Reviewed, UniProtKB/Swiss-Prot B7MIZ8 (ACEK_ECO45)

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:	ECS88_4481

Organism

Escherichia coli O45:K1 (strain S88 / ExPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

585035 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	574 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 By similarity.
Catalytic activity	ATP + [isocitrate dehydrogenase (NADP+)] = ADP + [isocitrate dehydrogenase (NADP+)] phosphate. HAMAP MF_00747
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the aceK family.

Ontologies

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
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: UniProtKB-SubCell
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 – 574	574	Isocitrate dehydrogenase kinase/phosphatase HAMAP MF_00747		PRO_1000133264
Regions
	Nucleotide binding	315 – 321	7	ATP By similarity
Sites
	Active site	371	1	By similarity
	Binding site	336	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7MIZ8-1 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: 8285CBDABE00D7EB	FASTA	574	67,206
	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 RDIHYIVRHL 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 PLPRYPEDEL ASEPWYSVSP GDVFPEEFRH WLCADPRIGP LFEEMHADLF 550 560 570 RADYWRALQN RIREGHVEDV YAYRRRQRFS VRFV

References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed: 19165319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU928161 Genomic DNA. Translation: CAR05642.1.
RefSeq	YP_002393991.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	7132030.
GenomeReviews	Gene locus ECS88_4481 in contig CU928161_GR.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_00747. [Tree]
InterPro	IPR010452. Isocitrate_DH_AceK. [Graphical view]
Pfam	PF06315. AceK. 1 hit. [Graphical view]
PIRSF	PIRSF000719. AceK. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ACEK_ECO45

Accession

Primary (citable) accession number: B7MIZ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	June 16, 2009
This is version 7 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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