ID IDHA_DICDI Reviewed; 354 AA. AC Q55BI2; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 25-NOV-2008, entry version 23. DE RecName: Full=Isocitrate dehydrogenase [NAD] regulatory subunit A, mitochondrial; DE EC=1.1.1.41; DE Flags: Precursor; GN Name=idhA; ORFNames=DDB_G0271344; OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX MEDLINE=22092622; PubMed=12097910; DOI=10.1038/nature00847; RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., RA Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., RA Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., RA Platzer M., Rosenthal A., Noegel A.A.; RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum."; RL Nature 418:79-85(2002). RN [2] 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., RA Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., RA Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., RA Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., RA Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., RA Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., RA Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., RA Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., RA Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., RA 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., RA Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., RA Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., RA Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., RA Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., RA Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., RA Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., RA 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 CC the citric acid cycle (By similarity). 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: Heteroligomer of catalytic and regulatory subunits (By CC similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). 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; AAFI02000006; EAL71802.1; -; Genomic_DNA. DR RefSeq; XP_645630.1; -. DR GeneID; 3396844; -. DR KEGG; ddi:DDB_0231288; -. DR dictyBase; DDB_G0271344; idhA. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. 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: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 InterPro; IPR010916; TonB_box_CS. 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 3: Inferred from homology; KW Complete proteome; Magnesium; Manganese; Metal-binding; Mitochondrion; KW NAD; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 354 Isocitrate dehydrogenase [NAD] regulatory FT subunit A, mitochondrial. FT /FTId=PRO_0000328018. FT NP_BIND 276 282 NADP (By similarity). FT METAL 243 243 Magnesium or manganese (By similarity). FT BINDING 95 95 Substrate (By similarity). FT BINDING 97 97 Substrate (By similarity). FT BINDING 101 101 Substrate (By similarity). FT BINDING 111 111 Substrate (By similarity). FT BINDING 132 132 Substrate (By similarity). FT BINDING 289 289 NADP; via amide nitrogen and carbonyl FT oxygen (By similarity). FT SITE 139 139 Critical for catalysis (By similarity). FT SITE 186 186 Critical for catalysis (By similarity). SQ SEQUENCE 354 AA; 38341 MW; 07BC0DC939425EBE CRC64; MFSRKSLSIF STLRNYSSST SKIQKVTLIP GDGIGPEISE SVKRVFSAVK APIEWETVVV DANTGISKEV IESISKNKIG LKGPISTPIG TGHQSLNLGL RKTFNLYANI RPCLSIPGHK TRYNNVNTVV VRENTEGEYS GIENQPVKGV AQSIKIITKE ASTRIAHYAF QYALANGRKK VTCIHKANIM KQSDGLFVKS CREVSTRYPS IKYEELTIDN NCMQLVLDPN QMDVMVLPNL YGDIVSDLCA GLIGGLGLTP SGNIGENGSA IFEAVHGTAP DIAGKNKANP TALILSSIMM LRHLGHFHEA SIIENAVLNT LTEGKVKTGD LGGNSSCSEY TDELVKKITE SLNK //