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Database: UniProt/TrEMBL
Entry: A0A127Q0Q2_9BURK
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ID   A0A127Q0Q2_9BURK        Unreviewed;       417 AA.
AC   A0A127Q0Q2;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446};
DE            EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446};
GN   Name=icd {ECO:0000313|EMBL:AMP03584.1};
GN   ORFNames=CPter291_1200 {ECO:0000313|EMBL:AMP13476.1}, CPter91_1201
GN   {ECO:0000313|EMBL:AMP03584.1};
OS   Collimonas pratensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=279113 {ECO:0000313|EMBL:AMP03584.1, ECO:0000313|Proteomes:UP000074561};
RN   [1] {ECO:0000313|Proteomes:UP000074561, ECO:0000313|Proteomes:UP000074914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter291 {ECO:0000313|EMBL:AMP13476.1,
RC   ECO:0000313|Proteomes:UP000074914}, and Ter91
RC   {ECO:0000313|EMBL:AMP03584.1, ECO:0000313|Proteomes:UP000074561};
RA   Song C., Schmidt R., de Jager V., Krzyzanowska D., Jongedijk E., Cankar K.,
RA   Beekwilder J., van Veen A., de Boer W., van Veen J.A., Garbeva P.;
RT   "Exploring the genomic traits of fungus-feeding bacterial genus
RT   Collimonas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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; CP013234; AMP03584.1; -; Genomic_DNA.
DR   EMBL; CP013236; AMP13476.1; -; Genomic_DNA.
DR   RefSeq; WP_061938073.1; NZ_WXXL01000002.1.
DR   AlphaFoldDB; A0A127Q0Q2; -.
DR   STRING; 279113.CPter91_1201; -.
DR   KEGG; cpra:CPter91_1201; -.
DR   PATRIC; fig|279113.10.peg.1201; -.
DR   OrthoDB; 9806254at2; -.
DR   Proteomes; UP000074561; Chromosome.
DR   Proteomes; UP000074914; 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          29..413
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   BINDING         105
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         154
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         340..346
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   BINDING         353
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   BINDING         392
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   BINDING         396
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   SITE            161
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT   SITE            231
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT   MOD_RES         101
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
SQ   SEQUENCE   417 AA;  45525 MW;  B7C5A87D64BB073F CRC64;
     MSQHIKVPAE GKKITVNADY SINVPDNPII PFIEGDGTGV DISPVMIKVV DAAVAKAYGG
     KRKISWMEVF AGEKSTKVYG PDVWLPEETL AAVRDYVVSI KGPLTTPVGG GIRSLNVALR
     QELDLYVCLR PVRYFKGVPS PVREPEKTDM VIFRENSEDI YAGIEWQEGS DGAKKLIEFL
     IKEMGVKKIR FPNTSGIGIK PVSREGTERL VRKAIQYAID NDKPSVTIVH KGNIMKFTEG
     GFRDWAYALA QKEFGAELID GGPWAKFKNP KTGRDIIVKD SIADAFLQQI LLRPNEYSVI
     ATLNLNGDYI SDALAAQVGG IGIAPGANLS DSVAMFEATH GTAPKYAGKD YVNPGSLILS
     AEMMLRHMGW VEAADLIIAS MQKSITSKKV TYDFARLMEG ATQVSCSGFG EVLIENM
//
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