ID A0A0P0MHC2_9BURK Unreviewed; 361 AA.
AC A0A0P0MHC2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN Name=dmlA {ECO:0000313|EMBL:ALK92517.1};
GN ORFNames=L103DPR2_02127 {ECO:0000313|EMBL:ALK92517.1};
OS Limnohabitans sp. 103DPR2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1678129 {ECO:0000313|EMBL:ALK92517.1, ECO:0000313|Proteomes:UP000063254};
RN [1] {ECO:0000313|EMBL:ALK92517.1, ECO:0000313|Proteomes:UP000063254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=103DPR2 {ECO:0000313|EMBL:ALK92517.1,
RC ECO:0000313|Proteomes:UP000063254};
RA Ahn J.-H., Kim S.B.;
RT "Limnohabitans sp. 2 strains.";
RL Submitted (JUN-2015) 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; CP011834; ALK92517.1; -; Genomic_DNA.
DR RefSeq; WP_055361061.1; NZ_CP011834.1.
DR AlphaFoldDB; A0A0P0MHC2; -.
DR STRING; 1678129.L103DPR2_02127; -.
DR KEGG; lim:L103DPR2_02127; -.
DR PATRIC; fig|1678129.3.peg.2116; -.
DR OrthoDB; 5289857at2; -.
DR Proteomes; UP000063254; 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 Oxidoreductase {ECO:0000313|EMBL:ALK92517.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000063254}.
FT DOMAIN 5..357
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 361 AA; 39547 MW; 4EBF6CC5772CE6E9 CRC64;
MSQKRIAVIA GDGIGKEVMP EGLRVMEAAA SKFNLDLKFD HFDFSSWDYF EKHGQMLPDN
WKDQIGGHDA IYFGAVGWPE KIADHVSLWG SLLLFRREFD QYINLRPARL MPGIIAPVVR
RDGSPRQPGE IDMYIVRENT EGEYSSIGGR MFPGTQREIV MQETVMSRVG VDRVLKFAFE
LAQSRPKKHL TSATKSNGIA ITMPYWDERV VEMAKNYPGV NVDKFHIDIL TAHFVQRPDF
FDVVVASNLF GDILSDLGPA CTGTIGIAPS ANLNPDRTHP SLFEPVHGSA PDIAGKNIAN
PIGQIWCGAM MLEFLGCKPA HDAVLAAIEK VLAPNSGAPR TADIGGSANT QDVGKAIAAA
L
//
