ID A0A1G6WL55_9RHOB Unreviewed; 360 AA.
AC A0A1G6WL55;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=D-malate dehydrogenase [decarboxylating] {ECO:0000256|ARBA:ARBA00030902};
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=SAMN05421538_102164 {ECO:0000313|EMBL:SDD66541.1};
OS Paracoccus isoporae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=591205 {ECO:0000313|EMBL:SDD66541.1, ECO:0000313|Proteomes:UP000199344};
RN [1] {ECO:0000313|EMBL:SDD66541.1, ECO:0000313|Proteomes:UP000199344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22220 {ECO:0000313|EMBL:SDD66541.1,
RC ECO:0000313|Proteomes:UP000199344};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
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 -!- 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 -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR EMBL; FNAH01000002; SDD66541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6WL55; -.
DR STRING; 591205.SAMN05421538_102164; -.
DR OrthoDB; 9767905at2; -.
DR UniPathway; UPA00839; UER00800.
DR Proteomes; UP000199344; 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 GO; GO:0050319; F:tartrate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009027; F:tartrate dehydrogenase activity; IEA:UniProtKB-EC.
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:UP000199344}.
FT DOMAIN 7..351
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 360 AA; 38952 MW; 1124383534D72AE7 CRC64;
MSKKLHRIAA IGGDGIGVEV VDACLEALEV LAERDGGFAF EVENFDWSTA RYKETGAFMP
EDGADQLRGF DAILFGAVGA PDVPDHLTLW GLRLAICQPL DQYANVRPTR MLPGIQSPLR
GVDRDELDWV IVRENSEGEY AGQGGRSHPG LPLEVATDVS IFTRAGIERI MRFAFGLAQS
RPRKLLTVVT KSNAQRHGMV LWDEIAAEVA QEFPDVTWDK MLVDAMTVRM VMNPQSLDTI
VATNLHADIL SDLAAALSGS IGVAPTANLN PERDTPSMFE PIHGSAFDIT GKGVANPVAT
FWTAAMMLEH LGEQAASDRL IQAVETVTAN PDLHTPDLGG QASTRQVTDA VIEAIRGRND
//
