ID W5XYE7_9CORY Unreviewed; 738 AA.
AC W5XYE7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=B843_02805 {ECO:0000313|EMBL:AHI21952.1};
OS Corynebacterium vitaeruminis DSM 20294.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224164 {ECO:0000313|EMBL:AHI21952.1, ECO:0000313|Proteomes:UP000019222};
RN [1] {ECO:0000313|EMBL:AHI21952.1, ECO:0000313|Proteomes:UP000019222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10234 {ECO:0000313|Proteomes:UP000019222};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "The complete genome sequence of Corynebacterium vitaeruminis DSM 20294.";
RL Submitted (FEB-2013) 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; CP004353; AHI21952.1; -; Genomic_DNA.
DR RefSeq; WP_025252008.1; NZ_CP004353.1.
DR AlphaFoldDB; W5XYE7; -.
DR STRING; 1224164.B843_02805; -.
DR KEGG; cvt:B843_02805; -.
DR PATRIC; fig|1224164.3.peg.555; -.
DR eggNOG; COG2838; Bacteria.
DR HOGENOM; CLU_025308_1_0_11; -.
DR Proteomes; UP000019222; 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 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 ECO:0000313|EMBL:AHI21952.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019222};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
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 346
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 543
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 544
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 548
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 580..581
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 585
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 596..598
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 645
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 416
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ SEQUENCE 738 AA; 79341 MW; 235D44A45BE9530C CRC64;
MAKIIWTRTD EAPLLATYSL KPVVEAFAST AGIEVETRDI SLAGRILSQF PDYLSDEQKV
DDALAELGQL AKTPEANIIK LPNISASVPQ LKAAIAELQA QGFALPEYPD APSTDEEKDV
RARYDSVKGS AVNPVLREGN SDRRAPIAVK NFAKKNPHRM GAWSADSKTN VATMTAGDFR
HNEKSVIMPA ADTLTFKLVK ADGSEEILKD GLKVLEGEVI DGTYMSAKAL DAFLAEQVKR
AADEGVLFSA HLKATMMKVS DPIMFGHVVR AFFDETFAKY GEELLAAGLN GENGLGAILA
GLGSLANGEE IKASFEKELA DGPAVAMVNS DKGITNLHVP SDVIVDASMP AMIRTSGHMW
NAAGEEQDTL AVLPDSSYAG IYQVVIDDCK ANGAFDPATM GTVPNVGLMA QKAEEYGSHD
KTFKIPADGT VQVVNSAGEV LIEHNVEAGD IWRACQTKDA PIQDWVKLAV NRARLSGMKA
IFWLDPERGH DRNIKSLVEK YLADHDTTGL DIEIMSPVEA TKVSIERIRR GEDTISVTGN
VLRDYNTDLF PILELGTSAK MLSIVPLMAG GGLFETGAGG SAPKHVQQVQ AENHLRWDSL
GEFLALAESL RHIANTEDAP SAAVLADALD AATERLLDEN LSPSRKVGEI DNRGSHFFLT
KFWAEELAKQ TTDAALAEVF APVAAALEEK SDEIAAGLIS NQGAPADLGG YYAPNEEKVT
AIMRPVAAFN EIIDELKK
//
