Reviewed, UniProtKB/Swiss-Prot Q5QWZ3 (ACEK_IDILO)

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:	IL0607

Organism

Idiomarina loihiensis [Complete proteome] [HAMAP]

Taxonomic identifier

135577 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Idiomarinaceae › Idiomarina

Protein attributes

Sequence length	564 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 – 564	564	Isocitrate dehydrogenase kinase/phosphatase HAMAP MF_00747		PRO_0000288288
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)
	Q5QWZ3-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 2E02538C5250F59D	FASTA	564	65,928
	10 20 30 40 50 60 MTISPETLAK SILDGFHSHY RRFQVLTQGA RERFLKRDWT AVVSAASERI HYYDHQVGTT 70 80 90 100 110 120 AKKVERRVGT ELDEGLWLAT RQRYQQLLKF HPQAELAETF YNSVFCRVFD RAYFNNDYIF 130 140 150 160 170 180 VETVLANHIP VPVENECHSY FPVVDGLEGT LTRVFEDIGL GGEFENFEND IEQLRDKFFE 190 200 210 220 230 240 RATETDIEAH NLRIDVLKSP FYRNKAAYIV GRVVTENNHY PFIVPVLINS QGKLYVDAFI 250 260 270 280 290 300 TRSDRMATIF GFARSYFMVE TEAPSALVRF LKDLMPHKTL AELYSSVGFH KQGKTEFYRE 310 320 330 340 350 360 FLHHLRRTDD QLSAAPGVKG MVMTVFTLPS FPYVFKVIKD RLGGTKEFGR QTVIDRYRMV 370 380 390 400 410 420 KRHDRVGRMA DTLEFVDVAL PLKRISADLL DEFKQTIANS ISIEGDTLVI HQLFVERRMT 430 440 450 460 470 480 PLNLYLEYAN DEEVDAAMDD YGRALKEMMA ANIFPGDMLL KNFGVTRHKR VVFYDYDEVR 490 500 510 520 530 540 YLTDMSFRRL PENDWEVSYA PDDVFPQQLA QFAVPQAKYR NKLLKRHPEL IDSAYWCRVQ 550 560 KNIRKGELTD VFPYDADLRF TRRF

References

[1]

"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy." Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. , Aizawa S., Shibata S., Malahoff A., Alam M. Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: L2-TR / ATCC BAA-735 / DSM 15497.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017340 Genomic DNA. Translation: AAV81448.1.
RefSeq	YP_154997.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3173236.
GenomeReviews	Gene locus IL0607 in contig AE017340_GR.
KEGG	ilo:IL0607.
NMPDR	fig|283942.3.peg.545.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5QWZ3.
OMA	FYRDFLH.
Enzyme and pathway databases
BioCyc	ILOI283942:IL0607-MON.
BRENDA	2.7.11.5. 280818.
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_IDILO

Accession

Primary (citable) accession number: Q5QWZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	January 4, 2005
Last modified:	November 3, 2009
This is version 28 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)