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Database: UniProt
Entry: S9ZIL0_9RHOO
LinkDB: S9ZIL0_9RHOO
Original site: S9ZIL0_9RHOO 
ID   S9ZIL0_9RHOO            Unreviewed;       745 AA.
AC   S9ZIL0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   ORFNames=M622_05450 {ECO:0000313|EMBL:EPZ14426.1};
OS   Thauera terpenica 58Eu.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=1348657 {ECO:0000313|EMBL:EPZ14426.1, ECO:0000313|Proteomes:UP000015455};
RN   [1] {ECO:0000313|EMBL:EPZ14426.1, ECO:0000313|Proteomes:UP000015455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=58Eu {ECO:0000313|EMBL:EPZ14426.1,
RC   ECO:0000313|Proteomes:UP000015455};
RA   Liu B., Frostegard A.H., Shapleigh J.P.;
RT   "Draft genome sequence of Thauera terpenica.";
RL   Submitted (JUN-2013) 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}.
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:EPZ14426.1}.
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DR   EMBL; ATJV01000081; EPZ14426.1; -; Genomic_DNA.
DR   RefSeq; WP_021250379.1; NZ_ATJV01000081.1.
DR   AlphaFoldDB; S9ZIL0; -.
DR   STRING; 1348657.M622_05450; -.
DR   PATRIC; fig|1348657.5.peg.2980; -.
DR   eggNOG; COG2838; Bacteria.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000015455; Unassembled WGS sequence.
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   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};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407,
KW   ECO:0000313|EMBL:EPZ14426.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015455};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT   BINDING         134..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
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         550
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         551
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         555
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
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   745 AA;  82657 MW;  28320ACAAE3598E0 CRC64;
     MAEGKSKIIY TLTDEAPLLA TCAFLPIVRS FTEPTGIEVE TADISVAGRV LAEFPEYLSE
     EQRVPDTLAE LGRLTLLPDT NIIKLPNISA SVAQLKVCIK ELQAKGYAIP DYPEDPKTDE
     EKALRQRYGK CLGSAVNPVL REGNSDRRAP LAVKNYAKKN PHSMGEWKQW SQTHVSHMHH
     GDFYHGEKSI TLDKARDVKM ELITASGKTI VLKPKVSLLD GEIIDSMFMS KKALCEFYER
     ELDDCREAGI LFSLHVKATM MKVSHPIVFG HCVRIYYKDA FAKHGKLFDE LGINVNNGMV
     DLYEKIKTLP ESKHDEIIRD LHACNEHRPE LAMVDSAKGI TNFHSPSDII VDASMPAMIR
     QGGKMWGSDG KQYDSKCVMP ESTFARIYQE MINFCKWHGN FDPRTMGTVP NVGLMAQKAE
     EYGSHDKTFE IAEAGVANIT DLATGEVLLA QNVEAGDIWR MCQVKDAPIR DWVKLAVTRA
     RNSGMPAVFW LDPYRPHENE LIKKVHTYLK DHDTKGLEIH IMSQVRAMRY TLERVGRGLD
     TISVTGNILR DYLTDLFPIL ELGTSAKMLS IVPLMNGGGM YETGAGGSAP KHVQQLVQEN
     HLRWDSLGEF LALAVSFEDL GIKTGNNKAK ILARTLDAAT GKLLDENKSP SPKTGQLDNR
     GSQFYLALFW AQALAAQTED AELAAHFVPL AKALSENETK IVDELNAVQG KPVDIGGYYK
     ADAAKTIAVM RPSATLNAIL KAARA
//
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