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Database: UniProt
Entry: A0A2D1SZ54_9BACL
LinkDB: A0A2D1SZ54_9BACL
Original site: A0A2D1SZ54_9BACL 
ID   A0A2D1SZ54_9BACL        Unreviewed;       363 AA.
AC   A0A2D1SZ54;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE            EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN   ORFNames=CSE16_08075 {ECO:0000313|EMBL:ATP42402.1};
OS   Solibacillus sp. R5-41.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Solibacillus.
OX   NCBI_TaxID=2048654 {ECO:0000313|EMBL:ATP42402.1, ECO:0000313|Proteomes:UP000222866};
RN   [1] {ECO:0000313|EMBL:ATP42402.1, ECO:0000313|Proteomes:UP000222866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R5-41 {ECO:0000313|EMBL:ATP42402.1,
RC   ECO:0000313|Proteomes:UP000222866};
RA   Guo Y., Chen Z., Wang H.;
RT   "Complete genome sequence of Solibacillus sp. R5-41.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP024123; ATP42402.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D1SZ54; -.
DR   KEGG; sob:CSE16_08075; -.
DR   OrthoDB; 9806254at2; -.
DR   Proteomes; UP000222866; Chromosome.
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   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   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222866}.
FT   DOMAIN          5..348
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   363 AA;  39915 MW;  4582C64C6F522EE1 CRC64;
     MTATRIAIIP GDGIGKEVME EAIKVLEVLQ EHDHTLQIEA TIFPWSSDYY LEHGRMMPNN
     ALETLAQYDA ILFGAIGDDR VPDDVTVWEL IMPIRKQFQQ YVNFRPIKSL PGIASPLANG
     KNIDFVIFRE NAEGEYSNSG GRIYNDQPQE MTIQNTIMTR IGIEKIVRAA CNYAHKHHKT
     KITSATKSNA IIHSMKFWDE HTKRVLGNTS PTLQLESIYI DALVAYFVER PQDFEVVVAS
     NLFGDILSDL GSALVGGLGL SPSANLNPEK AFPSMFEPVH GSAPNIAGKG IANPIAQIWS
     LALLFGHIGR PEVEELIVSA IEKVLREGSV KTADIGGQAN TQEMGNAICE VIVAMKSIAT
     RSD
//
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