ID   G3A9Z4_9RALS            Unreviewed;       361 AA.
AC   G3A9Z4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE            EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN   ORFNames=RALSY_mp10669 {ECO:0000313|EMBL:CCA88128.1};
OS   Ralstonia syzygii R24.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=907261 {ECO:0000313|EMBL:CCA88128.1};
RN   [1] {ECO:0000313|EMBL:CCA88128.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R24 {ECO:0000313|EMBL:CCA88128.1};
RX   PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA   Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA   Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT   "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT   solanacearum strains form a single genomic species despite divergent
RT   lifestyles.";
RL   PLoS ONE 6:e24356-e24356(2011).
RN   [2] {ECO:0000313|EMBL:CCA88128.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R24 {ECO:0000313|EMBL:CCA88128.1};
RA   Genoscope - CEA;
RL   Submitted (APR-2011) 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; FR854090; CCA88128.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3A9Z4; -.
DR   GO; GO:0046553; F:D-malate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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   Lyase {ECO:0000313|EMBL:CCA88128.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Oxidoreductase {ECO:0000313|EMBL:CCA88128.1}.
FT   DOMAIN          5..349
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   361 AA;  39035 MW;  DE57C9507D9FE8A9 CRC64;
     MKTYRIATIP GDGIGKEVVP AGREVMEALA AAGAGFRFEF ENFDWGGDYY RRHGAMMPED
     GLDALRGKDA ILFGSAGDAQ IPDHITLWGL RLKICQGFDQ YANVRPTRIL PGIDAPLKRC
     GPKDLDWVIV RENSEGEYAG VGGRVHQGHP IEAATDVSMM TRAGVERIMR FAFTLAQSRP
     RKLLTVITKS NAQRHAMVMW DEIAVQVSKE FPDVKWDKEL VDAATARMVN RPASLDTIVA
     TNLHADILSD LAAALAGSLG IAPTGNIDPE RRYPSMFEPI HGSAFDIMGK GLANPIGTFW
     SVVMLLEHLG EQAAARRVMQ AIEAVTATPA LHTRDLGGNA TTAQVTQAVC AFVAASQAQA
     A
//