IDH_COREF
ID IDH_COREF Reviewed; 729 AA.
AC Q8RQL9;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Isocitrate dehydrogenase [NADP];
DE Short=IDH;
DE EC=1.1.1.42;
DE AltName: Full=Oxalosuccinate decarboxylase;
GN Name=icd; OrderedLocusNames=CE0682;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RA Nonaka G., Kimura E., Kawahara Y., Sugimoto S.;
RT "Corynebacterium efficiens icd gene for isocitrate dehydrogenase, complete
RT cds.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Weakly inhibited by oxaloacetate, 2-oxoglutarate,
CC and citrate. Severely inhibited by oxaloacetate plus glyoxylate (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the monomeric-type IDH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC17492.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB083179; BAB88832.1; -; Genomic_DNA.
DR EMBL; BA000035; BAC17492.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_006769639.1; NZ_GG700687.1.
DR AlphaFoldDB; Q8RQL9; -.
DR SMR; Q8RQL9; -.
DR STRING; 196164.23492519; -.
DR PRIDE; Q8RQL9; -.
DR EnsemblBacteria; BAC17492; BAC17492; BAC17492.
DR KEGG; cef:CE0682; -.
DR eggNOG; COG2838; Bacteria.
DR HOGENOM; CLU_025308_1_0_11; -.
DR OrthoDB; 222705at2; -.
DR Proteomes; UP000001409; Chromosome.
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 PANTHER; PTHR36999; PTHR36999; 1.
DR Pfam; PF03971; IDH; 1.
DR PIRSF; PIRSF009407; IDH_monmr; 1.
DR TIGRFAMs; TIGR00178; monomer_idh; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..729
FT /note="Isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000083594"
FT BINDING 80..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 121..128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 534
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 535
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 571..572
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 576
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 587..589
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 636
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 244
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 407
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 729 AA; 79285 MW; 84BCDECA8687627B CRC64;
MAKIIWTRTD EAPLLATYSL KPVVEAFAAT AGIEVETRDI SLAGRILAQF ADQLPEEQKV
SDALAELGEL AKTPEANIIK LPNISASVPQ LKAAVKELQE QGYDLPEYED AKDRYAAVIG
SNVNPVLREG NSDRRAPVAV KNFVKKFPHR MGEWSADSKT NVATMGADDF RSNEKSVIMD
EADTVVIKHV AADGTETVLK DSLPLLKGEV IDGTFISAKA LDAFLLDQVK RAKEEGILFS
AHMKATMMKV SDPIIFGHIV RAYFADVYAQ YGEQLLAAGL NGENGLAAIY AGLDKLDNGA
EIKAAFDKGL EEGPDLAMVN SAKGITNLHV PSDVIIDASM PAMIRTSGKM WNKDDQTQDA
LAVIPDSSYA GVYQTVIEDC RKNGAFDPTT MGTVPNVGLM AQKAEEYGSH DKTFRIEADG
KVQVVASNGD VLIEHDVEKG DIWRACQTKD APIQDWVKLA VNRARLSGMP AVFWLDPARA
HDRNLTTLVE KYLADHDTEG LDIQILSPVE ATQHAIDRIR RGEDTISVTG NVLRDYNTDL
FPILELGTSA KMLSVVPLMA GGGLFETGAG GSAPKHVQQV IEENHLRWDS LGEFLALAES
FRHELNTRNN TKAGVLADAL DRATEKLLNE EKSPSRKVGE IDNRGSHFWL ATYWADELAN
QTEDAELAET FAPVAEALNN QAADIDAALI GEQGKPVDLG GYYAPSDEKT SAIMRPVAAF
NEIIDSLKK
