[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. PubMed=2836370 [NCBI, ExPASy, EBI, Israel, Japan] Klumpp D.J., Plank D.W., Bowdin L.J., Stueland C.S., Chung T., Laporte D.C.; "Nucleotide sequence of aceK, the gene encoding isocitrate dehydrogenase kinase/phosphatase."; J. Bacteriol. 170:2763-2769(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2826408 [NCBI, ExPASy, EBI, Israel, Japan] Cortay J.-C., Bleicher F., Rieul C., Reeves H.C., Cozzone A.J.; "Nucleotide sequence and expression of the aceK gene coding for isocitrate dehydrogenase kinase/phosphatase in Escherichia coli."; J. Bacteriol. 170:89-97(1988).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/21.23.5408; PubMed=8265357 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.; "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."; Nucleic Acids Res. 21:5408-5417(1993).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55. PubMed=3049537 [NCBI, ExPASy, EBI, Israel, Japan] Matsuoka M., McFadden B.A.; "Isolation, hyperexpression, and sequencing of the aceA gene encoding isocitrate lyase in Escherichia coli."; J. Bacteriol. 170:4528-4536(1988).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 552-578. DOI=10.1016/0378-1119(91)90024-6; PubMed=1995429 [NCBI, ExPASy, EBI, Israel, Japan] Galinier A., Bleicher F., Negre D., Perriere G., Duclos B., Cozzone A.J., Cortay J.-C.; "Primary structure of the intergenic region between aceK and iclR in the Escherichia coli chromosome."; Gene 97:149-150(1991).
[8]	REVIEW, AND MUTAGENESIS OF LYS-336. DOI=10.1016/0300-9084(89)90110-7; PubMed=2557093 [NCBI, ExPASy, EBI, Israel, Japan] Laporte D.C., Stueland C.S., Ikeda T.P.; "Isocitrate dehydrogenase kinase/phosphatase."; Biochimie 71:1051-1057(1989).
[9]	MUTAGENESIS OF ASP-371; ASN-377; ASP-403 AND GLU-439. DOI=10.1021/bi001713x; PubMed=11258918 [NCBI, ExPASy, EBI, Israel, Japan] Oudot C., Cortay J.-C., Blanchet C., Laporte D.C., Di Pietro A., Cozzone A.J., Jault J.-M.; "The 'catalytic' triad of isocitrate dehydrogenase kinase/phosphatase from E. coli and its relationship with that found in eukaryotic protein kinases."; Biochemistry 40:3047-3055(2001).

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.
SIMILARITY: Belongs to the aceK family.
SEQUENCE CAUTION:
- Sequence=AAA24007.1; Type=Frameshift; Positions=92, 137, 166;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M20714; AAA24010.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18974; AAA24007.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00006; AAC43110.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76986.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78018.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M22621; AAC13651.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M63497; AAA73005.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

G65208; KIECID.

RefSeq

AP_004517.1; -.
NP_418440.1; -.

3D structure databases

ModBase

P11071.

Protein-protein interaction databases

IntAct

P11071; -.

Protein family/group databases

PptaseDB

P3D0409136; -.

Enzyme and pathway databases

BioCyc

EcoCyc:ICITDEHASE-KIN-PHOSPHA; -.
MetaCyc:ICITDEHASE-KIN-PHOSPHA; -.

Organism-specific databases

EchoBASE

EB0025; -.

EcoGene

EG10026; aceK.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0008772;	Molecular function: [isocitrate dehydrogenase (NADP+)] kinase activity (inferred from electronic annotation from HAMAP).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0006097;	Biological process: glyoxylate cycle (inferred from electronic annotation from HAMAP).
GO:0006099;	Biological process: tricarboxylic acid cycle (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00747; -; 1.
PBIL [Tree]

InterPro

IPR010452; IsoCit_DHase_AceK.
Graphical view of domain structure.

Pfam

PF06315; AceK; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000719; AceK; 1.

BLOCKS

P11071.

Genome annotation databases

GeneID

944797; -.

GenomeReviews

U00096_GR; b4016.
AP009048_GR; JW3976.

KEGG

ecj:JW3976; -.
eco:b4016; -.

Phylogenomic databases

HOGENOM

P11071; -.

Genome annotation databases

CMR

P11071; b4016.

Other

ProtoNet

P11071.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Glyoxylate bypass; Hydrolase; Kinase; Nucleotide-binding; Protein phosphatase; Transferase; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 578`	`578`	`Isocitrate dehydrogenase kinase/phosphatase.`	`PRO_0000057898`
`NP_BIND`	`315 321`	`7`	`ATP (By similarity).`
`ACT_SITE`	`371 371`		`Probable.`
`BINDING`	`336 336`		`ATP (By similarity).`
`MUTAGEN`	`336 336`		`K->M: Inhibits enzyme.`
`MUTAGEN`	`371 371`		`D->A,E,Q: Loss of activity.`
`MUTAGEN`	`377 377`		`N->A: No loss of activity.`
`MUTAGEN`	`403 403`		`D->A: No loss of activity.`
`MUTAGEN`	`439 439`		`E->A: No loss of activity.`
`CONFLICT`	`140 140`		`A -> G (in Ref. 2; AAA24007).`
`CONFLICT`	`416 417`		`ER -> DG (in Ref. 1; AAA24010).`

Sequence information

Length: 578 AA [This is the length of the unprocessed precursor]

Molecular weight: 67699 Da [This is the MW of the unprocessed precursor]

CRC64: 5ABD5FB5FA1D9B29 [This is a checksum on the sequence]

        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

P11071 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools