ID   G8SIJ9_ACTS5            Unreviewed;       404 AA.
AC   G8SIJ9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   Name=icdA {ECO:0000313|EMBL:AEV81797.1};
GN   OrderedLocusNames=ACPL_900 {ECO:0000313|EMBL:AEV81797.1};
OS   Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV81797.1, ECO:0000313|Proteomes:UP000005440};
RN   [1] {ECO:0000313|Proteomes:UP000005440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC   {ECO:0000313|Proteomes:UP000005440};
RA   Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA   Wehmeier U.F., Stoye J., Puehler A.;
RT   "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT   SE50/110.";
RL   Submitted (DEC-2011) 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:PIRNR000108};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000108,
CC         ECO:0000256|PIRSR:PIRSR000108-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000108,
CC         ECO:0000256|PIRSR:PIRSR000108-3};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC       {ECO:0000256|PIRNR:PIRNR000108, ECO:0000256|PIRSR:PIRSR000108-3};
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       ECO:0000256|PIRNR:PIRNR000108}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003170; AEV81797.1; -; Genomic_DNA.
DR   RefSeq; WP_014687870.1; NZ_LT827010.1.
DR   AlphaFoldDB; G8SIJ9; -.
DR   STRING; 134676.ACPL_900; -.
DR   KEGG; ase:ACPL_900; -.
DR   PATRIC; fig|134676.3.peg.789; -.
DR   eggNOG; COG0538; Bacteria.
DR   HOGENOM; CLU_023296_1_1_11; -.
DR   OrthoDB; 9765655at2; -.
DR   Proteomes; UP000005440; Chromosome.
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   GO; GO:0006102; P:isocitrate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004790; Isocitrate_DH_NADP.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   NCBIfam; TIGR00127; nadp_idh_euk; 1.
DR   PANTHER; PTHR11822:SF21; ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11822; NADP-SPECIFIC ISOCITRATE DEHYDROGENASE; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PIRSF; PIRSF000108; IDH_NADP; 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, ECO:0000256|PIRNR:PIRNR000108};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR000108};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000108};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000108};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000108};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005440};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN          9..395
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   BINDING         75..77
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   BINDING         77
FT                   /ligand="D-threo-isocitrate"
FT                   /ligand_id="ChEBI:CHEBI:15562"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT   BINDING         82
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   BINDING         94..100
FT                   /ligand="D-threo-isocitrate"
FT                   /ligand_id="ChEBI:CHEBI:15562"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT   BINDING         109
FT                   /ligand="D-threo-isocitrate"
FT                   /ligand_id="ChEBI:CHEBI:15562"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT   BINDING         132
FT                   /ligand="D-threo-isocitrate"
FT                   /ligand_id="ChEBI:CHEBI:15562"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT   BINDING         251
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT   BINDING         259
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   BINDING         274
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT   BINDING         309..314
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   BINDING         327
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   SITE            139
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
FT   SITE            211
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
SQ   SEQUENCE   404 AA;  45116 MW;  59E08A6AD06C89AE CRC64;
     MAKIKVKNPV VEIDGDEMTR IIWKQIREQL IQPYLDVNLE YYDLGIQYRD ETDDQVTIDA
     ANAIKRHGVG VKCATITPDE ARVQEFGLKK MWRSPNGTIR NILGGVVFRE PIIMKNVPRL
     VPGWTKPIVI GRHAHGDQYK ASDFVAPSKG KMTVTFTPED GSAPIEMHVA DFPAGGVGMA
     MYNFDESIRD FARASLRYGL ARNYPVYLST KNTILKAYDG RFKDLFAEIF ETEFADQFKE
     AGITYEHRLI DDMVAAALKW EGGYVWACKN YDGDVQSDTV AQGFGSLGLM TSVLMTPDGQ
     TVEAEAAHGT VTRHYRQWQK GEKTSTNPIA SIFAWTGGLK HRGKLDGTPE VTQFAEALEQ
     VCIETVEGGQ MTKDLALLIS KDAPWLSTDE FMNALDENLA RKLA
//