ID A0A0G3H1J9_9CORY Unreviewed; 737 AA.
AC A0A0G3H1J9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
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 Name=icd {ECO:0000313|EMBL:AKK04992.1};
GN ORFNames=CMUST_03240 {ECO:0000313|EMBL:AKK04992.1};
OS Corynebacterium mustelae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=571915 {ECO:0000313|EMBL:AKK04992.1, ECO:0000313|Proteomes:UP000035199};
RN [1] {ECO:0000313|EMBL:AKK04992.1, ECO:0000313|Proteomes:UP000035199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45274 {ECO:0000313|EMBL:AKK04992.1,
RC ECO:0000313|Proteomes:UP000035199};
RX PubMed=26358597;
RA Ruckert C., Eimer J., Winkler A., Tauch A.;
RT "Complete Genome Sequence of the Type Strain Corynebacterium mustelae DSM
RT 45274, Isolated from Various Tissues of a Male Ferret with Lethal Sepsis.";
RL Genome Announc. 3:e01012-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45274 {ECO:0000313|Proteomes:UP000035199};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium mustelae DSM 45274, isolated
RT from various tissues of a male ferret with lethal sepsis.";
RL Submitted (MAY-2015) 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; CP011542; AKK04992.1; -; Genomic_DNA.
DR RefSeq; WP_047261297.1; NZ_CP011542.1.
DR AlphaFoldDB; A0A0G3H1J9; -.
DR STRING; 571915.CMUST_03240; -.
DR KEGG; cmv:CMUST_03240; -.
DR PATRIC; fig|571915.4.peg.686; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000035199; 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 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:AKK04992.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035199};
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 737 AA; 79309 MW; 281ADE86F7BBB337 CRC64;
MAKIIWTRTD EAPFLASLSL KPIVEAFAST AGIEVETRDI SLAGRILAQF PESLSDDQKV
EDALSALGEL AKTPEANIIK LPNISASVPQ LKAAIAELQG FGYKIPDYPD NPETDEEKDV
RARYDAVKGS AVNPVLREGN SDRRAPSAVK NFAKKNPHRM GAWSADSKTN VATMDANDFR
HNEKSVIMPS DDVLTIKHVA ADGTETVLKS DLKVLAGEVI DGTFMSAKAL DAFLAAQVAR
AKEDGVLFST HLKATMMKVS DPIIFGHVVR AYFTDVFAQY GDVLEANGLT GENGLAAIYS
GLESVENGAE IKAAFEKVLA EGPALAMVNS DKGITNLHVP SDVIVDASMP AMIRTSGHMW
NAAGEEQDTL AVIPDSSYAG VYQTVIDDCR ANGAFDPATM GTVPNVGLMA QKAEEYGSHD
KTFRVAADGK VQVVNSAGDV LIEHDVEAGD IWRACQTKDA PIQDWVKLAV TRSRLSGMPA
IFWLDPERAH DRNLISLVEK YLADHDTDGL DITIKSPVEA TKVSIERIRR GEDTISVTGN
VLRDYNTDLF PILELGTSAK MLSIVPLMAG GGLFETGAGG SAPKHVQQVQ EENHLRWDSL
GEFLALAESL RHITNTGGTK KAAVLADALD AATERLLDEN KSPSRKVGEI DNRGSHFFLA
TEWAKALAAQ TEDAELAETF KPVAEALVAG SDEINAELLA VQGSPADLGG YYQPDEKAEK
VMRPSAKFNE IIDGLKK
//
