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Database: UniProt
Entry: O15385_HUMAN
LinkDB: O15385_HUMAN
Original site: O15385_HUMAN 
ID   O15385_HUMAN            Unreviewed;       210 AA.
AC   O15385;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   SubName: Full=NAD (H)-specific isocitrate dehydrogenase gamma subunit {ECO:0000313|EMBL:AAB70116.1};
DE   Flags: Fragment;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:AAB70116.1};
RN   [1] {ECO:0000313|EMBL:AAB70116.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Soares liver spleen 1NFLS {ECO:0000313|EMBL:AAB70116.1};
RX   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 to
RT   head arrangement of IDH gamma and TRAP delta is conserved in rat and
RT   mouse.";
RL   Genomics 44:8-14(1997).
CC   -!- SUBUNIT: Heterooligomer of subunits alpha (IDH3A), beta (IDH3B), and
CC       gamma (IDH3G) in the apparent ratio of 2:1:1. The heterodimer
CC       containing one IDH3A and one IDH3B subunit and the heterodimer
CC       containing one IDH3A and one IDH3G subunit assemble into a
CC       heterotetramer (which contains two subunits of IDH3A, one of IDH3B and
CC       one of IDH3G) and further into the heterooctamer.
CC       {ECO:0000256|ARBA:ARBA00011525}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR   EMBL; U69269; AAB70116.1; -; mRNA.
DR   AlphaFoldDB; O15385; -.
DR   SMR; O15385; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; NAS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR   PANTHER; PTHR11835:SF42; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT GAMMA, MITOCHONDRIAL; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   2: Evidence at transcript level;
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          1..196
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAB70116.1"
SQ   SEQUENCE   210 AA;  22706 MW;  2F83A837F5A59B1B CRC64;
     KSLRIAEYAF KLAQESGRKK VTAVHKANIM KLGDGLFLQC CREVAARYPQ ITFENMIVDN
     TTMQLVSRPQ QFDVMVMPNL YGNIVNNVCA GLVGGPGLVA GANYGHVYAV FETATRNTGK
     SIANKNIANP TATLLASCMM LDHLKLHSYA TSIRKAVLAS MDNENGLVCA EPACVLQMHT
     PDIGGQGTTS EAIQDVIRHI RVINGRAVEA
//
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