ID K0JL59_BRAPL Unreviewed; 419 AA.
AC K0JL59;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446};
DE EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446};
GN ORFNames=WESB_1659 {ECO:0000313|EMBL:CCG57125.1};
OS Brachyspira pilosicoli WesB.
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=1161918 {ECO:0000313|EMBL:CCG57125.1, ECO:0000313|Proteomes:UP000003759};
RN [1] {ECO:0000313|EMBL:CCG57125.1, ECO:0000313|Proteomes:UP000003759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WesB {ECO:0000313|EMBL:CCG57125.1};
RX PubMed=22947175; DOI=10.1186/1471-2164-13-454;
RA Mappley L.J., Black M.L., Abuoun M., Darby A.C., Woodward M.J.,
RA Parkhill J., Turner A.K., Bellgard M.I., La T., Phillips N.D.,
RA La Ragione R.M., Hampson D.J.;
RT "Comparative genomics of Brachyspira pilosicoli strains: genome
RT rearrangements, reductions and correlation of genetic compliment with
RT phenotypic diversity.";
RL BMC Genomics 13:454-454(2012).
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|ARBA:ARBA00023554};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000256|PIRSR:PIRSR604439-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR EMBL; HE793032; CCG57125.1; -; Genomic_DNA.
DR RefSeq; WP_014933368.1; NC_018604.1.
DR AlphaFoldDB; K0JL59; -.
DR KEGG; bpw:WESB_1659; -.
DR PATRIC; fig|1161918.5.peg.1170; -.
DR HOGENOM; CLU_031953_7_1_12; -.
DR OrthoDB; 9806254at2; -.
DR Proteomes; UP000003759; Chromosome.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR NCBIfam; TIGR00183; prok_nadp_idh; 1.
DR PANTHER; PTHR43504; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR PANTHER; PTHR43504:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435,
KW ECO:0000256|RuleBase:RU004446};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604439-3};
KW Manganese {ECO:0000256|PIRSR:PIRSR604439-3, ECO:0000256|RuleBase:RU004446};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004446};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR604439-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU004446}.
FT DOMAIN 18..415
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 92
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT BINDING 355
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT SITE 148
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT SITE 218
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT MOD_RES 88
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 130
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 230
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
SQ SEQUENCE 419 AA; 46230 MW; 5C795E2F4A283A61 CRC64;
MSKIEMKNGK LIVPNKVTIP FIEGDGVGAE ITPVSQMVVN AAVKKAYNGE KSIEWLEVLA
GDKAQKELGT PLPDETINIF KEYLIGIKGP LTTPVGEGMR SLNVALRQTL DLYVCLRPVR
WFKGTSSPLK EPNKVNMVVF RENTEDIYAG IEWKTGTEEA KKFYNFLKNE MGVTKVRFPE
TSSFGVKPVS EEGSKRLIRS AIEYALSNKL PSVTLVHKGN IMKFTEGGFK KYGYELARKE
FAHQTFTMEE YAEIKKEFGE DKAKEKLKEA KEQGKLIIKD NICDAFLQNT LLKPEDYSVI
ATLNLNGDYV SDQLAAMVGG IGIAPGGNIN YKTGHAIFEA THGTAPDIAG KNKANPCSLI
LSSVMALEYL NMNEAASLII NALEKSFESG YATEDLASFM DNGTKLGTKE FAEKIVSIM
//
