ID   Q2GF85_EHRCR            Unreviewed;       482 AA.
AC   Q2GF85;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   02-SEP-2026, entry version 110.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|ARBA:ARBA00019562};
DE            EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013};
DE   AltName: Full=IDP {ECO:0000256|ARBA:ARBA00029765};
DE   AltName: Full=NADP(+)-specific ICDH {ECO:0000256|ARBA:ARBA00029990};
DE   AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|ARBA:ARBA00031098};
GN   OrderedLocusNames=ECH_1114 {ECO:0000313|EMBL:ABD45001.1};
OS   Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rickettsiales; Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=205920 {ECO:0000313|EMBL:ABD45001.1, ECO:0000313|Proteomes:UP000008320};
RN   [1] {ECO:0000313|EMBL:ABD45001.1, ECO:0000313|Proteomes:UP000008320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC CRL-10679 / Arkansas {ECO:0000313|Proteomes:UP000008320};
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
CC   -!- FUNCTION: Catalyzes the oxidative decarboxylation of isocitrate to 2-
CC       oxoglutarate and carbon dioxide with the concomitant reduction of
CC       NADP(+). {ECO:0000256|ARBA:ARBA00046127}.
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|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR   EMBL; CP000236; ABD45001.1; -; Genomic_DNA.
DR   RefSeq; WP_006011301.1; NC_007799.1.
DR   AlphaFoldDB; Q2GF85; -.
DR   STRING; 205920.ECH_1114; -.
DR   KEGG; ech:ECH_1114; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_1_1_5; -.
DR   OrthoDB; 9767905at2; -.
DR   Proteomes; UP000008320; Chromosome.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:TreeGrafter.
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:InterPro.
DR   GO; GO:0006102; P:isocitrate metabolic process; IEA:TreeGrafter.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   FunFam; 3.40.718.10:FF:000020; Isocitrate dehydrogenase; 1.
DR   Gene3D; 3.30.70.1570; -; 1.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR014273; Isocitrate_DH_bac-typ.
DR   InterPro; IPR040978; Isocitrate_DH_TT1725_C.
DR   InterPro; IPR046997; Isocitrate_DH_TT1725_C_sf.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   NCBIfam; TIGR02924; ICDH_alpha; 1.
DR   NCBIfam; NF006673; PRK09222.1; 1.
DR   PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR   PANTHER; PTHR11835:SF43; ISOPROPYLMALATE DEHYDROGENASE-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   Pfam; PF18324; Isocitrate_DH_C_bact; 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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008320};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          4..335
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   482 AA;  54138 MW;  32361B8B69B70C82 CRC64;
     MSIPITVAYG DGIGPEIMEA VLLILSEAES GLVVETIEVG HNLYKKEWSS GIAPSSWDSI
     YRTKVLLKSP TMTPQGRGHK SLNVTLRKRL GLYANIRPCI SYHPVIKTRY PNLNVVIVRE
     NEEDTYTGIE HRLTNDTYQC SKVITRSGSE RICDYAFHYA KVHNRKRVTC LIKDNIMKMT
     DGIFHKSFSK IAENYPDIES DHYIVDIGMA KVASNPENFD VIVTTNLYGD IVSDIVAELS
     GSIGLAGSAN IGNNYAMFEA VHGSAPDIAG KNIANPSGLL NAAIQMLMYL KQFDKAQLIY
     NAFLKTLEDG IHTADIYQSQ VSKKKVSTMD FAKAVVENFG QSPSQLPKSM FQDNVDRTGV
     SYTYEPSYVT RVLVGVDITI GCDGVGLDFK QLINNLQNIT HDKLELVLIH NKGLEIWPDE
     SVSVNLSYMD QVCCRFYMKS KDDKIMNEHI NQLLFDIEQK KIDVVKMEKL YLYNDQPGFF
     TM
//