ID C1F8G5_ACIC5 Unreviewed; 466 AA. AC C1F8G5; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 79. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446}; DE EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446}; GN Name=icd1 {ECO:0000313|EMBL:ACO34056.1}; GN OrderedLocusNames=ACP_0089 {ECO:0000313|EMBL:ACO34056.1}; OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM OS 7670 / NBRC 15755 / NCIMB 13165 / 161). OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae; OC Acidobacterium. OX NCBI_TaxID=240015 {ECO:0000313|EMBL:ACO34056.1, ECO:0000313|Proteomes:UP000002207}; RN [1] {ECO:0000313|EMBL:ACO34056.1, ECO:0000313|Proteomes:UP000002207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 / RC NCIMB 13165 / 161 {ECO:0000313|Proteomes:UP000002207}; RX PubMed=19201974; DOI=10.1128/AEM.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). CC -!- CATALYTIC ACTIVITY: CC Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH; CC Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42; CC Evidence={ECO:0000256|ARBA:ARBA00023554}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000256|PIRSR:PIRSR604439-3}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001472; ACO34056.1; -; Genomic_DNA. DR RefSeq; WP_012680497.1; NC_012483.1. DR AlphaFoldDB; C1F8G5; -. DR STRING; 240015.ACP_0089; -. DR KEGG; aca:ACP_0089; -. DR eggNOG; COG0538; Bacteria. DR HOGENOM; CLU_031953_7_1_0; -. DR InParanoid; C1F8G5; -. DR OrthoDB; 9806254at2; -. DR Proteomes; UP000002207; Chromosome. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 2. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR NCBIfam; TIGR00183; prok_nadp_idh; 1. DR PANTHER; PTHR43504; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR PANTHER; PTHR43504:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 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 3: Inferred from homology; KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435, KW ECO:0000256|RuleBase:RU004446}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604439-3}; KW Manganese {ECO:0000256|PIRSR:PIRSR604439-3, ECO:0000256|RuleBase:RU004446}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU004446}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR604439-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000313|EMBL:ACO34056.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002207}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, KW ECO:0000256|RuleBase:RU004446}. FT DOMAIN 31..462 FT /note="Isopropylmalate dehydrogenase-like" FT /evidence="ECO:0000259|SMART:SM01329" FT BINDING 105 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 114 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 116 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 120 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 130 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 154 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1" FT BINDING 357 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3" FT BINDING 389..395 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 402 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 441 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT BINDING 445 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2" FT SITE 161 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4" FT SITE 232 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4" FT MOD_RES 101 FT /note="N6-succinyllysine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" FT MOD_RES 114 FT /note="Phosphoserine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" FT MOD_RES 143 FT /note="N6-acetyllysine" FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5" SQ SEQUENCE 466 AA; 51501 MW; 4E35E746973523BB CRC64; MQASYNGVSL PEGGQPITYS GGKYTVPDHP IIPFIEGDGT GRDIWRASQR VFDAAVHKAY GGQRSVKWFE IFAGEKAFRE FKTWLPDDSV KAATDLRVSI KGPLTTPVGG GIRSLNVALR QIMDLYACVR PVKYYAGVPS PVKHPEKLDV VIFRENTEDV YAGIEFKQGT PEAKKLIDFL NDEMLKGGKK KVRSDSGVGI KPISITGTKR LVRYAIQYAI ENGRRSVTLV HKGNIQKFTE GAFREWGYEV AVEEFREHVV TERESWILGN AEANPGLTVE QNAAMIEPGL EFGSEDFRKD LYAEIKGVLD SIGQSHGAGK WKQKILINDR IADSIFQQVI IRPDEYDILA CPNLNGDYIS DACAAQVGGL GIAPGANIGD GYAVFEATHG TAPKYADKDV INPGSVMLSG VMMFEFLGWK EAARLIESAM EKTIQQKHVT YDFERQMPGA TKVKTSEFAT KMIENM //