ID A0QSZ3_MYCS2 Unreviewed; 743 AA. AC A0QSZ3; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 126. 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 OrderedLocusNames=MSMEG_1654 {ECO:0000313|EMBL:ABK69615.1}; OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium OS smegmatis). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycolicibacterium. OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK69615.1, ECO:0000313|Proteomes:UP000000757}; RN [1] {ECO:0000313|EMBL:ABK69615.1, ECO:0000313|Proteomes:UP000000757} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757}; RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., RA Fraser C.M.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:4ZDA} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH MANGANESE. RA Pojer F., Murima P., McKinney J.D.; RT "crystal structure of isocitrate dehydrogenase in complex with isocitrate RT and Mn from M. smegmatis."; RL Submitted (APR-2015) to the PDB data bank. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000480; ABK69615.1; -; Genomic_DNA. DR RefSeq; WP_011727802.1; NZ_SIJM01000023.1. DR RefSeq; YP_886031.1; NC_008596.1. DR PDB; 4ZDA; X-ray; 2.80 A; A/B/C/D/E/F=1-743. DR PDBsum; 4ZDA; -. DR AlphaFoldDB; A0QSZ3; -. DR SMR; A0QSZ3; -. DR STRING; 246196.MSMEG_1654; -. DR PaxDb; 246196-MSMEI_1615; -. DR GeneID; 66733104; -. DR KEGG; msm:MSMEG_1654; -. DR PATRIC; fig|246196.19.peg.1639; -. DR eggNOG; COG2838; Bacteria. DR OrthoDB; 9807643at2; -. DR Proteomes; UP000000757; 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 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4ZDA}; KW Glyoxylate bypass {ECO:0000256|PIRNR:PIRNR009407}; KW Magnesium {ECO:0000256|PIRSR:PIRSR009407-3}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3, ECO:0007829|PDB:4ZDA}; KW NADP {ECO:0000256|PIRNR:PIRNR009407, ECO:0000256|PIRSR:PIRSR009407-4}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407, KW ECO:0000313|EMBL:ABK69615.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000757}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}. FT BINDING 84..89 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 134..141 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 134 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0007829|PDB:4ZDA" FT BINDING 137 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0007829|PDB:4ZDA" FT BINDING 137 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 141 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0007829|PDB:4ZDA" FT BINDING 147 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0007829|PDB:4ZDA" FT BINDING 147 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 257 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0007829|PDB:4ZDA" FT BINDING 352 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3, FT ECO:0007829|PDB:4ZDA" FT BINDING 422 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0007829|PDB:4ZDA" FT BINDING 550 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0007829|PDB:4ZDA" FT BINDING 550 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2" FT BINDING 551 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0007829|PDB:4ZDA" FT BINDING 551 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3, FT ECO:0007829|PDB:4ZDA" FT BINDING 555 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3, FT ECO:0007829|PDB:4ZDA" FT BINDING 587..588 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 592 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 603..605 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT BINDING 652 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4" FT SITE 257 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" FT SITE 422 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1" SQ SEQUENCE 743 AA; 82604 MW; C30D68DBA13A1198 CRC64; MSAQQPTIIY TLTDEAPLLA TYAFLPVVRK FAEAAGIDVK TSDISVAARI LAEFGDHLTE EQRVPDNLGE LGALTQDPSA NIIKLPNISA SVPQLLAAIK ELQGKGYNVP DYPANPKTDD EKKIKDRYAK ILGSAVNPVL REGNSDRRAP KAVKEYARKH PHSMGEWSQA SRTHVATMKT GDFYHGEKSM TLDRDRRVKM VLKTKSGEEI VLKPEVKLDA GDIIDSMYMS KKALIAFYEE QIEDAYKTGV MFSLHVKATM MKVSHPIVFG HAVKVFYKDA FAKHEKLFDE LGVNVNNGLS DLYDKIEALP ASQREEIIED LHKCHEHRPE LAMVDSAKGI SNFHSPSDVI VDASMPAMIR LGGKMYGADG RTKDTKAVNP ESTFSRMYQE MINFCKTHGQ FDPTTMGTVP NVGLMAQKAE EYGSHDKTFE IPEDGVADIV DIDTGEVLLT QNVEEGDIWR MPIVKDAPIR DWVKLAVTRA RLSGMPVVFW LDTERPHEVE LRKKVKEYLK DHDTEGLKIQ IMPQVWAMRY TLERVVRGKD TIAATGNILR DYLTDLFPIL ELGTSAKMLS IVPLMAGGGL YETGAGGSAP KHVHQLVEEN HLRWDSLGEF LALGASLEDM GNKTGNEKAK VLAKALDTAT GKLLEENKSP SRRTGELDNR GSQFYLSLFW AQALAEQTED AELAERFKPL AKALAEQEEA IVSELNSVQG KTVDIGGYYY PDPEKTSEVM RPSKTFNTTL ESV //