C1NAN7 (C1NAN7_9ESCH) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Isocitrate dehydrogenase kinase/phosphatase HAMAP MF_00747
Short name=IDH kinase/phosphatase HAMAP MF_00747
Short name=IDHK/P HAMAP MF_00747
EC=2.7.11.5 HAMAP MF_00747
EC=3.1.3.- HAMAP MF_00747

Gene names

Name:	aceK HAMAP MF_00747
ORF Names:	ESCG_00774 EMBL EEH72116.1

Organism

Escherichia sp. 1_1_43 EMBL EEH72116.1

Taxonomic identifier

457400 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	578 AA.
Sequence status	Complete.
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. HAMAP MF_00747 SAAS SAAS010452
Catalytic activity	ATP + [isocitrate dehydrogenase (NADP+)] = ADP + [isocitrate dehydrogenase (NADP+)] phosphate. HAMAP MF_00747 SAAS SAAS010452
Subcellular location	Cytoplasm By similarity HAMAP MF_00747 SAAS SAAS010452.
Sequence similarities	Belongs to the AceK family. HAMAP MF_00747

Ontologies

Keywords
Biological process	Glyoxylate bypass HAMAP MF_00747 SAAS SAAS010452 Tricarboxylic acid cycle HAMAP MF_00747 SAAS SAAS010452
Cellular component	Cytoplasm HAMAP MF_00747 SAAS SAAS010452
Ligand	ATP-binding HAMAP MF_00747 SAAS SAAS010452 NADP HAMAP MF_00747 Nucleotide-binding
Molecular function	Hydrolase Kinase HAMAP MF_00747 SAAS SAAS010452 EMBL EEH72116.1 Protein phosphatase HAMAP MF_00747 SAAS SAAS010452 Transferase
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...

Sequences

	Sequence		Length	Mass (Da)
	C1NAN7 [UniParc]. Last modified May 26, 2009. Version 1. 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

[1]

"The Genome Sequence of Escherichia sp. strain 1_1_43." The Broad Institute Genome Sequencing Platform Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C. , Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., Lander E., Nusbaum C., Galagan J., Birren B. Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: 1_1_43 EMBL EEH72116.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	GG665811 Genomic DNA. Translation: EEH72116.1.
3D structure databases
ProteinModelPortal	C1NAN7.
SMR	C1NAN7. Positions 2-574.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
PATRIC	31131357. VBIEscSp5885_0285.
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...

Entry information

Entry name

C1NAN7_9ESCH

Accession

Primary (citable) accession number: C1NAN7

Entry history

Integrated into UniProtKB/TrEMBL:	May 26, 2009
Last sequence update:	May 26, 2009
Last modified:	January 25, 2012
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)