IDH_SYNY3
ID IDH_SYNY3 Reviewed; 475 AA.
AC P80046; P72820;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Isocitrate dehydrogenase [NADP];
DE Short=IDH;
DE EC=1.1.1.42;
DE AltName: Full=IDP;
DE AltName: Full=NADP(+)-specific ICDH;
DE AltName: Full=Oxalosuccinate decarboxylase;
GN Name=icd; OrderedLocusNames=slr1289;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8763933; DOI=10.1128/jb.178.14.4070-4076.1996;
RA Muro-Pastor M.I., Reyes J.C., Florencio F.J.;
RT "The NADP+-isocitrate dehydrogenase gene (icd) is nitrogen regulated in
RT cyanobacteria.";
RL J. Bacteriol. 178:4070-4076(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP PROTEIN SEQUENCE OF 1-20.
RX PubMed=1730247; DOI=10.1111/j.1432-1033.1992.tb19833.x;
RA Muro-Pastor M.I., Florencio F.J.;
RT "Purification and properties of NADP-isocitrate dehydrogenase from the
RT unicellular cyanobacterium Synechocystis sp. PCC 6803.";
RL Eur. J. Biochem. 203:99-105(1992).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibition of this enzyme by phosphorylation
CC regulates the branch point between the Krebs cycle and the glyoxylate
CC bypass, which is an alternate route that accumulates carbon for
CC biosynthesis when acetate is the sole carbon source for growth.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; X83563; CAA58549.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA16835.1; -; Genomic_DNA.
DR PIR; S74684; S74684.
DR AlphaFoldDB; P80046; -.
DR SMR; P80046; -.
DR IntAct; P80046; 2.
DR STRING; 1148.1651909; -.
DR PaxDb; P80046; -.
DR PRIDE; P80046; -.
DR EnsemblBacteria; BAA16835; BAA16835; BAA16835.
DR KEGG; syn:slr1289; -.
DR eggNOG; COG0538; Bacteria.
DR InParanoid; P80046; -.
DR PhylomeDB; P80046; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR43504; PTHR43504; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00183; prok_nadp_idh; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glyoxylate bypass; Magnesium;
KW Manganese; Metal-binding; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..475
FT /note="Isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000083570"
FT BINDING 104
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 394..400
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 160
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 237
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CONFLICT 60..62
FT /note="REE -> ERK (in Ref. 2; BAA16835)"
FT /evidence="ECO:0000305"
FT CONFLICT 83..84
FT /note="IF -> YL (in Ref. 2; BAA16835)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="K -> L (in Ref. 2; BAA16835)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="P -> A (in Ref. 2; BAA16835)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="C -> L (in Ref. 2; BAA16835)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 52275 MW; 6F3254A8BBA75F92 CRC64;
MYEKLQPPSV GSKITFVAGK PVVPNDPIIP YIRGDGTGVD IWPATELVIN AAIAKAYGGR
EEINWFKVYA GDEACELYGT YQIFPEDTLT AIKEYGVAIK GPLTTPVGGG IRSLNVALRQ
IFDLYTCVRP CRYYPGTPSP HKTPEKLDII VYRENTEDIY LGIEWAEGTE GAKKLIAYLN
DELIPTTPAL GKKQIRLDSG IGIKPISKTG SQRLVRRAIL HAKRLPKAKQ MVTLVHKGNI
MKFTEGPFRD WGYELATTEF RAECVTERES WICGNKESNP DLTIEANAHM IDPGYDTLTE
EKQAVIKQEV EQVLNSIWES HGNGQWKEKV MVNDRIADSI FQQIQTRPDE YSILATMNLN
GDYLSDAAAA VVGGLGMGPG ANIGDSAAIF EATHGTAPKH AGLDRINPGS VILSGVMMLE
FMGWQEAADL IKKGIGAAIA NREVTYDLAR LMEPKVDKPL KCSEFAQAIV SHFDD
