ID A0A0D8KJM2_9HYPH Unreviewed; 347 AA. AC A0A0D8KJM2; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 19-JAN-2022, entry version 17. DE RecName: Full=D-malate dehydrogenase [decarboxylating] {ECO:0000256|ARBA:ARBA00013301}; DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126}; DE EC=1.1.1.93 {ECO:0000256|ARBA:ARBA00013144}; DE EC=4.1.1.73 {ECO:0000256|ARBA:ARBA00012223}; GN ORFNames=RS75_04090 {ECO:0000313|EMBL:KJF69156.1}; OS Rhizobium nepotum 39/7. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1368418 {ECO:0000313|EMBL:KJF69156.1, ECO:0000313|Proteomes:UP000052068}; RN [1] {ECO:0000313|EMBL:KJF69156.1, ECO:0000313|Proteomes:UP000052068} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=39/7 {ECO:0000313|EMBL:KJF69156.1, RC ECO:0000313|Proteomes:UP000052068}; RA Kuzmanovic N., Pulawska J., Obradovic A.; RT "Draft Genome Sequences of Agrobacterium nepotum Strain 39/7T (= CFBP 7436T RT = LMG 26435T) and Agrobacterium sp. Strain KFB 330 (= CFBP 8308 = LMG RT 28674)."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Has multiple catalytic activities. Apart from catalyzing the CC oxidation of (+)-tartrate to oxaloglycolate, also converts meso- CC tartrate to D-glycerate and catalyzes the oxidative decarboxylation of CC D-malate to pyruvate. {ECO:0000256|ARBA:ARBA00004033}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R,3R)-tartrate + H(+) = (R)-glycerate + CO2; CC Xref=Rhea:RHEA:13317, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:16659, ChEBI:CHEBI:30924; EC=4.1.1.73; CC Evidence={ECO:0000256|ARBA:ARBA00001421}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R,3R)-tartrate + NAD(+) = 2-hydroxy-3-oxosuccinate + H(+) + CC NADH; Xref=Rhea:RHEA:15209, ChEBI:CHEBI:15378, ChEBI:CHEBI:30924, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58265; EC=1.1.1.93; CC Evidence={ECO:0000256|ARBA:ARBA00001571}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R,3S)-tartrate + NAD(+) = 2-hydroxy-3-oxosuccinate + H(+) + CC NADH; Xref=Rhea:RHEA:16457, ChEBI:CHEBI:15378, ChEBI:CHEBI:30928, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58265; EC=1.1.1.93; CC Evidence={ECO:0000256|ARBA:ARBA00000818}; 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 -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + tartrate = 2-hydroxy-3-oxosuccinate + H(+) + NADH; CC Xref=Rhea:RHEA:18853, ChEBI:CHEBI:15378, ChEBI:CHEBI:30929, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58265; EC=1.1.1.93; CC Evidence={ECO:0000256|ARBA:ARBA00001276}; CC -!- PATHWAY: Carbohydrate acid metabolism; tartrate degradation; 2-hydroxy- CC 3-oxosuccinate from L-tartrate: step 1/1. CC {ECO:0000256|ARBA:ARBA00004981}. CC -!- PATHWAY: Carbohydrate acid metabolism; tartrate degradation; 2-hydroxy- CC 3-oxosuccinate from meso-tartrate: step 1/1. CC {ECO:0000256|ARBA:ARBA00005110}. CC -!- PATHWAY: Carbohydrate acid metabolism; tartrate degradation; D- CC glycerate from L-tartrate: step 1/1. {ECO:0000256|ARBA:ARBA00004803}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. 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:KJF69156.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JWJH01000003; KJF69156.1; -; Genomic_DNA. DR RefSeq; WP_045017608.1; NZ_JWJH01000003.1. DR STRING; 1368418.RS75_04090; -. DR EnsemblBacteria; KJF69156; KJF69156; RS75_04090. DR PATRIC; fig|1368418.3.peg.3116; -. DR UniPathway; UPA00839; UER00800. DR Proteomes; UP000052068; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:0050319; F:tartrate decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0009027; F:tartrate dehydrogenase activity; IEA:UniProtKB-EC. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR InterPro; IPR011829; TTC_DH. DR Pfam; PF00180; Iso_dh; 1. DR SMART; SM01329; Iso_dh; 1. DR TIGRFAMs; TIGR02089; TTC; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 3: Inferred from homology; KW Lyase {ECO:0000256|ARBA:ARBA00023239}. FT DOMAIN 5..342 FT /note="Iso_dh" FT /evidence="ECO:0000259|SMART:SM01329" SQ SEQUENCE 347 AA; 36961 MW; 8DD1BC0F5AA35678 CRC64; MKTHRIALIP GDGIGRSVTE AAWQVLNAAA KSSNFALEGT EFPWSCAFYK ETGAMMPKDG IETLRGFDAV MLGAVGWPAE VPDSVSLHGL LLPIRKAFVQ YANIRPHRLL PGVQGPLKSD GFDILCIREN TEGEYSGAGG RVHQGTGDEV AVETSIFTRK GVERILRFGF EQAQKRRGKL ASVTKSNAQK YSMVFWDEVT QKLADEYPDV EVSSYHIDAM AARMVMAPES LDVVVASNLF GDILTDLGAA IQGGLGFAAS ANINPDRSAP SMFEPVHGSA PDIAHLGIAN PIAAIWSGAM MFEHLGETDA AAKIMTALET ATGRGIGTVP GKDKTDTITA AILAALD //