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Database: UniProt/TrEMBL
Entry: A0A160DWN3_9GAMM
LinkDB: A0A160DWN3_9GAMM
Original site: A0A160DWN3_9GAMM 
ID   A0A160DWN3_9GAMM        Unreviewed;       328 AA.
AC   A0A160DWN3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-NOV-2017, entry version 14.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|SAAS:SAAS00369716};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|SAAS:SAAS00369716};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN   ORFNames=I596_3073 {ECO:0000313|EMBL:ANB19065.1};
OS   Dokdonella koreensis DS-123.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dokdonella.
OX   NCBI_TaxID=1300342 {ECO:0000313|EMBL:ANB19065.1, ECO:0000313|Proteomes:UP000076830};
RN   [1] {ECO:0000313|EMBL:ANB19065.1, ECO:0000313|Proteomes:UP000076830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-123 {ECO:0000313|EMBL:ANB19065.1,
RC   ECO:0000313|Proteomes:UP000076830};
RA   Kim J.F., Lee H., Kwak M.-J.;
RT   "Complete genome sequence of Dokdonella koreensis DS-123T.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate. {ECO:0000256|HAMAP-Rule:MF_01517,
CC       ECO:0000256|SAAS:SAAS00755561}.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC       {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|SAAS:SAAS00369698}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01517}.
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DR   EMBL; CP015249; ANB19065.1; -; Genomic_DNA.
DR   RefSeq; WP_067649399.1; NZ_CP015249.1.
DR   EnsemblBacteria; ANB19065; ANB19065; I596_3073.
DR   KEGG; dko:I596_3073; -.
DR   PATRIC; fig|1300342.3.peg.3000; -.
DR   KO; K00024; -.
DR   Proteomes; UP000076830; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_01517; Malate_dehydrog_2; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23382; PTHR23382; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000076830};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076830};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   DOMAIN        5    146       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      157    321       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND      11     17       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   NP_BIND     129    131       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    187    187       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                1}.
FT   BINDING      92     92       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING      98     98       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING     105    105       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     112    112       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     131    131       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
SQ   SEQUENCE   328 AA;  35105 MW;  26B015369EAFB696 CRC64;
     MKAPVRVAVT GAAGQIGYAL LFRIAAGDML GPDQPVILHL LEITPALPAL NGVVMELNDC
     AFPTLHGVVA TDDVNVAFKD VDFALLVGAR PRGPGMERKD LLEANGAIFA PQGKAINDHA
     KRDVRVLVVG NPANTNALIA QQNAPDLDPR RFTAMVRLDH NRAISQLAEK TGALNTDIAK
     VTIWGNHSST QYPDIHQTTV KGKPALSLVD QTWYENDFIP VVQQRGAAII KARGASSAAS
     AASAAIDHMR NWALGTAAGD WVSMGIPSDG SYGIEPGVIY GYPVTVSNGS YEIVQGLEIN
     AFSRARMDAT DRELREERAA VEHLFAKR
//
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