ID   F5X5K1_STRPX            Unreviewed;       391 AA.
AC   F5X5K1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|ARBA:ARBA00019562};
DE            EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013};
DE   AltName: Full=IDP {ECO:0000256|ARBA:ARBA00029765};
DE   AltName: Full=NADP(+)-specific ICDH {ECO:0000256|ARBA:ARBA00029990};
DE   AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|ARBA:ARBA00031098};
GN   Name=icd {ECO:0000313|EMBL:BAK29691.1};
GN   OrderedLocusNames=SGPB_0584 {ECO:0000313|EMBL:BAK29691.1};
OS   Streptococcus pasteurianus (strain ATCC 43144 / JCM 5346 / CDC 1723-81).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=981540 {ECO:0000313|EMBL:BAK29691.1, ECO:0000313|Proteomes:UP000007946};
RN   [1] {ECO:0000313|EMBL:BAK29691.1, ECO:0000313|Proteomes:UP000007946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43144 / JCM 5346 / CDC 1723-81
RC   {ECO:0000313|Proteomes:UP000007946};
RX   PubMed=21633709; DOI=10.1371/journal.pone.0020519;
RA   Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M.,
RA   Chang C.-H., Hsu M.-T.;
RT   "Sequencing and comparative genome analysis of two pathogenic Streptococcus
RT   gallolyticus subspecies: genome plasticity, adaptation and virulence.";
RL   PLoS ONE 6:E20519-E20519(2011).
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; AP012054; BAK29691.1; -; Genomic_DNA.
DR   RefSeq; WP_013851634.1; NC_015600.1.
DR   AlphaFoldDB; F5X5K1; -.
DR   STRING; 981540.SGPB_0584; -.
DR   GeneID; 76467553; -.
DR   KEGG; stb:SGPB_0584; -.
DR   HOGENOM; CLU_031953_7_1_9; -.
DR   Proteomes; UP000007946; 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   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   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604439-3};
KW   Manganese {ECO:0000256|PIRSR:PIRSR604439-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR604439-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:BAK29691.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007946};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          19..387
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         283
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT   BINDING         330
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   SITE            149
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT   SITE            219
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT   MOD_RES         89
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT   MOD_RES         102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT   MOD_RES         131
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
SQ   SEQUENCE   391 AA;  42591 MW;  8D00AB2684BB62BA CRC64;
     MADKIILENG HLTVSNNPII PFIEGDGVGR DIWKNARAVF DAAIDKAYQG QKKVEWLELL
     AGKKAHEATG EWLPEATLET IKEDLVAIKG PLETPVGGGI RSLNVALRQE LDLYACVRPV
     RYFKGIESPL KEPEKTSITI FRENTEDIYA GIEWNAGTEE VKKVIDFLQN EMSVSKIRFP
     ETSSIGIKPI SQEGSERLIR SAIEYALANN LTKVTLVHKG NIQKFTEGGF RSWGYDLAKR
     EYADELASGK LVINDIIADN FLQQILLNPE KFDVVALTNL NGDYASDALA AQVGGIGISP
     GANINYLTGH AIFEATHGTA PDIAGKDIAN PCSVLLSGCM LFDYIGWTEV ASLITAAIEK
     TFAQGQFTAD LAQEKVACST SGFAAKLIEN L
//