IDH_SPHYA
ID IDH_SPHYA Reviewed; 406 AA.
AC P50215;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
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; Synonyms=idhA;
OS Sphingobium yanoikuyae (Sphingomonas yanoikuyae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=13690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 6900 / JCM 10274 / B1;
RX PubMed=8626059; DOI=10.1016/0378-1119(95)00732-6;
RA Wang Y., Lau P.C.K.;
RT "Sequence and expression of an isocitrate dehydrogenase-encoding gene from
RT a polycyclic aromatic hydrocarbon oxidizer, Sphingomonas yanoikuyae B1.";
RL Gene 168:15-21(1996).
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 -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; U37523; AAC43640.1; -; Genomic_DNA.
DR PIR; JC4600; JC4600.
DR RefSeq; WP_004211167.1; NZ_QRAL01000015.1.
DR AlphaFoldDB; P50215; -.
DR SMR; P50215; -.
DR STRING; 13690.CP98_01384; -.
DR eggNOG; COG0538; Bacteria.
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:0006102; P:isocitrate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004790; Isocitrate_DH_NADP.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR11822; PTHR11822; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR PIRSF; PIRSF000108; IDH_NADP; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00127; nadp_idh_euk; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP;
KW Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle.
FT CHAIN 1..406
FT /note="Isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000083567"
FT BINDING 75..77
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 94..100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 308..313
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 139
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 210
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 406 AA; 45483 MW; 093F7E18303A89E7 CRC64;
MAKIKVKNPV VEIDGDEMTR IIWEWIRERL ILPYLDVDLK YYDLSVEKRD ETSDQITIDA
ANAIKEYGVG VKCATITPDE ARVEEFGLKK MWKSPNGTIR NILGGVVFRE PIVIKNVPRL
VPGWTDPIVV GRHAFGDQYK ATDFKVPGAG TLTMKWVGTN GEELEYEVFE FPSAGVAMGM
YNLDESIRDF AKASFNYGLN RGWPVYLSTK NTILKAYDGR FKDLFQEVFD AEFADKFKAA
GIVYEHRLID DMVASALKWS GKFVWACKNY DGDVQSDTVA QGFGSLGLMT SVLLSPDGKT
VEAEAAHGTV TRHYRQHQQG KATSTNPIAS IFAWTQGLSF RGKFDDTPDV VKFAETLEQV
CIKTVEGGAM TKDLALLIGP DQAWMTTEQF FEAIRVNLEA EMAKWA
