ID   Q7V4L5_PROMM            Unreviewed;       474 AA.
AC   Q7V4L5;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 124.
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:CAE22109.1};
GN   OrderedLocusNames=PMT_1935 {ECO:0000313|EMBL:CAE22109.1};
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=74547 {ECO:0000313|EMBL:CAE22109.1, ECO:0000313|Proteomes:UP000001423};
RN   [1] {ECO:0000313|EMBL:CAE22109.1, ECO:0000313|Proteomes:UP000001423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313 {ECO:0000313|Proteomes:UP000001423};
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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; BX548175; CAE22109.1; -; Genomic_DNA.
DR   RefSeq; WP_011131300.1; NC_005071.1.
DR   AlphaFoldDB; Q7V4L5; -.
DR   KEGG; pmt:PMT_1935; -.
DR   eggNOG; COG0538; Bacteria.
DR   HOGENOM; CLU_031953_7_1_3; -.
DR   OrthoDB; 9806254at2; -.
DR   Proteomes; UP000001423; 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; 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   ECO:0000313|EMBL:CAE22109.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001423};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU004446}.
FT   DOMAIN          30..470
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   BINDING         106
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         364
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT   BINDING         409
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   BINDING         448
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   BINDING         452
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   SITE            162
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT   SITE            239
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT   MOD_RES         102
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT   MOD_RES         144
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
SQ   SEQUENCE   474 AA;  51961 MW;  D6DBD6364F78E897 CRC64;
     MAQFEKLSPP SQGTAIRFVN GQPVIPNEPI IPFIRGDGTG VDIWPATQRV LDAAVTKAYQ
     GVRRIEWFKV YAGDEACDLY GTYQYLPEDT LEAIRTYGVA IKGPLTTPIG GGIRSLNVAL
     RQIFDLYSCV RPCRYYKGTP SPHKRPQDLD VIVYRENTED IYMGVEWEAD DPVGKTLREH
     LNTVVIPANG KLGKRQIPEG SGIGIKPVSK HGSQRHIRKA IQHALRLKGD KRHVTLVHKG
     NIMKFTEGAF RDWGYELATS EFRDVCITER ESWILGNLEN DPQLSIQANA RMIEPGYDSL
     TPERKASIDA EVHGVLDAIG TSHGNGQWKA MVLVDDRIAD SIFQQIQTRP QEYSILATLN
     LNGDYISDAA AAMVGGLGMA PGANIGENAA IFEATHGTAP KHAGLDRINP GSVILSGVMM
     LEFLGWQEAA DLITKGLSAA IANQQVTYDL ARLMDPPVDP VSCSGFSEAV ISHF
//