ID   E8R149_ISOPI            Unreviewed;       499 AA.
AC   E8R149;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|ARBA:ARBA00019562};
DE            EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013};
DE   AltName: Full=IDP {ECO:0000256|ARBA:ARBA00029765};
DE   AltName: Full=NADP(+)-specific ICDH {ECO:0000256|ARBA:ARBA00029990};
DE   AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|ARBA:ARBA00031098};
GN   OrderedLocusNames=Isop_2834 {ECO:0000313|EMBL:ADV63400.1};
OS   Isosphaera pallida (strain ATCC 43644 / DSM 9630 / IS1B).
OC   Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC   Isosphaera.
OX   NCBI_TaxID=575540 {ECO:0000313|EMBL:ADV63400.1, ECO:0000313|Proteomes:UP000008631};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 43644;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Eisen J.A.;
RT   "The complete sequence of chromosome of Isophaera pallida ATCC 43644.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADV63400.1, ECO:0000313|Proteomes:UP000008631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43644 / DSM 9630 / IS1B
RC   {ECO:0000313|Proteomes:UP000008631};
RX   PubMed=21475588; DOI=10.4056/sigs.1533840;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Goker M., Cleland D., Saunders E., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA   Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Detter J.C., Beck B., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Isosphaera pallida type strain (IS1B).";
RL   Stand. Genomic Sci. 4:63-71(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|ARBA:ARBA00001946};
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; CP002353; ADV63400.1; -; Genomic_DNA.
DR   RefSeq; WP_013565688.1; NC_014962.1.
DR   AlphaFoldDB; E8R149; -.
DR   STRING; 575540.Isop_2834; -.
DR   KEGG; ipa:Isop_2834; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_1_0_0; -.
DR   InParanoid; E8R149; -.
DR   OrthoDB; 9806254at2; -.
DR   Proteomes; UP000008631; 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:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 3.30.70.1570; -; 1.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR014273; Isocitrate_DH_bac-typ.
DR   InterPro; IPR040978; Isocitrate_DH_TT1725_C.
DR   InterPro; IPR046997; Isocitrate_DH_TT1725_C_sf.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   NCBIfam; TIGR02924; ICDH_alpha; 1.
DR   PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR   PANTHER; PTHR11835:SF43; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   Pfam; PF18324; Isocitrate_DH_C_bact; 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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ADV63400.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008631}.
FT   DOMAIN          4..334
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   REGION          347..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..371
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   499 AA;  54375 MW;  7E0177102D3923A2 CRC64;
     MGIPITVAYG DGIGPEIMAA TLIVLKEAGA DLEPEVIEIG ESIYQRGVSS GIEPTSWESL
     RRTGVFLKSP VTTPQGGGFK SLNVTIRKGL GLYANVRPCQ AYAPFVRTLH PRMDLVIIRE
     NEEDLYAGIE HRQTDEVMQC LKLISRPGCE RIVRYAFEFA RAHGRTKVTC MTKDNIMKLT
     DGLFHQVFDE IGRDYPELKQ DHLIIDIGAA RLADTPEIFD VIVTPNLYGD ILSDIAAQVA
     GSVGLAGSAN IGDHGAMFEA IHGSAPTIAG KNLANPSGLL QAAVMMLVHL GLGELATTIR
     NAWLRTLEDG LHTADIAGTL TKTTVGTLEF AQAVVERLGQ RPERLKPASF EADNPDPIPA
     PAHPPSLTRA PAPSPAAALP AYRRAPETSK TLVGVDLFLN WREGSPEDLG RTLSKSATPK
     LTLCMITNRG VKVWPNGLPE TFCTDHWRCR FMSERQEPID HRDILELYQR VIQSGFDVIK
     TENLCLFDGV PGFALGQGQ
//