180 LFIFSSQPER RFRTIPRPLA KDFHPDHGWE SLLMRVISDL PLRLRWQNKS RDIHYIIRHL 190 200 210 220 230 240 TETLGTDNLA ESHLQVANEL FYRNKAAWLV GKLITPSGTL PFLLPIHQTD DGELFIDTCL 250 260 270 280 290 300 TTTAEASIVF GFARSYFMVY APLPAALVEW LREILPGKTT AELYMAIGCQ KHAKTESYRE 310 320 330 340 350 360 YLVYLQGCNE QFIEAPGIRG MVMLVFTLPG FDRVFKVIKD RFAPQKEMSA AHVRACYQLV 370 380 390 400 410 420 KEHDRVGRMA DTQEFENFVL EKRHISPALM ELLLQEAAEK ITDLGEQIVI RHLYIERRMV 430 440 450 460 470 480 PLNIWLEQVE GQQLRDAIEE YGNAIRQLAA ANIFPGDMLF KNFGVTRHGR VVFYDYDEIC 490 500 510 520 530 540 YMTEVNFRDI PPPRYPEDEL ASEPWYSVSP GDVFPEEFRH WLCADPRIGP LFEEMHADLF 550 560 570 RADYWRALQN RIREGHVEDV YAYRRRQRFS VRYGEMLF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of aceK, the gene encoding isocitrate dehydrogenase kinase/phosphatase." Klumpp D.J., Plank D.W., Bowdin L.J., Stueland C.S., Chung T., Laporte D.C. J. Bacteriol. 170:2763-2769(1988) [PubMed: 2836370] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Nucleotide sequence and expression of the aceK gene coding for isocitrate dehydrogenase kinase/phosphatase in Escherichia coli." Cortay J.-C., Bleicher F., Rieul C., Reeves H.C., Cozzone A.J. J. Bacteriol. 170:89-97(1988) [PubMed: 2826408] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Isolation, hyperexpression, and sequencing of the aceA gene encoding isocitrate lyase in Escherichia coli." Matsuoka M., McFadden B.A. J. Bacteriol. 170:4528-4536(1988) [PubMed: 3049537] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
[7]	"Primary structure of the intergenic region between aceK and iclR in the Escherichia coli chromosome." Galinier A., Bleicher F., Negre D., Perriere G., Duclos B., Cozzone A.J., Cortay J.-C. Gene 97:149-150(1991) [PubMed: 1995429] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 552-578.
[8]	"Isocitrate dehydrogenase kinase/phosphatase." Laporte D.C., Stueland C.S., Ikeda T.P. Biochimie 71:1051-1057(1989) [PubMed: 2557093] [Abstract] Cited for: REVIEW, MUTAGENESIS OF LYS-336.
[9]	"The 'catalytic' triad of isocitrate dehydrogenase kinase/phosphatase from E. coli and its relationship with that found in eukaryotic protein kinases." Oudot C., Cortay J.-C., Blanchet C., Laporte D.C., Di Pietro A., Cozzone A.J., Jault J.-M. Biochemistry 40:3047-3055(2001) [PubMed: 11258918] [Abstract] Cited for: MUTAGENESIS OF ASP-371; ASN-377; ASP-403 AND GLU-439.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M20714 Genomic DNA. Translation: AAA24010.1. M18974 Genomic DNA. Translation: AAA24007.1. Frameshift. U00006 Genomic DNA. Translation: AAC43110.1. U00096 Genomic DNA. Translation: AAC76986.1. AP009048 Genomic DNA. Translation: BAE78018.1. M22621 Genomic DNA. Translation: AAC13651.1. M63497 Genomic DNA. Translation: AAA73005.1.
PIR	KIECID. G65208.
RefSeq	AP_004517.1. NP_418440.1.
3D structure databases
ModBase	Search...
Protein family/group databases
PptaseDB	P3D0409136.
Genome annotation databases
GeneID	944797.
GenomeReviews	Gene locus b4016 in contig U00096_GR. Gene locus JW3976 in contig AP009048_GR.
KEGG	ecj:JW3976. eco:b4016.
Organism-specific databases
EchoBASE	EB0025.
EcoGene	EG10026. aceK.
CMR	Search...
Phylogenomic databases
HOGENOM	P11071.
Enzyme and pathway databases
BioCyc	EcoCyc:ICITDEHASE-KIN-PHOSPHA. MetaCyc:ICITDEHASE-KIN-PHOSPHA.
Family and domain databases
HAMAP	MF_00747. [Tree]
InterPro	IPR010452. IsoCit_DHase_AceK. [Graphical view]
Pfam	PF06315. AceK. 1 hit. [Graphical view]
PIRSF	PIRSF000719. AceK. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ACEK_ECOLI

Accession

Primary (citable) accession number: P11071
Secondary accession number(s): P11070, Q2M6T8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	December 1, 2000
Last modified:	November 25, 2008
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)