ID F2I209_PELSM Unreviewed; 354 AA.
AC F2I209;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 OrderedLocusNames=SAR11G3_00013 {ECO:0000313|EMBL:AEA80488.1};
OS Pelagibacter sp. (strain IMCC9063).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae; Pelagibacter.
OX NCBI_TaxID=1002672 {ECO:0000313|EMBL:AEA80488.1, ECO:0000313|Proteomes:UP000009181};
RN [1] {ECO:0000313|EMBL:AEA80488.1, ECO:0000313|Proteomes:UP000009181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC9063 {ECO:0000313|EMBL:AEA80488.1,
RC ECO:0000313|Proteomes:UP000009181};
RX PubMed=21515764; DOI=10.1128/JB.05033-11;
RA Oh H.M., Kang I., Lee K., Jang Y., Lim S.I., Cho J.C.;
RT "Complete genome sequence of strain IMCC9063, belonging to SAR11 subgroup
RT 3, isolated from the Arctic Ocean.";
RL J. Bacteriol. 193:3379-3380(2011).
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; CP002511; AEA80488.1; -; Genomic_DNA.
DR RefSeq; WP_013694653.1; NC_015380.1.
DR AlphaFoldDB; F2I209; -.
DR STRING; 1002672.SAR11G3_00013; -.
DR KEGG; pel:SAR11G3_00013; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_0_1_5; -.
DR OrthoDB; 9767905at2; -.
DR UniPathway; UPA00839; UER00800.
DR Proteomes; UP000009181; 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 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 Lyase {ECO:0000313|EMBL:AEA80488.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Oxidoreductase {ECO:0000313|EMBL:AEA80488.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009181}.
FT DOMAIN 5..350
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 354 AA; 39336 MW; 72C94C13EDDBC8B7 CRC64;
MKEYKIASIA GDGIGKEVTP EGIRILKKVA EQHQFKIHFD EFDFASCDYH EKHGKMLPDN
WKDQIGKHDA IFFGAVGMPD QLPDHISLWG SLLKFRREFD QYINLRPVKL MPGVPCPLAN
KKPGDIDMLI VRENTEGEYS SVGGRMYKGT DREIAIQETI MSAQGIDRVM KYAFELAKTT
KRKKLTSATK SNGISITMPF WDERFKEMKT KYPDVKTDEF HIDILAARFV LTPEWFDVVV
ASNLFGDILS DLGPACTGTI GIAASANINP EKKFPSLFEP VHGSAPDIAG KGIANPIGQI
WSGAMMLDYL GEKEAADNIV KAIEKTLSNN ESRTKDLKGS SNTVQCADSV LANL
//
