ID IDH3G_HUMAN Reviewed; 393 AA. AC P51553; Q9BUU5; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 16-DEC-2008, entry version 91. DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial; DE EC=1.1.1.41; DE AltName: Full=Isocitric dehydrogenase; DE AltName: Full=NAD(+)-specific ICDH; DE Flags: Precursor; GN Name=IDH3G; 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 [GENOMIC DNA / MRNA]. RC TISSUE=Brain; RX MEDLINE=97432815; PubMed=9286695; DOI=10.1006/geno.1997.4822; RA Brenner V., Nyakatura G., Rosenthal A., Platzer M.; RT "Genomic organization of two novel genes on human Xq28: compact head RT to head arrangement of IDH gamma and TRAP delta is conserved in rat RT and mouse."; RL Genomics 44:8-14(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Heart; RX MEDLINE=20069662; PubMed=10601238; DOI=10.1074/jbc.274.52.36866; RA Kim Y.-O., Koh H.-J., Kim S.-H., Jo S.-H., Huh J.-W., Jeong K.-S., RA Lee I.J., Song B.J., Huh T.-L.; RT "Identification and functional characterization of a novel, tissue- RT specific NAD+-dependent isocitrate dehydrogenase beta subunit RT isoform."; RL J. Biol. Chem. 274:36866-36875(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta, and Skin; 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 [4] RP SUBCELLULAR LOCATION. RX MEDLINE=21151112; PubMed=11256614; DOI=10.1093/embo-reports/kvd058; RA Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.; RT "Systematic subcellular localization of novel proteins identified by RT large-scale cDNA sequencing."; RL EMBO Rep. 1:287-292(2000). 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 -!- ENZYME REGULATION: Activated by increasing ADP/ATP ratios and by CC Ca(2+) (By 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 -!- 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; Z68907; CAA93143.1; -; mRNA. DR EMBL; Z68129; CAA92214.1; -; Genomic_DNA. DR EMBL; U52111; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U40272; AAD09357.1; -; mRNA. DR EMBL; BC000933; AAH00933.1; -; mRNA. DR EMBL; BC001902; AAH01902.1; -; mRNA. DR RefSeq; NP_004126.1; -. DR UniGene; Hs.410197; -. DR HSSP; P00351; 1XAA. DR PhosphoSite; P51553; -. DR PRIDE; P51553; -. DR Ensembl; ENSG00000067829; Homo sapiens. DR GeneID; 3421; -. DR KEGG; hsa:3421; -. DR GeneCards; GC0XM152704; -. DR H-InvDB; HIX0017139; -. DR HGNC; HGNC:5386; IDH3G. DR HPA; HPA000425; -. DR HPA; HPA002017; -. DR MIM; 300089; gene. DR PharmGKB; PA29634; -. DR HOGENOM; P51553; -. DR HOVERGEN; P51553; -. DR Reactome; REACT_1046; Pyruvate metabolism and TCA cycle. DR DrugBank; DB00157; NADH. DR LinkHub; P51553; -. DR NextBio; 13490; -. DR CleanEx; HS_IDH3G; -. DR GermOnline; ENSG00000067829; Homo sapiens. DR GO; GO:0005759; C:mitochondrial matrix; EXP:Reactome. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; ISS:UniProtKB. 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:0005975; P:carbohydrate metabolic process; NAS:ProtInc. DR GO; GO:0006102; P:isocitrate metabolic process; ISS:UniProtKB. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR InterPro; IPR004434; IsoCit_DHase_NAD_mit. DR InterPro; IPR001804; IsoCit_IM_DHase. 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 2: Evidence at transcript level; KW ATP-binding; Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; KW Nucleotide-binding; Oxidoreductase; Phosphoprotein; Transit peptide; KW Tricarboxylic acid cycle. FT TRANSIT 1 39 Mitochondrion (By similarity). FT CHAIN 40 393 Isocitrate dehydrogenase [NAD] subunit FT gamma, mitochondrial. FT /FTId=PRO_0000014449. FT NP_BIND 56 84 NAD (Potential). FT NP_BIND 309 316 ATP (Potential). FT METAL 254 254 Magnesium or manganese (By similarity). FT BINDING 136 136 Substrate (By similarity). FT BINDING 167 167 Substrate (By similarity). FT BINDING 254 254 Substrate (By similarity). FT SITE 174 174 Critical for catalysis (By similarity). FT SITE 221 221 Critical for catalysis (By similarity). FT MOD_RES 363 363 Phosphothreonine (By similarity). FT CONFLICT 267 267 F -> L (in Ref. 3; AAH01902). SQ SEQUENCE 393 AA; 42794 MW; A0870F2B7D228A37 CRC64; MALKVATVAG SAAKAVLGPA LLCRPWEVLG AHEVPSRNIF SEQTIPPSAK YGGRHTVTMI PGDGIGPELM LHVKSVFRHA CVPVDFEEVH VSSNADEEDI RNAIMAIRRN RVALKGNIET NHNLPPSHKS RNNILRTSLD LYANVIHCKS LPGVVTRHKD IDILIVRENT EGEYSSLEHE SVAGVVESLK IITKAKSLRI AEYAFKLAQE SGRKKVTAVH KANIMKLGDG LFLQCCREVA ARYPQITFEN MIVDNTTMQL VSRPQQFDVM VMPNLYGNIV NNVCAGLVGG PGLVAGANYG HVYAVFETAT RNTGKSIANK NIANPTATLL ASCMMLDHLK LHSYATSIRK AVLASMDNEN MHTPDIGGQG TTSEAIQDVI RHIRVINGRA VEA //