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UniProtKB/Swiss-Prot entry Q54B68

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IDHB_DICDI
Primary accession number Q54B68
Secondary accession numbers None
Integrated into Swiss-Prot on April 8, 2008
Sequence was last modified on May 24, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 22)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NAD] regulatory subunit B, mitochondrial [Precursor]
Synonym EC 1.1.1.41
Gene name
Name: idhB
ORFNames: DDB_0231294
From
Dictyostelium discoideum (Slime mold) [TaxID: 44689] 
Taxonomy Eukaryota; Mycetozoa; Dictyosteliida; Dictyostelium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
DOI=10.1038/nature03481; PubMed=15875012 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AAFI02000223; EAL60507.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_628920.1; -.
3D structure databases
ModBase Q54B68.
Organism-specific databases
dictyBase DDB0231294; idhB.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from sequence or structural similarity from UniProtKB).
GO:0004449; Molecular function: isocitrate dehydrogenase (NAD+) activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006102; Biological process: isocitrate metabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR004434; IsoCit_DHase_NAD_mit.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11835; IDH_IMDH_dimeric; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00175; mito_nad_idh; 1.
PROSITE PS00470; IDH_IMDH; 1.
BLOCKS Q54B68.
Genome annotation databases
GeneID 3385582; -.
KEGG ddi:DDB_0231294; -.
Other
ProtoNet Q54B68.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1   113  113     Mitochondrion (Potential). 
CHAIN   114   360  247     Isocitrate dehydrogenase [NAD] regulatory subunit B, mitochondrial. PRO_0000328019
NP_BIND   284   290  7     NADP (By similarity). 
METAL   227   227        Magnesium or manganese (By similarity). 
BINDING   101   101        Substrate (By similarity). 
BINDING   103   103        Substrate (By similarity). 
BINDING   107   107        Substrate (By similarity). 
BINDING   140   140        Substrate (By similarity). 
BINDING   297   297        NADP; via amide nitrogen and carbonyl oxygen (By similarity). 
SITE   147   147  1     Critical for catalysis (By similarity). 
SITE   194   194  1     Critical for catalysis (By similarity). 
Sequence information
Length: 360 AA [This is the length of the unprocessed precursor] Molecular weight: 38688 Da [This is the MW of the unprocessed precursor] CRC64: 23CA6A3540462C19 [This is a checksum on the sequence] 
        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
Q54B68 in FASTA format

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