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Database: UniProt
Entry: A0A1H1RDJ4_9ACTN
LinkDB: A0A1H1RDJ4_9ACTN
Original site: A0A1H1RDJ4_9ACTN 
ID   A0A1H1RDJ4_9ACTN        Unreviewed;       739 AA.
AC   A0A1H1RDJ4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=SAMN04488570_1660 {ECO:0000313|EMBL:SDS33824.1};
OS   Nocardioides scoriae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=642780 {ECO:0000313|EMBL:SDS33824.1, ECO:0000313|Proteomes:UP000198859};
RN   [1] {ECO:0000313|Proteomes:UP000198859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22127 {ECO:0000313|Proteomes:UP000198859};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; LT629757; SDS33824.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1RDJ4; -.
DR   STRING; 642780.SAMN04488570_1660; -.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000198859; Chromosome i.
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   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         349
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         546
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         547
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         551
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         583..584
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         588
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         599..601
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         648
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            254
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            419
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   739 AA;  79872 MW;  6CA5E7B3A0452046 CRC64;
     MTDSKIIYTQ TDEAPALATY SFLPIIEAYA AKAGVDVETR DISLAGRIIA VFADRLPEDQ
     RVDDALAELG ALAKTPEANI IKLPNISASV PQLKAAVAEL QEQGVALPDY PDNPQTDDER
     DARARYDKVK GSAVNPVLRE GNSDRRAPES VKSYARKNPH SMGAWTPSSK TDVATMDADD
     FRHNEQSVVI ADAGTLRVEL VTDAGTQVLK ESIPVEAGEV VDATFMSTSA LQDFLRAQIA
     RAKADDVLFS IHLKATMMKV SDPILFGHAV QAFFPSLFAD NAEALLEHGL DPKNGLGGIV
     SGAEKVGGDV AARVKASVEK DLADGPAIAM VDSDKGITNL HVPSDVIVDA SMPAMIRTSG
     HMWGPDGAEA DTLAVIPDSS YAGIYQVVID DCRAHGAYDP STMGSVPNVG LMARAAEEYG
     SHDKTFEIAE AGTVRLVDQD DQVLTEHHVQ AGDVWRACQT KDVPIQDWVK LAVTRARATG
     DPAIFWLDET RAHDRNLIAK VEQYLPEHDT DGLDLTIQSP VEAIQVSVDR IRRGENTISV
     TGNVLRDYLT DLFPILELGT SAKMLSVVPL INGGGLFETG AGGSAPKHVQ QLVKENYLRW
     DSLGEFLALS ESFSHLATTG DNLRARLLGE TLDRATGRLL EENRSPQRRL GTIDNRGSHF
     YVALFWAEEL SVQTEDEALA ADFAELAKRL RSEEETITGE LLAVQGSPAD IGGYFRPDPE
     KAARVMRPSE TFNASLASL
//
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