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Database: UniProt
Entry: W2V1D0_9RICK
LinkDB: W2V1D0_9RICK
Original site: W2V1D0_9RICK 
ID   W2V1D0_9RICK            Unreviewed;       495 AA.
AC   W2V1D0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
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   Name=icd {ECO:0000313|EMBL:ETO91472.1};
GN   ORFNames=P857_387 {ECO:0000313|EMBL:ETO91472.1};
OS   Candidatus Xenolissoclinum pacificiensis L6.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Xenolissoclinum.
OX   NCBI_TaxID=1401685 {ECO:0000313|EMBL:ETO91472.1, ECO:0000313|Proteomes:UP000018951};
RN   [1] {ECO:0000313|EMBL:ETO91472.1, ECO:0000313|Proteomes:UP000018951}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L6 {ECO:0000313|Proteomes:UP000018951};
RX   PubMed=24324632;
RA   Kwan J.C., Schmidt E.W.;
RT   "Bacterial endosymbiosis in a chordate host: long-term co-evolution and
RT   conservation of secondary metabolism.";
RL   PLoS ONE 8:E80822-E80822(2013).
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   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETO91472.1}.
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DR   EMBL; AXCJ01000005; ETO91472.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2V1D0; -.
DR   STRING; 1401685.P857_387; -.
DR   PATRIC; fig|1401685.3.peg.677; -.
DR   Proteomes; UP000018951; Unassembled WGS sequence.
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   Gene3D; 3.30.70.1570; -; 1.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR040978; Isocitrate_DH_TT1725_C.
DR   InterPro; IPR046997; Isocitrate_DH_TT1725_C_sf.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR   PANTHER; PTHR11835:SF43; ISOCITRATE DEHYDROGENASE [NADP]; 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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018951}.
FT   DOMAIN          6..332
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   495 AA;  55714 MW;  59956CC55FE0DA94 CRC64;
     MNTPKSIAVC YGDGIGPEIM ESTLSICKSA GFKHTIEVIT LGKNLYDKGY KTGMSEEAVS
     VLKRVPVLLK APLTTVQGEG MRSVNVTLRK MMGLFVNVRP SNNLIFNHSK NINVVVIREN
     SEDIYSGIEY RNSYDTRTSI KIITEQASYR ICDYAFRFAQ QNGRKKVSCF VKDNIMKMTD
     GIFHKMFLEV ANHYPDIEKE VLILDIAMAN LAKYPERFDV IVTTNLYGDV VSDVCAELSG
     SIGIAGSVNL GTKYAMFEAV HGSAPKIANK NIANPMGMVN AAIMMLNYLN ENHISEKILR
     AWMQCVKNKW LTRDLVDNPK VALNTQDFTD TMIKCIRDDN KTSVNIDAHS INIPDTMQTD
     TSDYYSRVSE YIKHRTLVGV DIYVDFTGNL NKILEIINTF DKINGKNVSI DLVPINESIF
     LNSILSKGME LWPTVLLTND YTTDYITCRF IASKNINFNN HDITALMNAF EENSVNIVKI
     ETLYISPKRD MGFAN
//
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