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Database: UniProt/SWISS-PROT
Entry: MDH_DEIRA
LinkDB: MDH_DEIRA
Original site: MDH_DEIRA 
ID   MDH_DEIRA               Reviewed;         330 AA.
AC   Q9RXI8;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   05-JUL-2017, entry version 113.
DE   RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517};
DE            EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517};
GN   Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517}; OrderedLocusNames=DR_0325;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 /
OS   LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus
RT   radiodurans R1.";
RL   Science 286:1571-1577(1999).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate. {ECO:0000255|HAMAP-Rule:MF_01517}.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC       {ECO:0000255|HAMAP-Rule:MF_01517}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01517}.
DR   EMBL; AE000513; AAF09906.1; -; Genomic_DNA.
DR   PIR; E75535; E75535.
DR   RefSeq; NP_294048.1; NC_001263.1.
DR   RefSeq; WP_010886970.1; NZ_CP015081.1.
DR   ProteinModelPortal; Q9RXI8; -.
DR   SMR; Q9RXI8; -.
DR   STRING; 243230.DR_0325; -.
DR   EnsemblBacteria; AAF09906; AAF09906; DR_0325.
DR   GeneID; 1798897; -.
DR   KEGG; dra:DR_0325; -.
DR   PATRIC; fig|243230.17.peg.491; -.
DR   eggNOG; ENOG4105D9Z; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000220953; -.
DR   InParanoid; Q9RXI8; -.
DR   KO; K00024; -.
DR   OMA; RPRTKGM; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR   GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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; IPR016040; NAD(P)-bd_dom.
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; NAD; Oxidoreductase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    330       Malate dehydrogenase.
FT                                /FTId=PRO_0000113368.
FT   NP_BIND      13     19       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   NP_BIND     131    133       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    189    189       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING      94     94       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     100    100       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     107    107       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   BINDING     114    114       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   BINDING     133    133       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     164    164       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
SQ   SEQUENCE   330 AA;  35148 MW;  2F9710386D3A2110 CRC64;
     MTMKQPVRVA VTGAAGQIGY SLLFRIAAGD MLGQDQPVIL QLLEITPALK ALNGVVMELR
     DGAFPLLADV ITSDDPMVAF KDADYALLVG AMPRKAGMER GDLLGANGGI FKPQGEALGA
     VASRNVKVLV VGNPANTNAL IAQQNAPDLD PKCFTAMVRL DHNRALSQLA EKTGAAVSDI
     KNVTIWGNHS STQYPDLSQA TVNGKPALEQ VDRTWYENDY IPTVAKRGAA IIEARGASSA
     ASAASAAIDH MHDWALGTKD GEWVSMGIPS DGSYGIPEGL IYGFPVRVKD GKYEIVQGLD
     VSDFSRGKMD ATAQELEEER DEVRKLGLVK
//
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