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Database: UniProt
Entry: A0A0M2GMU6_9ACTN
LinkDB: A0A0M2GMU6_9ACTN
Original site: A0A0M2GMU6_9ACTN 
ID   A0A0M2GMU6_9ACTN        Unreviewed;       739 AA.
AC   A0A0M2GMU6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=UK15_13045 {ECO:0000313|EMBL:KJK39387.1};
OS   Streptomyces variegatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=284040 {ECO:0000313|EMBL:KJK39387.1, ECO:0000313|Proteomes:UP000034786};
RN   [1] {ECO:0000313|Proteomes:UP000034786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16380 {ECO:0000313|Proteomes:UP000034786};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) 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:KJK39387.1}.
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DR   EMBL; JYJH01000007; KJK39387.1; -; Genomic_DNA.
DR   RefSeq; WP_031135313.1; NZ_JYJH01000007.1.
DR   AlphaFoldDB; A0A0M2GMU6; -.
DR   STRING; 284040.UK15_13045; -.
DR   PATRIC; fig|284040.3.peg.7301; -.
DR   Proteomes; UP000034786; 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, ECO:0000256|PIRSR:PIRSR009407-4};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407,
KW   ECO:0000313|EMBL:KJK39387.1};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT   BINDING         82..87
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         132..139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         135
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         348
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         545
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         546
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         550
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         582..583
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         587
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         598..600
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         647
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            255
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            418
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   739 AA;  79359 MW;  70E9C9E5B918BDA6 CRC64;
     MTDSTIIYTH TDEAPALATY SFLPVVRAYA SQAGVAVETR DISLAGRIIA LFPEYLTEDQ
     RIPDALAELG ELAKTPAANI IKLPNISASI PQLKAAVAEL QGQGYALPDY PDDPKTDEER
     EIRARYDKVK GSAVNPVLRE GNSDRRAPAS VKNYAKSHPH RMGAWTAESK TNVATMGQND
     FRSTEKSVVI AEDGALRIEL VGDDGTTTVL RESVPVLAGE VVDASVMRVA ALREFLTAQV
     AEAKAQGVLF SVHLKATMMK VSDPIVFGHV LRAFFPKTFA QYGDKLAAAG LTPNDGLGGI
     YKGLEALPEG AEIKASFDAE LAEGPALAMV DSDKGITNLH VPSDVIVDAS MPAMIRTSGH
     MWGPDGEEAD TLAVLPDSSY AGVYQAVIED CRANGAYDPS TMGSVPNVGL MAQKAEEYGS
     HDKTFEVPTT GTVRLVDQNG TALIEQAVAA GDIFRACQTK DAPIKDWVKL AVTRARATGD
     PAVFWLDETR AHDANLIAKV HTYLAEHDTE GLDIRILNPV EATKLSVERI RRGENTISVT
     GNVLRDYLTD LFPILELGTS AKMLSVVPLM AGGGLFETGA GGSAPKHVQQ LVKENYLRWD
     SLGEFFALVP SFEQFAKVTG NARAQVLADT LDRATATFLN EDKSPTRRVG GIDNRGSHFY
     LSLYWAQELA GQTDDADLAK AFAPLAETLA ANEQKIVEEL IAAQGKPVEI GGYYQPDPEK
     AAAAMRPSAT WNETLASLS
//
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