ID A0A2E8EDQ9_9ARCH Unreviewed; 329 AA.
AC A0A2E8EDQ9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Isocitrate dehydrogenase {ECO:0000313|EMBL:MBQ03383.1};
DE EC=1.1.1.41 {ECO:0000313|EMBL:MBQ03383.1};
GN ORFNames=CL673_01550 {ECO:0000313|EMBL:MBQ03383.1};
OS Candidatus Bathyarchaeota archaeon.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=2026714 {ECO:0000313|EMBL:MBQ03383.1, ECO:0000313|Proteomes:UP000230510};
RN [1] {ECO:0000313|Proteomes:UP000230510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Graham E.D., Heidelberg J.F.;
RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT Global Oceans.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:MBQ03383.1}.
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DR EMBL; PBSW01000019; MBQ03383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2E8EDQ9; -.
DR Proteomes; UP000230510; Unassembled WGS sequence.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) 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:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR011828; LEU3_arc.
DR NCBIfam; TIGR02088; LEU3_arch; 1.
DR PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR PANTHER; PTHR11835:SF34; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00180; Iso_dh; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:MBQ03383.1}.
FT DOMAIN 3..325
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 329 AA; 35402 MW; 5AD98A1ED6D07F3E CRC64;
MYDVAVVPGD GIGKEVVPEA VRALESTGLE FNFHRFDVGY EVFKRDGNPV PNEAIVGIKQ
NPVCLFGATT TPLGIPNYSS AILTLRKALG VYANIRPAKS CPVRWSRDGV DLVVVRENTE
GLYSGIEFGD RDRAYTLRVI SLEASERIAK CAFKLAMSRR RQLTLVTKAN VLRKTDGLFR
DVSLGVAEEH PEVEVNELLV DVAAMHIVMK PQIFDVILAP NLYGDILSDE AAGLVGGLGL
APSASIGDDY ALFEPVHGSA PDIAGKGIAN PMAAILSAKM MLEHIGEDKW AHKLEAAVIS
VLMEGKHLTP DIGGNSTTLE VTDAIIKAL
//
