ID V9X8M6_9NOCA Unreviewed; 752 AA.
AC V9X8M6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=Y013_03200 {ECO:0000313|EMBL:AHD19771.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD19771.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD19771.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD19771.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
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; CP006996; AHD19771.1; -; Genomic_DNA.
DR RefSeq; WP_024100900.1; NC_023150.1.
DR AlphaFoldDB; V9X8M6; -.
DR GeneID; 29936833; -.
DR KEGG; rpy:Y013_03200; -.
DR PATRIC; fig|1435356.3.peg.637; -.
DR eggNOG; COG2838; Bacteria.
DR HOGENOM; CLU_025308_1_0_11; -.
DR Proteomes; UP000018781; 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:AHD19771.1};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 85..90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 135..142
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 138
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 551
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 552
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 556
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 588..589
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 593
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 604..606
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 653
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT SITE 258
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT SITE 423
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ SEQUENCE 752 AA; 83545 MW; 8F3485C0FF9F53B5 CRC64;
MSADKQSTII YTLTDEAPLL ATYAFLPIVR TFAGAAGIEV ETSDISVPAR ILAEFPEHLT
EEQRVPDNLA ELGRLTQLPE TNIIKLPNIS ASVPQLLAAI KELQSKGYQV PDFPDAPKTD
EERAIRERYG KILGSAVNPV LREGNSDRRA PRAVKEYARK HPHSMGEWSM ASRSHVAHMR
HGDFYHGEKS MTLDRARKVR MELVTKDGET IVLKPEVELG EGDIMDSMFM SKKALLEFYE
EQMEDARKTG VMFSLHVKAT MMKVSHPIVF GHAVKTFYKD AFAKHQKLFD ELGVNVNNGL
GDLYDKIETL PSTQRDEIKQ DLHNCHEHRP ELAMVDSARG ISNFHSPSDV IVDASMPAMI
RSGGKMYGAD GRPKDVKAVM PESTFARIYQ EIINFCKTNG AFDPTTMGTV PNVGLMAQKA
EEYGSHDKTF EVPEAGEANF VDAETGEVLL TQHVEAGDIW RMCTVKDAPI RDWVKLAVTR
ARNSGMPVLF WLDPYRPHEN ELIKKVELYL QDHDTDGLDI HIMSQVRSMR YTLERLNRGM
DTIAATGNIL RDYLTDLFPI LELGTSAKML SIVPLMAGGG LYETGAGGSA PKHVKQLVEE
NHLRWDSLGE FLALAVSLED LGIKTGNERA KIVANALDAA TGKLLETNKS PSRKVGELDN
RGSQFYLAMY WAQELAAQTE DPELAEQFAP LAEALARDED TIVRELNEVQ GAPVDIGGYY
RPDRDKTVAV MRPSRTLITA LTAVDPEAGN AP
//
