ID W1SC19_9SPHN Unreviewed; 355 AA.
AC W1SC19;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=C100_06350 {ECO:0000313|EMBL:ETI64663.1};
OS Sphingobium sp. C100.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1207055 {ECO:0000313|EMBL:ETI64663.1, ECO:0000313|Proteomes:UP000018867};
RN [1] {ECO:0000313|EMBL:ETI64663.1, ECO:0000313|Proteomes:UP000018867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C100 {ECO:0000313|EMBL:ETI64663.1,
RC ECO:0000313|Proteomes:UP000018867};
RX PubMed=24482512;
RA Dong C., Bai X., Lai Q., Xie Y., Chen X., Shao Z.;
RT "Draft Genome Sequence of Sphingobium sp. Strain C100, a Polycyclic
RT Aromatic Hydrocarbon-Degrading Bacterium from the Deep-Sea Sediment of the
RT Arctic Ocean.";
RL Genome Announc. 2:0-0(2014).
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}.
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:ETI64663.1}.
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DR EMBL; AYOY01000079; ETI64663.1; -; Genomic_DNA.
DR RefSeq; WP_008828091.1; NZ_AYOY01000079.1.
DR AlphaFoldDB; W1SC19; -.
DR STRING; 1207055.C100_06350; -.
DR PATRIC; fig|1207055.3.peg.1196; -.
DR eggNOG; COG0473; Bacteria.
DR OrthoDB; 9767905at2; -.
DR UniPathway; UPA00839; UER00800.
DR Proteomes; UP000018867; 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:UP000018867}.
FT DOMAIN 5..348
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 355 AA; 38661 MW; 8BCA1C220AD55369 CRC64;
MRRYSIASIP GDGIGREVVP AAIAVLTAAA AKCGFVLEFR HFDWSCQTYL KTGKMMPDDG
LDRLRDHDAV FLGAVGFPGV PDHISLWGLL LPIRREFEQY VNLRPVRLLP GIASPLRDKA
RGDIDFWVVR ENSEGEYSQI GGRTGTGENE IVVQQAIFTR RGTDRILRYA FDFARRSGRR
HVTSATKSNG LYHSMPFWDE RFAAIGAEYP DVAADQYHVD ILAARFVMSP ERFNVVVGSN
LFGDILSDLG PGITGTIAVA PSANLNPERR FPSMFEPVHG SAPDIAGQGI ANPIGQIWSG
AMMLEHLGET EPAALVMRAL ETALIAPDIA RTPDLGGNGT TAGFAQAVRN TLLGL
//
