ID   C4XH10_SOLM1            Unreviewed;       383 AA.
AC   C4XH10;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=isocitrate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00013013};
DE            EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013};
GN   Name=icd {ECO:0000313|EMBL:BAH76313.1};
GN   OrderedLocusNames=DMR_28220 {ECO:0000313|EMBL:BAH76313.1};
OS   Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
OS   (Desulfovibrio magneticus).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Solidesulfovibrio.
OX   NCBI_TaxID=573370 {ECO:0000313|EMBL:BAH76313.1, ECO:0000313|Proteomes:UP000009071};
RN   [1] {ECO:0000313|EMBL:BAH76313.1, ECO:0000313|Proteomes:UP000009071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700980 / DSM 13731 / RS-1
RC   {ECO:0000313|Proteomes:UP000009071};
RX   PubMed=19675025; DOI=10.1101/gr.088906.108;
RA   Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N.,
RA   Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H.,
RA   Matsunaga T.;
RT   "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed
RT   common gene clusters in magnetotactic bacteria.";
RL   Genome Res. 19:1801-1808(2009).
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; AP010904; BAH76313.1; -; Genomic_DNA.
DR   RefSeq; WP_015861478.1; NC_012796.1.
DR   AlphaFoldDB; C4XH10; -.
DR   STRING; 573370.DMR_28220; -.
DR   KEGG; dma:DMR_28220; -.
DR   eggNOG; COG0538; Bacteria.
DR   HOGENOM; CLU_031953_7_1_7; -.
DR   OrthoDB; 9806254at2; -.
DR   Proteomes; UP000009071; 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   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          4..379
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         274
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT   BINDING         319
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   383 AA;  41109 MW;  F21089CA0C891D98 CRC64;
     MEKTVFWIEG DGIGPDVWKA GRPVLDAAVD KAYGGARKLV WKELLAGEKA FKEVGEYLPQ
     ATVEALTTAE LAFKGPLGTP VGGGFRSLNV TLRQVLDLYA CIRPIRYFQG IESPVKRPDL
     VDMIIFRENT EDVYAGIEYA TGTPEAKRLI AFLRDELGAK VDETAGIGIK PITPAGSKRL
     VRKAIQHAVD HKKPSVTLVH KGNIMKYTEG AFRAFGYEVA AQEFAAQCMT EQDAAAGGTK
     PIVVKDRIAD NMFQVALMRP QDYSVIATTN LNGDYISDAL AAQVGGLGLA PGVNMSEKLA
     FFEPTHGTAP GIAGKDKANP GSLILSGAML LEHLGWHEAA KLIHDSMDKT ISEKKVTVDL
     ADQIPGATTI GCAAFGELLA KNL
//