IDHB_DICDI
ID IDHB_DICDI Reviewed; 360 AA.
AC Q54B68;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Isocitrate dehydrogenase [NAD] regulatory subunit B, mitochondrial;
DE EC=1.1.1.41;
DE Flags: Precursor;
GN Name=idhB; ORFNames=DDB_G0293872;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Performs an essential role in the oxidative function of the
CC citric acid cycle. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH;
CC Xref=Rhea:RHEA:23632, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.41;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterooligomer of catalytic and regulatory subunits.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; AAFI02000223; EAL60507.1; -; Genomic_DNA.
DR RefSeq; XP_628920.1; XM_628918.1.
DR AlphaFoldDB; Q54B68; -.
DR SMR; Q54B68; -.
DR STRING; 44689.DDB0231294; -.
DR PaxDb; Q54B68; -.
DR EnsemblProtists; EAL60507; EAL60507; DDB_G0293872.
DR GeneID; 8629462; -.
DR KEGG; ddi:DDB_G0293872; -.
DR dictyBase; DDB_G0293872; idhB.
DR eggNOG; KOG0785; Eukaryota.
DR HOGENOM; CLU_031953_0_0_1; -.
DR InParanoid; Q54B68; -.
DR OMA; TCAHKAN; -.
DR PhylomeDB; Q54B68; -.
DR Reactome; R-DDI-71403; Citric acid cycle (TCA cycle).
DR PRO; PR:Q54B68; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006102; P:isocitrate metabolic process; ISS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004434; Isocitrate_DH_NAD.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase;
KW Reference proteome; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..113
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 114..360
FT /note="Isocitrate dehydrogenase [NAD] regulatory subunit B,
FT mitochondrial"
FT /id="PRO_0000328019"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT BINDING 284..290
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 147
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 194
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 360 AA; 38688 MW; 23CA6A3540462C19 CRC64;
MLGRLRTVVK ASSSNSIRNY LGYTSGVQKK TVTVIPGDGI GPEITSSVMG VFQAAKVPIE
WEIFDISGGQ PISQELIASI TRNKVALKGP LYTEILSGSQ SRNMELRKAL DLYAHVVPCK
QIPGITARHD DVLVDFVVIR ENTQGEYSGL EQVLTPGVVQ SLKIITKEAS ERIARYAFEY
AKANGRKKVT AVHKANIQKQ TDGLFLATCT QIAKEYPEIK FENTIIDNCC MQLVKSPEQY
DVMVTPNLYG NIVSNIGAAL VGGPGLAGGA NVGEGSIIFE MGAHHVAADI AGKDKANPTG
LLLASVMMLK HLGLNEHATK VENAVKAVIK EGTLTSDIGG KSSTKQFTGA VIDYIEKNQN
