ID   I4B3K5_TURPD            Unreviewed;       742 AA.
AC   I4B3K5;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR009407};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR009407};
DE   AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|PIRNR:PIRNR009407};
GN   OrderedLocusNames=Turpa_1214 {ECO:0000313|EMBL:AFM11862.1};
OS   Turneriella parva (strain ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H)
OS   (Leptospira parva).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Turneriella.
OX   NCBI_TaxID=869212 {ECO:0000313|EMBL:AFM11862.1, ECO:0000313|Proteomes:UP000006048};
RN   [1] {ECO:0000313|EMBL:AFM11862.1, ECO:0000313|Proteomes:UP000006048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H
RC   {ECO:0000313|Proteomes:UP000006048};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of genome of Turneriella parva DSM 21527.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR009407};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC       {ECO:0000256|PIRSR:PIRSR009407-3};
CC   -!- SIMILARITY: Belongs to the monomeric-type IDH family.
CC       {ECO:0000256|PIRNR:PIRNR009407}.
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DR   EMBL; CP002959; AFM11862.1; -; Genomic_DNA.
DR   RefSeq; WP_014802378.1; NC_018020.1.
DR   AlphaFoldDB; I4B3K5; -.
DR   STRING; 869212.Turpa_1214; -.
DR   KEGG; tpx:Turpa_1214; -.
DR   PATRIC; fig|869212.3.peg.1201; -.
DR   HOGENOM; CLU_025308_1_0_12; -.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000006048; Chromosome.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR004436; Isocitrate_DH_NADP_mono.
DR   NCBIfam; TIGR00178; monomer_idh; 1.
DR   PANTHER; PTHR36999; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR   PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR   Pfam; PF03971; IDH; 1.
DR   PIRSF; PIRSF009407; IDH_monmr; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Glyoxylate bypass {ECO:0000256|PIRNR:PIRNR009407};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR009407-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3};
KW   NADP {ECO:0000256|PIRNR:PIRNR009407, ECO:0000256|PIRSR:PIRSR009407-4};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006048};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT   BINDING         84..89
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         134..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         137
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         352
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         549
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         550
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         554
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         586..587
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         591
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         602..604
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         651
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            257
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            422
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   742 AA;  81285 MW;  1220201EC922CCAB CRC64;
     MADSKSKIIW TKIDEAPALA TYSLLPIVNA FTKAAGVVVE TCDISLAGRI LANFPENLSE
     SQKVADGLAA LGKLVLLPEA NVIKLPNISA SIPQLKAAIK ELQSQGYKVP DYPEEPKTED
     EKAIKARYAK VLGSAVNPVL REGNSDRRVA RSVKEFAKKN PHKLGEWSKE CKSHVANMKA
     GDFFHNEKSV TIEDATDVKF EFEDKSGNKT VLKEKLSLKK GEVFDATFMS AKALRQFIED
     QLADAKAKNL LFSVHLKATM MKVSDPIIFG HFVSVYFKDV FAKHAATFQK LGVNPDLGLG
     DLYAKIKTLP DAERAEIEAD IQATYSVRPP LAMVDSAKGI TNLHAGNDVI IDASMPVVIR
     DSGKMWGPDG KLHECKAVIP DTSYAEFYQT GFDFCRQQGA FDPRVMGNVA NVGLMAQQAE
     EYGSHDKTFK APGDGVIRVI DAAGKVLTEH HVETGDIWRA CQTKDEAIRD WVKLAVRRAR
     ATGSPAVFWL TSARAHDAQI IAKVNTYLKE HDTSGLEIHI LSLVDAMQFT LERVKAGKDT
     ISVTGNVMRD YLTDLFPILE LNTSAKMLSI VPLLNGGGLF ETGAGGSAPK HVQQFQQEGY
     LRWDSTGEFL ALGVSLEHLA ATFKNAKAQV LADTIDKAFG KFLDNNKSPA RKVGEIDNRG
     SHFYFGLYWA QALAEQTADK ELQARFAPIA KQLTENEAKI DKELIDAQGK PVDMGGYFHP
     DDAKTAKAMR PSATLNSIID AI
//