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Entry: A0A0Q9MWB3_9MICC
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ID   A0A0Q9MWB3_9MICC        Unreviewed;       365 AA.
AC   A0A0Q9MWB3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE            EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN   ORFNames=ASG92_01960 {ECO:0000313|EMBL:KRE68645.1};
OS   Arthrobacter sp. Soil736.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736395 {ECO:0000313|EMBL:KRE68645.1, ECO:0000313|Proteomes:UP000051775};
RN   [1] {ECO:0000313|Proteomes:UP000051775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil736 {ECO:0000313|Proteomes:UP000051775};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE68645.1, ECO:0000313|Proteomes:UP000051775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil736 {ECO:0000313|EMBL:KRE68645.1,
RC   ECO:0000313|Proteomes:UP000051775};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC         + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.85;
CC         Evidence={ECO:0000256|ARBA:ARBA00000624};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC         Xref=Rhea:RHEA:18365, ChEBI:CHEBI:15361, ChEBI:CHEBI:15588,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.83;
CC         Evidence={ECO:0000256|ARBA:ARBA00001361};
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:KRE68645.1}.
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DR   EMBL; LMSB01000001; KRE68645.1; -; Genomic_DNA.
DR   RefSeq; WP_056623603.1; NZ_LMSB01000001.1.
DR   AlphaFoldDB; A0A0Q9MWB3; -.
DR   STRING; 1736395.ASG92_01960; -.
DR   OrthoDB; 5289857at2; -.
DR   Proteomes; UP000051775; Unassembled WGS sequence.
DR   GO; GO:0046553; F:D-malate dehydrogenase (decarboxylating) 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:UniProtKB-KW.
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; IPR011829; TTC_DH.
DR   NCBIfam; TIGR02089; TTC; 1.
DR   PANTHER; PTHR43275; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR   PANTHER; PTHR43275:SF1; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211}.
FT   DOMAIN          8..354
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   365 AA;  39285 MW;  79434A6CADBD2E5A CRC64;
     MSATQKFSIA SIPADGVGKE VVSAGRRVLD ALAENSGGKF SFEWTEFPWG CGYFEKTGQM
     MDPNGLETLK DFDAIYFGAV GWENVPDHIS LWGLRLNITQ NFDQWANIRP VKFLPGIQSP
     LRKADNTELD WVVVRENSEG EYAGLGGRNL SGRGPGNEVA LQTALFTEKG CERIMRFAFD
     LARTRTVKKV SSVTKSNAQQ YGMVLWDETF QRVALDYPDV ATESVLVDAM SAKFILKPED
     LSVVVASNLN ADILSDLGSA LAGSLGLAAS ANLNPERRFP SMFEPVHGSA PDIAGQGISN
     PIGAIASAAL MLDHFGLHEE ARRVEAAIEQ TTGAGHLTRD VGGDSTTDDV TDAIIKALTL
     SLAAV
//
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