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Entry: A0A0K9Y159_9FLAO
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ID   A0A0K9Y159_9FLAO        Unreviewed;       478 AA.
AC   A0A0K9Y159;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=AC804_06050 {ECO:0000313|EMBL:KNB62406.1};
OS   Chryseobacterium sp. Hurlbut01.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1681828 {ECO:0000313|EMBL:KNB62406.1, ECO:0000313|Proteomes:UP000036769};
RN   [1] {ECO:0000313|Proteomes:UP000036769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hurlbut01 {ECO:0000313|Proteomes:UP000036769};
RA   Couger M.B., Youseff N., Elshahed M., French D., Hoff W.;
RT   "Draft Genome Sequence of the Environmental Isolate Chryseobacterium sp.
RT   Hurlbut 01.";
RL   Submitted (JUL-2015) 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}.
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:KNB62406.1}.
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DR   EMBL; LGIP01000003; KNB62406.1; -; Genomic_DNA.
DR   RefSeq; WP_050378174.1; NZ_LGIP01000003.1.
DR   AlphaFoldDB; A0A0K9Y159; -.
DR   PATRIC; fig|1681828.3.peg.3443; -.
DR   Proteomes; UP000036769; 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   ECO:0000313|EMBL:KNB62406.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          3..334
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   478 AA;  53015 MW;  015110C769AF56BC CRC64;
     MKRITVAKGD GIGPEIMDAT LKIILAAGAE LEIDEIEIGE KVYLSGNTSG ISSESWDIIR
     RNKIFLKAPI TTPQGGGYKS LNVTTRKFLG LYANVRPCTS LHPFVSTKHP VMDMVIVREN
     EEDLYAGIEH QQTDEVIQCL KLISRPGCEK IVRYAFEYAK QQNRKKVTCF SKDNIMKQTD
     GLFHQVFNEI AKEYPEIENE HWIVDIGAAK VADTPEDFDV IVMPNLYGDI ISDIAAQITG
     SVGLAGSANI GEECSMFEAI HGSAPTIAGQ NVANPSGLLQ GAVMMLNHIG QTEVAEKIQN
     AWLKTLEDGI HTQDIYKEST SKQKVGTKEF ADAVIANLGQ KPAQLKPVSY ANNTVMNLPK
     YQRKPSAKKE LAGVDVFVHW SGTNPDELAD KMKSIESDGI NLSMITNRGI KVWPDGFKET
     FCTDHWRCRF KPSENQKIQK EHVIKLLQNA LHEIIDVVKT ENLYDFDGKA GYSLGQGQ
//
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