Isocitrate dehydrogenase kinase/phosphatase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P11071 (ACEK_ECOLI)

Last modified June 15, 2010. Version 96. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and originHide

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

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Protein attributesHide

Sequence length	578 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)Hide

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. HAMAP MF_00747
Catalytic activity	ATP + [isocitrate dehydrogenase (NADP⁺)] = ADP + [isocitrate dehydrogenase (NADP⁺)] phosphate. HAMAP MF_00747
Subcellular location	Cytoplasm HAMAP MF_00747.
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.

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OntologiesHide

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Cellular component	Cytoplasm
Ligand	ATP-binding NADP 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 peptidyl-serine phosphorylation Inferred from direct assay. Source: UniProtKB regulation of catalytic activity Inferred from direct assay. Source: UniProtKB tricarboxylic acid cycle Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from direct assay. Source: UniProtKB [isocitrate dehydrogenase (NADP+)] kinase activity Inferred from direct assay. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay. Source: UniProtKB protein serine/threonine phosphatase activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)Hide

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 578

578

Isocitrate dehydrogenase kinase/phosphatase HAMAP MF_00747

PRO_0000057898

Regions

Nucleotide binding

315 – 321

ATP By similarity

Sites

Active site

371

Probable

Binding site

336

ATP By similarity

Experimental info

Mutagenesis

336

K → M: Inhibits enzyme. Ref.8

Mutagenesis

371

D → A, E or Q: Loss of activity. Ref.9

Mutagenesis

377

N → A: No loss of activity. Ref.9

Mutagenesis

403

D → A: No loss of activity. Ref.9

Mutagenesis

439

E → A: No loss of activity. Ref.9

Sequence conflict

140

A → G in AAA24007. Ref.2

Sequence conflict

416 – 417

ER → DG in AAA24010. Ref.1

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SequencesHide

Sequence

Length

Mass (Da)

Tools

P11071-1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 5ABD5FB5FA1D9B29
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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

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ReferencesHide

	« 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.

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Cross-referencesHide

Sequence databases
EMBL GenBank DDBJ	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-protein interaction databases
STRING	P11071.
Protein family/group databases
PptaseDB	P3D0409136.
Genome annotation databases
EnsemblBacteria	EBESCT00000002125; EBESCP00000002125; EBESCG00000001741. EBESCT00000016793; EBESCP00000016084; EBESCG00000015852.
GeneID	944797.
GenomeReviews	Gene locus JW3976 in contig AP009048_GR. Gene locus b4016 in contig U00096_GR.
KEGG	ecj:JW3976. eco:b4016.
Organism-specific databases
EchoBASE	EB0025.
EcoGene	EG10026. aceK.
CMR	Search...
Phylogenomic databases
eggNOG	COG4579.
HOGENOM	HBG298593.
OMA	RMTPLNI.
ProtClustDB	PRK02946.
Enzyme and pathway databases
BioCyc	EcoCyc:ICITDEHASE-KIN-PHOSPHA. ECOL168927:B4016-MONOMER. MetaCyc:ICITDEHASE-KIN-PHOSPHA.
Gene expression databases
Genevestigator	P11071.
Family and domain databases
HAMAP	MF_00747. AceK. [Tree]
InterPro	IPR010452. Isocitrate_DH_AceK. [Graphical view]
Pfam	PF06315. AceK. 1 hit. [Graphical view]
PIRSF	PIRSF000719. AceK. 1 hit.
ProDom	PD043552. Isocitrate_DH_AceK. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

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Entry informationHide

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:	June 15, 2010
This is version 96 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)

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Relevant documentsHide

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names and originHide

Protein attributesHide

General annotation (Comments)Hide

OntologiesHide

Sequence annotation (Features)Hide

Molecule processing

Regions

Sites

Experimental info

SequencesHide

ReferencesHide

Cross-referencesHide

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry informationHide

Relevant documentsHide