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Database: UniProt
Entry: I3Z0K5_BELBD
LinkDB: I3Z0K5_BELBD
Original site: I3Z0K5_BELBD 
ID   I3Z0K5_BELBD            Unreviewed;       484 AA.
AC   I3Z0K5;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
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=Belba_0102 {ECO:0000313|EMBL:AFL82773.1};
OS   Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Belliella.
OX   NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL82773.1, ECO:0000313|Proteomes:UP000006050};
RN   [1] {ECO:0000313|Proteomes:UP000006050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134
RC   {ECO:0000313|Proteomes:UP000006050};
RA   Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA   Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I.,
RA   Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Belliella baltica DSM 15883.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003281; AFL82773.1; -; Genomic_DNA.
DR   RefSeq; WP_014770790.1; NC_018010.1.
DR   AlphaFoldDB; I3Z0K5; -.
DR   STRING; 866536.Belba_0102; -.
DR   KEGG; bbd:Belba_0102; -.
DR   PATRIC; fig|866536.3.peg.108; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_1_0_10; -.
DR   OrthoDB; 9806254at2; -.
DR   Proteomes; UP000006050; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006050}.
FT   DOMAIN          6..337
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   484 AA;  53248 MW;  595471ADA9AFCAB5 CRC64;
     MSSKTKITVA YGDGIGPEIM KATLNILEAA GAQLEYDVIE IGEQVYLKGI SSGMEPKAFD
     SLRETKVFLK SPITTPQGGG FKSLNVTTRK SFGLFANVRP CKAYSPFVKT HFPKTDMVII
     RENEEDLYAG IEHRQTQEVY QCLKLISQPG SEKIIRYAFE YAKKYNRKKV TCMTKDNIMK
     LADGLFHKTF DEIAKEYPEI ETDHKIIDIG SALIAERPEI FDVIVTLNLY GDIISDIAAQ
     VTGSVGLGGS ANVGAEVAMF EAIHGSAPDI AGKDMANPSG LLNGAVMMLV HIGQPEIAEK
     IANAWMKTLE DGIHTGDIYQ EGLSSKKVGT QEFAKAVIER LGQLPVNMVP AVFDKSSTDP
     INIKLAPVTK SEKKLIGVDV FIDWDKDGRD PNSIGDTLRK ADANGLVLQL ITNRGIKVYP
     GGMKETFCTD HWRCRFQKAD QSPVTHAEVL DLMDQVAKLG FDFIKTENLY SFDGVRAYSL
     AQGE
//
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