ID   B1WXK9_CROS5            Unreviewed;       496 AA.
AC   B1WXK9;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 87.
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:ACB52550.1};
GN   OrderedLocusNames=cce_3202 {ECO:0000313|EMBL:ACB52550.1};
OS   Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS   ATCC 51142)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX   NCBI_TaxID=43989 {ECO:0000313|EMBL:ACB52550.1, ECO:0000313|Proteomes:UP000001203};
RN   [1] {ECO:0000313|EMBL:ACB52550.1, ECO:0000313|Proteomes:UP000001203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51142 / BH68 {ECO:0000313|Proteomes:UP000001203};
RX   PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA   Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA   Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA   Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT   "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT   important in the marine nitrogen cycle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
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; CP000806; ACB52550.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1WXK9; -.
DR   STRING; 43989.cce_3202; -.
DR   KEGG; cyt:cce_3202; -.
DR   eggNOG; COG0538; Bacteria.
DR   HOGENOM; CLU_031953_7_1_3; -.
DR   Proteomes; UP000001203; Chromosome circular.
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; 2.
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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000001203};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU004446}.
FT   DOMAIN          49..490
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   BINDING         125
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         383
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT   BINDING         428
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   BINDING         467
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   BINDING         471
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   SITE            181
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT   SITE            258
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT   MOD_RES         121
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT   MOD_RES         134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT   MOD_RES         163
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
SQ   SEQUENCE   496 AA;  54936 MW;  AA93BA2BC59A0564 CRC64;
     MGELNRLGSV IKKQPLIIDH FMYEKLTPPT TGSKITFKDG KPIVPNDPIV PFIRGDGTGV
     DIWPATEKVI DAAVKTAYGD SKKINWFKVY AGDEACDKYG TYQYLPEDTL TAIREYGIAI
     KGPLTTPVGG GIRSLNVALR QIFELYACVR PCRYYPGTPS PHKSPEKLDV IVYRENTEDI
     YLGIEWKEGT ELAQKLINYL NNELIPATPE HGKKQIRLDS GIGVKPISKT GSQRLVRRAI
     EHALRLPKAK QMVTLVHKGN IMKYTEGSFR DWGYELATSE FREVCVTERE SWILSNKEGN
     ADISIEDNAR KVEPGYDGLT LDKKEEICGE VKGVLDAIWD SHGDGKWKDK IMVNDRIADS
     IFQQIQTRPD EYSILATMNL NGDYLSDAAA AVVGGLGMGP GANIGDTCAI FEATHGTAPK
     HAGLDRINPG SVILSGVMML EYMGWKEAAE LIKKGIGNAI ANRQVTYDLA RLMEPKVDPP
     LKCSEFAQAI IDHFND
//