ID IDH3B_HUMAN Reviewed; 385 AA. AC O43837; O95106; Q5JXS8; Q9NQ06; Q9NQ07; Q9UEX0; Q9UG99; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 07-JUL-2009, entry version 95. DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial; DE EC=1.1.1.41; DE AltName: Full=Isocitric dehydrogenase; DE AltName: Full=NAD(+)-specific ICDH; DE Flags: Precursor; GN Name=IDH3B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND VARIANT VAL-3. RC TISSUE=Heart; RA Ko H.-J., Kim Y.-O., Park H., Oh I., Yeo S., Hong S., Chae B., Kim S., RA Son B., Lee Y., Yeo H., Huh T.-L.; RT "Mitochondrial NAD+-specific isocitrate dehydrogenase."; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND VARIANT VAL-3. RA Ko H.-J., Kim Y.-O., Huh T.-L.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-385 (ISOFORM B). RC TISSUE=Uterus; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., RA Ottenwalder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [7] RP VARIANT RP46 PRO-132. RX PubMed=18806796; DOI=10.1038/ng.223; RA Hartong D.T., Dange M., McGee T.L., Berson E.L., Dryja T.P., RA Colman R.F.; RT "Insights from retinitis pigmentosa into the roles of isocitrate RT dehydrogenases in the Krebs cycle."; RL Nat. Genet. 40:1230-1234(2008). CC -!- CATALYTIC ACTIVITY: Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + CC NADH. CC -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By CC similarity). CC -!- SUBUNIT: Heterooligomer of subunits alpha, beta, and gamma in the CC apparent ratio of 2:1:1 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=O43837-1; Sequence=Displayed; CC Name=A; CC IsoId=O43837-2; Sequence=VSP_002462; CC -!- DISEASE: Defects in IDH3B are the cause of retinitis pigmentosa CC type 46 (RP46) [MIM:612572]. RP is a retinal dystrophy belonging CC to the group of pigmentary retinopathies. RP is characterized by CC retinal pigment deposits visible on fundus examination and primary CC loss of rod photoreceptor cells followed by secondary loss of cone CC photoreceptors. Patients typically have night vision blindness and CC loss of midperipheral visual field. As their condition progresses, CC they lose their far peripheral visual field and eventually central CC vision as well. CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U49283; AAB94295.1; -; mRNA. DR EMBL; AF023265; AAD09339.1; -; mRNA. DR EMBL; AF023266; AAD09340.1; -; mRNA. DR EMBL; AL049712; CAC01442.2; -; Genomic_DNA. DR EMBL; AL049712; CAC01443.1; -; Genomic_DNA. DR EMBL; BC001960; AAH01960.1; -; mRNA. DR EMBL; AL050094; CAB43266.1; -; mRNA. DR IPI; IPI00304417; -. DR IPI; IPI00304419; -. DR PIR; T08743; T08743. DR PIR; T13147; T13147. DR RefSeq; NP_008830.2; -. DR RefSeq; NP_777280.1; -. DR UniGene; Hs.436405; -. DR HSSP; P39126; 1HQS. DR IntAct; O43837; 8. DR PhosphoSite; O43837; -. DR PRIDE; O43837; -. DR Ensembl; ENSG00000101365; Homo sapiens. DR GeneID; 3420; -. DR KEGG; hsa:3420; -. DR NMPDR; fig|9606.3.peg.19736; -. DR UCSC; uc002wgp.1; human. DR UCSC; uc002wgq.1; human. DR GeneCards; GC20M002587; -. DR H-InvDB; HIX0015578; -. DR HGNC; HGNC:5385; IDH3B. DR MIM; 604526; gene. DR MIM; 612572; phenotype. DR Orphanet; 791; Retinitis pigmentosa. DR PharmGKB; PA29633; -. DR HOVERGEN; O43837; -. DR OMA; O43837; TTTDFIK. DR BRENDA; 1.1.1.41; 247. DR Reactome; REACT_1046; Pyruvate metabolism and TCA cycle. DR Reactome; REACT_1505; Integration of energy metabolism. DR Reactome; REACT_15380; Diabetes pathways. DR DrugBank; DB00157; NADH. DR NextBio; 13482; -. DR Bgee; O43837; -. DR CleanEx; HS_IDH3B; -. DR GermOnline; ENSG00000101365; Homo sapiens. DR GO; GO:0005759; C:mitochondrial matrix; EXP:Reactome. DR GO; GO:0009055; F:electron carrier activity; TAS:UniProtKB. DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; TAS:ProtInc. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro. DR GO; GO:0006102; P:isocitrate metabolic process; TAS:ProtInc. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH. DR InterPro; IPR004434; Isocitrate_DH_NAD_mit. DR Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1. DR PANTHER; PTHR11835; IDH_IMDH_dimeric; 1. DR Pfam; PF00180; Iso_dh; 1. DR TIGRFAMs; TIGR00175; mito_nad_idh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Disease mutation; Magnesium; KW Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase; KW Polymorphism; Retinitis pigmentosa; Sensory transduction; KW Transit peptide; Tricarboxylic acid cycle; Vision. FT TRANSIT 1 34 Mitochondrion (By similarity). FT CHAIN 35 385 Isocitrate dehydrogenase [NAD] subunit FT beta, mitochondrial. FT /FTId=PRO_0000014444. FT METAL 251 251 Magnesium or manganese (By similarity). FT BINDING 133 133 Substrate (By similarity). FT BINDING 164 164 Substrate (By similarity). FT BINDING 251 251 Substrate (By similarity). FT SITE 171 171 Critical for catalysis (By similarity). FT SITE 218 218 Critical for catalysis (By similarity). FT VAR_SEQ 361 385 RDMGGYSTTTDFIKSVIGHLQTKGS -> SDMGGYATCHDF FT TEAVIAALPHP (in isoform A). FT /FTId=VSP_002462. FT VARIANT 3 3 A -> V (in dbSNP:rs3178817). FT /FTId=VAR_022660. FT VARIANT 132 132 L -> P (in RP46). FT /FTId=VAR_054851. FT VARIANT 166 166 Q -> H (in dbSNP:rs11542741). FT /FTId=VAR_049781. FT VARIANT 360 360 T -> A (in dbSNP:rs8296). FT /FTId=VAR_056005. FT CONFLICT 127 130 SYDM -> RTLV (in Ref. 5). FT CONFLICT 385 385 S -> SNL (in Ref. 2; AAD09340). SQ SEQUENCE 385 AA; 42184 MW; 7324E6CC30A68EE2 CRC64; MAALSGVRWL TRALVSAGNP GAWRGLSTSA AAHAASRSQA EDVRVEGSFP VTMLPGDGVG PELMHAVKEV FKAAAVPVEF QEHHLSEVQN MASEEKLEQV LSSMKENKVA IIGKIHTPME YKGELASYDM RLRRKLDLFA NVVHVKSLPG YMTRHNNLDL VIIREQTEGE YSSLEHESAR GVIECLKIVT RAKSQRIAKF AFDYATKKGR GKVTAVHKAN IMKLGDGLFL QCCEEVAELY PKIKFETMII DNCCMQLVQN PYQFDVLVMP NLYGNIIDNL AAGLVGGAGV VPGESYSAEY AVFETGARHP FAQAVGRNIA NPTAMLLSAS NMLRHLNLEY HSSMIADAVK KVIKVGKVRT RDMGGYSTTT DFIKSVIGHL QTKGS //