ID   Q30VM7_OLEA2            Unreviewed;       382 AA.
AC   Q30VM7;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=isocitrate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00013013};
DE            EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013};
GN   OrderedLocusNames=Dde_3476 {ECO:0000313|EMBL:ABB40269.1};
OS   Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS   (Desulfovibrio alaskensis).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Oleidesulfovibrio.
OX   NCBI_TaxID=207559 {ECO:0000313|EMBL:ABB40269.1, ECO:0000313|Proteomes:UP000002710};
RN   [1] {ECO:0000313|EMBL:ABB40269.1, ECO:0000313|Proteomes:UP000002710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA 1058 / DSM 17464 / G20
RC   {ECO:0000313|Proteomes:UP000002710};
RX   PubMed=21685289; DOI=10.1128/JB.05400-11;
RA   Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA   Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA   Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA   Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT   "Complete genome sequence and updated annotation of Desulfovibrio
RT   alaskensis G20.";
RL   J. Bacteriol. 193:4268-4269(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; CP000112; ABB40269.1; -; Genomic_DNA.
DR   RefSeq; WP_011369174.1; NC_007519.1.
DR   AlphaFoldDB; Q30VM7; -.
DR   STRING; 207559.Dde_3476; -.
DR   KEGG; dde:Dde_3476; -.
DR   eggNOG; COG0538; Bacteria.
DR   HOGENOM; CLU_031953_7_1_7; -.
DR   Proteomes; UP000002710; 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:ABB40269.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002710};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          4..378
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         93
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         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         273
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT   BINDING         318
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   SITE            134
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT   SITE            201
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT   MOD_RES         74
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT   MOD_RES         116
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
SQ   SEQUENCE   382 AA;  41273 MW;  5ECA1783E7A269A3 CRC64;
     MRKTVYFIEG DGIGPEVWNA ARPVIDKAVE LAYGNGRSLE WKELLAGEKA YAETGTYLPQ
     ETLDTLAGAE LAIKGPLGTP VGKGFRSLNV TMRQTLDLYA CIRPIRYFEG IESPVKHPER
     VNMVVFRENT EDVYAGIEYK ADTDEARKLI AFLRDELGAN VDERCAVGIK PMSEKGSKRL
     VRRAMDFALA QGLPSVTLVH KGNIMKFTEG GFRQWGYELA HDEYAGRAVT EAQAAAGETG
     LVVKDRIADA MFQEVLIRPE QYSVVATSNL NGDYISDALA AQVGGLGLAP GVNMSDTLAF
     FEATHGTAPT IAGKDMANPG SLILCGGMLL EHLGWHEAAT RIHTAMNTVI GNRTVTVDLA
     SQMQGASTVG CRQFGELLGA AL
//