ID A0A099P7Y4_9GAMM Unreviewed; 354 AA.
AC A0A099P7Y4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN ORFNames=LH51_16740 {ECO:0000313|EMBL:KGK41143.1};
OS Nitrincola sp. A-D6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Nitrincola.
OX NCBI_TaxID=1545442 {ECO:0000313|EMBL:KGK41143.1, ECO:0000313|Proteomes:UP000029924};
RN [1] {ECO:0000313|EMBL:KGK41143.1, ECO:0000313|Proteomes:UP000029924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-D6 {ECO:0000313|EMBL:KGK41143.1,
RC ECO:0000313|Proteomes:UP000029924};
RA Valdes N., Rivera-Araya J., Bijman J., Escudero G L., Demergasso C.,
RA Fernandez S., Ferrer A., Chavez R., Levican G.;
RT "Draft Genome Sequence of the Arsenic-Resistant Bacterium Nitrincola sp.
RT Strain A-D6 Isolated from a Salt Flat in Northern Chile.";
RL Submitted (SEP-2014) 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}.
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:KGK41143.1}.
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DR EMBL; JRLB01000101; KGK41143.1; -; Genomic_DNA.
DR RefSeq; WP_036524165.1; NZ_JRLB01000101.1.
DR AlphaFoldDB; A0A099P7Y4; -.
DR STRING; 1545442.LH51_16740; -.
DR OrthoDB; 9806254at2; -.
DR Proteomes; UP000029924; 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 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:UP000029924}.
FT DOMAIN 6..350
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 354 AA; 38938 MW; AC8A023758FF018D CRC64;
MNQSFNIAVI AGDGIGKEVM PEGLRALQAV AERFNISLNY TPIEWASCDY YQQHGQMMPD
DWKAQLSGMD AILFGAAGWP ETVPDHISLW GSLLKFRREF DQYINLRPVR LFEGVPCPLA
GRKAGDIDFY VVRENTEGEY TNLGGRIFEG TDREVVIQES VFTRYGTDRV LKYAFELAQS
RRRKHLTVAT KSNGIAISMP WWDERADAMA EHYPDIHVDK QHIDILSARF VLQPNRFDVV
VASNLFGDIL SDLGPACTGT IGLAPSANLN PEGLFPSLFE PVHGSAPDIY GQNIANPVAM
IWSAALMLNF LGCTDAHDAM LSAIETVLAN GPRTPDLGGT ASTTEMGEAI AALI
//
