ID A0A1Q5Q5C6_9ACTO Unreviewed; 740 AA.
AC A0A1Q5Q5C6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BSZ39_01220 {ECO:0000313|EMBL:OKL55024.1};
OS Bowdeniella nasicola.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Bowdeniella.
OX NCBI_TaxID=208480 {ECO:0000313|EMBL:OKL55024.1, ECO:0000313|Proteomes:UP000185628};
RN [1] {ECO:0000313|Proteomes:UP000185628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19116 {ECO:0000313|Proteomes:UP000185628};
RA Meng X.;
RL Submitted (DEC-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}.
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:OKL55024.1}.
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DR EMBL; MQVR01000003; OKL55024.1; -; Genomic_DNA.
DR RefSeq; WP_073715575.1; NZ_MQVR01000003.1.
DR AlphaFoldDB; A0A1Q5Q5C6; -.
DR STRING; 208480.SAMN02910418_02142; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000185628; 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 Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
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:UP000185628};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT REGION 103..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 130..137
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 133
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 143
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 253
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 740 AA; 79940 MW; 8F3C3C51CE08812E CRC64;
MATIIYTHTD EAPMLATHSL LPIIEAFAKT AGVDVETRDI SLAGRILAAF SDKLPEDQKV
NDALAELGEL AKQPEANIIK LPNISASIPQ LKAAIKELQE QGFDLPNFPD NAETDEEKDA
KERYDSVKGS AVNPVLREGN SDRRAPIAVK NFARKYPHRM GAWTADSKTE VATMGADDFA
TNEKSVVMPS DDTLTIQLKQ ADGETVVLKD GLKVLEGEVI DGTFMSAKKL DAFLAEQVKR
AKDLGVLFSV HLKATMMKVS DPIIFGHVVK AYFADVFDKY GDQLAAAGLS PNDGLGAIFA
GLDSGKVENA DEIKAAFEAA LKDGPRLAMV NSHKGITNLH VPSDVIVDAS MPAMIRTSGH
MWGPDGEEDD TIAVIPDSSY AGVYQAVIED CKVNGAFDPT TMGSVPNVGL MAQKAEEYGS
HDKTFEIGAD GTVEVVNSAG EVLMSHDVEA GDIWRACQTK DAPIRDWVKL AVTRARLSET
PAIFWLDEDR AHDANLIDKV NAYLPEYDTG GISIAIMNPV EATKASIARI REGKDTISVT
GNVLRDYNTD LFPILELGTS AKMLSVVPLM NGGGLFEAGA GGSAPKHVQQ LVEENYLRWD
SLGEFLALAE SLRHLARFAD NPRAAVLADA LDKATEGVLN EGKSPARRLG QIDNRGSHMW
LATYWAKALA EQTEDAELAE KFADVAAKLA ENAEKIDAEL IEVQGDVVEI GGYYRPDEDK
TFAVMRPSKT LNEIIDSLVG
//
