IDH2_COLMA
ID IDH2_COLMA Reviewed; 743 AA.
AC P41561;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Isocitrate dehydrogenase [NADP] 2;
DE EC=1.1.1.42;
DE AltName: Full=IDH-II;
DE AltName: Full=IDP-2;
DE AltName: Full=NADP(+)-specific ICDH 2;
DE AltName: Full=Oxalosuccinate decarboxylase 2;
GN Name=icd2;
OS Colwellia maris.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=77524;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8226630; DOI=10.1128/jb.175.21.6873-6880.1993;
RA Ishii A., Suzuki M., Sahara T., Takada Y., Sasaki S., Fukunaga N.;
RT "Genes encoding two isocitrate dehydrogenase isozymes of a psychrophilic
RT bacterium, Vibrio sp. strain ABE-1.";
RL J. Bacteriol. 175:6873-6880(1993).
RN [2]
RP SEQUENCE REVISION TO 660-673.
RA Ishii A., Suzuki M., Sahara T., Takada Y., Sasaki S., Fukunaga N.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-39.
RX PubMed=1295895; DOI=10.1093/oxfordjournals.jbchem.a123988;
RA Fukunaga N., Imagawa S., Sahara T., Ishii A., Suzuki M.;
RT "Purification and characterization of monomeric isocitrate dehydrogenase
RT with NADP(+)-specificity from Vibrio parahaemolyticus Y-4.";
RL J. Biochem. 112:849-855(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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the monomeric-type IDH family. {ECO:0000305}.
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DR EMBL; D14047; BAA03134.2; -; Genomic_DNA.
DR PIR; A49341; A49341.
DR AlphaFoldDB; P41561; -.
DR SMR; P41561; -.
DR PRIDE; P41561; -.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR InterPro; IPR004436; Isocitrate_DH_NADP_mono.
DR PANTHER; PTHR36999; PTHR36999; 1.
DR Pfam; PF03971; IDH; 1.
DR PIRSF; PIRSF009407; IDH_monmr; 1.
DR TIGRFAMs; TIGR00178; monomer_idh; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese;
KW Metal-binding; NADP; Oxidoreductase; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1295895"
FT CHAIN 2..743
FT /note="Isocitrate dehydrogenase [NADP] 2"
FT /id="PRO_0000083596"
FT BINDING 84..89
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 134..141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 549
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 550
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 554
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 586..587
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 591
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 602..604
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 651
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 257
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 422
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 743 AA; 80882 MW; DE1E71FF4B5A6E06 CRC64;
MSTDNSKIIY TITDEAPALA TYSLLPIIQA YTASSGINVE TRDISLAGRI LANFPKYLTK
EQRIDDALAE LGELAQTPEA NIIKLPNISA SIPQLEAVIK ELQAKGYDLP HYPAEPQNEA
EESIKLTYAK ILGSAVNPVL REGNSDRRAP ASVKQYARNN PHSMGAWSKE SKSHVAHMAS
GDFYGSEKSV TIDGATSVNI EFVAKNGDVT LLKSKLPLLD KEIIDASVMS KSALVEFFET
EINKAKEEDV LLSLHLKATM MKVSDPVMFG HAVRVFYKDV FAKHAATFEQ LGVDADNGIG
DVYAKIARLP AAQKEEIEAD LQAVYATRPE MAMVDSDKGI TNLHVPSDVI IDASMPAALR
ASGMMWGPDG KQKDTKFMIP DRNYAGVFSA VVDFCRENGA FNPATMGTVP NVGLMAQKAE
EYGSHDKTFT MKAAGTVRVV NSQGERLIEQ EVAQGDIYRM CQVKDAPIQD WVKLAVTRAR
ATGTPTVFWL DENRGHDEQM IKKVNTYLAD HDTTGLDIQI LEPVKACEFT LARVAKGEDA
ISVTGNVLRD YLTDLFPILE LGTSAKMLSI VPLMNGGGLF ETGAGGSAPK HVQQFEKENH
LRWDSLGEFL ALAASLEHVA VTTGNARAQI LADTLDAATG KFLDTNKSPS RKVGELDNRG
SHFYLAMYWA QALAAQTTDT ELQASFSSVA QALTKQEEKI VAELNAAQGP AIDLNGYYFA
DTKLAEKAMR PSETFNTILS ALL
