ID A0A1X9N9H3_9GAMM Unreviewed; 353 AA.
AC A0A1X9N9H3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN ORFNames=BST96_06710 {ECO:0000313|EMBL:ARN73831.1};
OS Oceanicoccus sagamiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Oceanicoccus.
OX NCBI_TaxID=716816 {ECO:0000313|EMBL:ARN73831.1, ECO:0000313|Proteomes:UP000193450};
RN [1] {ECO:0000313|EMBL:ARN73831.1, ECO:0000313|Proteomes:UP000193450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107125 {ECO:0000313|EMBL:ARN73831.1,
RC ECO:0000313|Proteomes:UP000193450};
RA Kumagai Y.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (NOV-2016) 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}.
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DR EMBL; CP019343; ARN73831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9N9H3; -.
DR STRING; 716816.BST96_06710; -.
DR KEGG; osg:BST96_06710; -.
DR OrthoDB; 9767905at2; -.
DR Proteomes; UP000193450; 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 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:UP000193450}.
FT DOMAIN 5..348
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 353 AA; 38897 MW; CEB1B682ADD1395A CRC64;
MIILKIAVIP GDGIGREVIP EGIRVLEQAG KIHGIEFHWT HFNWSCETYH QTGYMMPADA
IEQLRAFDAI YLGAVGFPGV PDHISLWGLL IPIRREFDQY INLRPVRLFE GVPCPLAGKK
PGDIDMIVVR ENVEGEYSNI GGIQYAGTEH EIVIQQSLLT RRGIDRVFKY AFELAQTRAA
KHVSSATKSN GIIHTMPFWD KRFAEMGKEY PAIKTDQYHI DIMTANFVLK PEHYDVVVGS
NLFGDILSDL GPAITGTIAI APSANINPEK NFPSMFEPVH GSAPDIAGQN IANPIGAVWA
GAMMLQHLGH HQAYNTIMAA IEEVLSESRN LTCDMGGQAS TQELGRAVAR AII
//
