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Database: UniProt/TrEMBL
Entry: Q5M3U5_STRT2
LinkDB: Q5M3U5_STRT2
Original site: Q5M3U5_STRT2 
ID   Q5M3U5_STRT2            Unreviewed;       391 AA.
AC   Q5M3U5;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   24-JAN-2024, entry version 113.
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:AAV60898.1};
GN   OrderedLocusNames=stu1266 {ECO:0000313|EMBL:AAV60898.1};
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199 {ECO:0000313|EMBL:AAV60898.1, ECO:0000313|Proteomes:UP000001170};
RN   [1] {ECO:0000313|EMBL:AAV60898.1, ECO:0000313|Proteomes:UP000001170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311 {ECO:0000313|Proteomes:UP000001170};
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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; CP000023; AAV60898.1; -; Genomic_DNA.
DR   RefSeq; WP_011226165.1; NC_006448.1.
DR   AlphaFoldDB; Q5M3U5; -.
DR   STRING; 264199.stu1266; -.
DR   GeneID; 66899055; -.
DR   KEGG; stl:stu1266; -.
DR   PATRIC; fig|264199.4.peg.1248; -.
DR   eggNOG; COG0538; Bacteria.
DR   HOGENOM; CLU_031953_7_1_9; -.
DR   OMA; CVRPCRY; -.
DR   Proteomes; UP000001170; 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:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000001170};
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;  43219 MW;  8C4549316A051441 CRC64;
     MAERILMTNG NLKVTDNPII PFIEGDGVGR DIWKNAQAIF DKAVEVAYGG QRRIEWQEFL
     AGKKAFDKTG EWLPQETLEA IRESLVAIKG PLETPVGGGI RSLNVALRQE LDLYACVRPV
     RYFEGVASPL KEPEKTDITI FRENTEDIYA GIEWEAGTVD VERVIAFFQT EMNVDKIRFP
     KSSSIGIKPI SIEGSKRLIR SAIDYALKNN LKKVTLVHKG NIQKFTEGGF RKWGYEVAEE
     EYKEEMLAGR LEVNDIIADN FLQQILLNPE KFDVVALTNL NGDYASDALA AQVGGIGISP
     GANINYQTGH AIFEATHGTA PDIADQDRAN PCSILLSGCM LLEYIGWSEA AELIISAIEK
     NFKSGIFTAD LAFGKRAYST SGFSNQILSI I
//
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