Reviewed, UniProtKB/Swiss-Prot O94229 (IDH1_KLULA)

Names and origin

Protein names

Recommended name:
    Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial
    EC=1.1.1.41
Alternative name(s):
    Isocitric dehydrogenase
    NAD(+)-specific ICDH

Gene names

Name:	IDH1
Ordered Locus Names:	KLLA0F04103g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Performs an essential role in the oxidative function of the citric acid cycle By similarity.
Catalytic activity	Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH.
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity.
Subunit structure	Octamer of two non-identical subunits IDH1 and IDH2 By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Magnesium Manganese Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro isocitrate dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding 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
	Transit peptide	1 – 12	12	Mitochondrion By similarity
	Chain	13 – 361	349	Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial		PRO_0000014429
Sites
	Metal binding	229	1	Magnesium or manganese By similarity
	Binding site	110	1	Substrate By similarity
	Binding site	141	1	Substrate By similarity
	Binding site	229	1	Substrate By similarity
	Site	148	1	Critical for catalysis By similarity
	Site	195	1	Critical for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	O94229-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 7F3D7F7C5406ECAB	FASTA	361	39,158
	10 20 30 40 50 60 MLRQGIAAQK KSFATLAAEQ LLPKKYGGRY TVTLIPGDGV GKEVTDSVVK IFENENIPID 70 80 90 100 110 120 WETIDISGLE NTENVQRAVE SLKRNKVGLK GIWHTPADQT GHGSLNVALR KQLDIFANVA 130 140 150 160 170 180 LFKSIPGVKT RLNNIDMVII RENTEGEYSG LEHESVPGVV ESLKIMTRAK SERIARFAFD 190 200 210 220 230 240 FALKNNRKSV CAVHKANIMK LGDGLFRNTV NEIGANEYPE LDVKNIIVDN ASMQAVAKPH 250 260 270 280 290 300 QFDVLVTPNL YGSILGNIGS ALIGGPGLVP GANFGREYAV FEPGSRHVGL DIKGQNVANP 310 320 330 340 350 360 TAMILSSTLM LRHLGLNAYA DRISKATYDV ISEGKSTTRD IGGSASTSEF TNAVIEKLAK L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and RNA-binding analysis of NAD+ -isocitrate dehydrogenases from Kluyveromyces lactis and Schizosaccharomyces pombe." Elzinga S.D.J., van Oosterum K., Maat C., Grivell L.A., van der Spek H. Curr. Genet. 38:87-94(2000) [PubMed: 10975257] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC MYA-539 / JBD100.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF045153 Genomic DNA. Translation: AAC69608.1. CR382126 Genomic DNA. Translation: CAG97974.1.
RefSeq	XP_455266.1.
3D structure databases
SMR	O94229. Positions 18-361.
ModBase	Search...
Protein-protein interaction databases
STRING	O94229.
Genome annotation databases
GeneID	2894997.
GenomeReviews	Gene locus KLLA0F04103g in contig CR382126_GR.
KEGG	kla:KLLA0F04103g.
Phylogenomic databases
eggNOG	fuNOG04063.
HOGENOM	HBG518924.
OMA	TAMILSS.
OrthoDB	EOG9BK6MD.
PhylomeDB	O94229.
Enzyme and pathway databases
BRENDA	1.1.1.41. 74088.
Family and domain databases
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004434. Isocitrate_DH_NAD_mit. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHER	PTHR11835. IDH_IMDH_dimeric. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR00175. mito_nad_idh. 1 hit.
PROSITE	PS00470. IDH_IMDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IDH1_KLULA

Accession

Primary (citable) accession number: O94229

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	May 1, 1999
Last modified:	February 9, 2010
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)