IDH_CORGL
ID IDH_CORGL Reviewed; 738 AA.
AC P50216;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Isocitrate dehydrogenase [NADP];
DE Short=IDH;
DE EC=1.1.1.42;
DE AltName: Full=Oxalosuccinate decarboxylase;
GN Name=icd; OrderedLocusNames=Cgl0664, cg0766;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=7836312; DOI=10.1128/jb.177.3.774-782.1995;
RA Eikmanns B.J., Rittmann D., Sahm H.;
RT "Cloning, sequence analysis, expression, and inactivation of the
RT Corynebacterium glutamicum icd gene encoding isocitrate dehydrogenase and
RT biochemical characterization of the enzyme.";
RL J. Bacteriol. 177:774-782(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND
RP SUBUNIT.
RX PubMed=16416443; DOI=10.1002/prot.20867;
RA Imabayashi F., Aich S., Prasad L., Delbaere L.T.;
RT "Substrate-free structure of a monomeric NADP isocitrate dehydrogenase: an
RT open conformation phylogenetic relationship of isocitrate dehydrogenase.";
RL Proteins 63:100-112(2006).
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;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.;
CC -!- ACTIVITY REGULATION: Weakly inhibited by oxaloacetate, 2-oxoglutarate,
CC and citrate. Severely inhibited by oxaloacetate plus glyoxylate.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16416443}.
CC -!- SIMILARITY: Belongs to the monomeric-type IDH family. {ECO:0000305}.
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DR EMBL; X71489; CAA50590.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98057.1; -; Genomic_DNA.
DR EMBL; BX927149; CAF19369.1; -; Genomic_DNA.
DR PIR; I40719; I40719.
DR RefSeq; NP_599896.1; NC_003450.3.
DR RefSeq; WP_011013800.1; NC_006958.1.
DR PDB; 2B0T; X-ray; 1.75 A; A=1-738.
DR PDB; 3MBC; X-ray; 1.90 A; A/B=1-738.
DR PDBsum; 2B0T; -.
DR PDBsum; 3MBC; -.
DR AlphaFoldDB; P50216; -.
DR SMR; P50216; -.
DR STRING; 196627.cg0766; -.
DR PRIDE; P50216; -.
DR KEGG; cgb:cg0766; -.
DR KEGG; cgl:Cgl0664; -.
DR PATRIC; fig|196627.13.peg.650; -.
DR eggNOG; COG2838; Bacteria.
DR HOGENOM; CLU_025308_1_0_11; -.
DR OMA; FRMCQTK; -.
DR BRENDA; 1.1.1.42; 960.
DR EvolutionaryTrace; P50216; -.
DR Proteomes; UP000000582; 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 1: Evidence at protein level;
KW 3D-structure; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..738
FT /note="Isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000083595"
FT BINDING 80..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 130..137
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:16416443"
FT BINDING 543
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 544
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:16416443"
FT BINDING 548
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:16416443"
FT BINDING 580..581
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 585
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 596..598
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 645
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 253
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 416
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 11..29
FT /evidence="ECO:0007829|PDB:2B0T"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:2B0T"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 205..214
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 227..244
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:2B0T"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 260..272
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 274..286
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 308..321
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:2B0T"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 366..372
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 376..392
FT /evidence="ECO:0007829|PDB:2B0T"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:2B0T"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 427..434
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 440..446
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 459..476
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 489..502
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 512..515
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 517..529
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 535..538
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 540..555
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 562..567
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 572..575
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 583..592
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 600..617
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 620..638
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 652..669
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 674..700
FT /evidence="ECO:0007829|PDB:2B0T"
FT STRAND 711..713
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 716..723
FT /evidence="ECO:0007829|PDB:2B0T"
FT HELIX 727..735
FT /evidence="ECO:0007829|PDB:2B0T"
SQ SEQUENCE 738 AA; 80081 MW; EAC4C5FA38C33F63 CRC64;
MAKIIWTRTD EAPLLATYSL KPVVEAFAAT AGIEVETRDI SLAGRILAQF PERLTEDQKV
GNALAELGEL AKTPEANIIK LPNISASVPQ LKAAIKELQD QGYDIPELPD NATTDEEKDI
LARYNAVKGS AVNPVLREGN SDRRAPIAVK NFVKKFPHRM GEWSADSKTN VATMDANDFR
HNEKSIILDA ADEVQIKHIA ADGTETILKD SLKLLEGEVL DGTVLSAKAL DAFLLEQVAR
AKAEGILFSA HLKATMMKVS DPIIFGHVVR AYFADVFAQY GEQLLAAGLN GENGLAAILS
GLESLDNGEE IKAAFEKGLE DGPDLAMVNS ARGITNLHVP SDVIVDASMP AMIRTSGHMW
NKDDQEQDTL AIIPDSSYAG VYQTVIEDCR KNGAFDPTTM GTVPNVGLMA QKAEEYGSHD
KTFRIEADGV VQVVSSNGDV LIEHDVEAND IWRACQVKDA PIQDWVKLAV TRSRLSGMPA
VFWLDPERAH DRNLASLVEK YLADHDTEGL DIQILSPVEA TQLSIDRIRR GEDTISVTGN
VLRDYNTDLF PILELGTSAK MLSVVPLMAG GGLFETGAGG SAPKHVQQVQ EENHLRWDSL
GEFLALAESF RHELNNNGNT KAGVLADALD KATEKLLNEE KSPSRKVGEI DNRGSHFWLT
KFWADELAAQ TEDADLAATF APVAEALNTG AADIDAALLA VQGGATDLGG YYSPNEEKLT
NIMRPVAQFN EIVDALKK
