Reviewed, UniProtKB/Swiss-Prot Q54B68 (IDHB_DICDI)

Names and origin

Protein names

Recommended name:
    Isocitrate dehydrogenase [NAD] regulatory subunit B, mitochondrial
    EC=1.1.1.41

Gene names

Name:	idhB
ORF Names:	DDB_0231294

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	360 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 + CO(2) + NADH.
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity.
Subunit structure	Heteroligomer of catalytic and regulatory subunits.
Subcellular location	MitochondrionBy 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	isocitrate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	isocitrate dehydrogenase (NAD+) activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Transit peptide	1 – 113	113	Mitochondrion Potential
	Chain	114 – 360	247	Isocitrate dehydrogenase [NAD] regulatory subunit B, mitochondrial
Regions
	Nucleotide binding	284 – 290	7	NADP By similarity
Sites
	Metal binding	227	1	Magnesium or manganese By similarity
	Binding site	101	1	Substrate By similarity
	Binding site	103	1	Substrate By similarity
	Binding site	107	1	Substrate By similarity
	Binding site	140	1	Substrate By similarity
	Binding site	297	1	NADP; via amide nitrogen and carbonyl oxygen By similarity
	Site	147	1	Critical for catalysis By similarity
	Site	194	1	Critical for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54B68-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 23CA6A3540462C19	FASTA	360	38,688
	10 20 30 40 50 60 MLGRLRTVVK ASSSNSIRNY LGYTSGVQKK TVTVIPGDGI GPEITSSVMG VFQAAKVPIE 70 80 90 100 110 120 WEIFDISGGQ PISQELIASI TRNKVALKGP LYTEILSGSQ SRNMELRKAL DLYAHVVPCK 130 140 150 160 170 180 QIPGITARHD DVLVDFVVIR ENTQGEYSGL EQVLTPGVVQ SLKIITKEAS ERIARYAFEY 190 200 210 220 230 240 AKANGRKKVT AVHKANIQKQ TDGLFLATCT QIAKEYPEIK FENTIIDNCC MQLVKSPEQY 250 260 270 280 290 300 DVMVTPNLYG NIVSNIGAAL VGGPGLAGGA NVGEGSIIFE MGAHHVAADI AGKDKANPTG 310 320 330 340 350 360 LLLASVMMLK HLGLNEHATK VENAVKAVIK EGTLTSDIGG KSSTKQFTGA VIDYIEKNQN

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000223 Genomic DNA. Translation: EAL60507.1.
RefSeq	XP_628920.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3385582.
KEGG	ddi:DDB_0231294.
Organism-specific databases
dictyBase	DDB0231294. idhB.
Family and domain databases
InterPro	IPR004434. IsoCit_DHase_NAD_mit. IPR001804. IsoCit_IM_DHase. [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]
ProDom	Q54B68. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

IDHB_DICDI

Accession

Primary (citable) accession number: Q54B68

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	July 22, 2008
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)