ID A9DIJ5_9FLAO Unreviewed; 503 AA.
AC A9DIJ5;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 ORFNames=KAOT1_11897 {ECO:0000313|EMBL:EDP97915.1};
OS Kordia algicida OT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Kordia.
OX NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP97915.1, ECO:0000313|Proteomes:UP000002945};
RN [1] {ECO:0000313|EMBL:EDP97915.1, ECO:0000313|Proteomes:UP000002945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT-1 {ECO:0000313|EMBL:EDP97915.1,
RC ECO:0000313|Proteomes:UP000002945};
RX PubMed=21622754; DOI=10.1128/JB.05241-11;
RA Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL J. Bacteriol. 193:4031-4032(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP97915.1}.
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DR EMBL; ABIB01000001; EDP97915.1; -; Genomic_DNA.
DR RefSeq; WP_007094929.1; NZ_DS544873.1.
DR AlphaFoldDB; A9DIJ5; -.
DR STRING; 391587.KAOT1_11897; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_1_0_10; -.
DR OrthoDB; 9806254at2; -.
DR Proteomes; UP000002945; Unassembled WGS sequence.
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002945}.
FT DOMAIN 19..350
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 503 AA; 55443 MW; 13A29AE6FF5F40A1 CRC64;
MENIKTQVTQ AQHTATKTKV AVAYGDGIGP EIMKATLKIL EASGANIEPE IIEVGEKVYL
SGNSSGIEKK SWEAINRNKI ILKAPITTPQ GKGYKSLNVT LRKSLGLFAN VRPVNALHPY
VQTHFPNMDV VIIRENEEDL YAGIEHQQTQ DVVQCLKLIT RPGCEKIVRY AFEYAKLYGR
KKVTCMVKDN IMKLTDGLFH NVFKEIAAEY PEIKSESQII DIGSARLAAN PENYDVVVTS
NLYGDIISDI AAEIAGSVGM AGSANVGKNV AMFEAIHGSA PDIAGRAIAN PSGLLNAAVM
MLIHIGKANI ANKIKNAWLT TIEQGYHTAD IYKEGQSKQK MSTSEFADKV IENLGKTPQQ
LTPSTIDENV GNIQIPEYNR PKQEQALVGT DVFINWQGSN PQEIGDALAS LQSYKLKLKM
ITNRGVKVYP NGLPETYCTD HWRCRFVATD AVINGEKPKY MPVDFEQILA LLSNINEIGY
EVIKTENLYE FDGKRGFSLG QGE
//
