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Database: UniProt/SWISS-PROT
Entry: MDH_DEIGD
LinkDB: MDH_DEIGD
Original site: MDH_DEIGD 
ID   MDH_DEIGD               Reviewed;         334 AA.
AC   Q1IWC9;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   07-JUN-2017, entry version 83.
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};
GN   OrderedLocusNames=Dgeo_2161;
OS   Deinococcus geothermalis (strain DSM 11300).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K.,
RA   Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM
RT   11300.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000359; ABF46455.1; -; Genomic_DNA.
DR   RefSeq; WP_011531280.1; NC_008025.1.
DR   ProteinModelPortal; Q1IWC9; -.
DR   SMR; Q1IWC9; -.
DR   STRING; 319795.Dgeo_2161; -.
DR   PRIDE; Q1IWC9; -.
DR   EnsemblBacteria; ABF46455; ABF46455; Dgeo_2161.
DR   KEGG; dge:Dgeo_2161; -.
DR   eggNOG; ENOG4105D9Z; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000220953; -.
DR   KO; K00024; -.
DR   OMA; RPRTKGM; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000002431; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
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-KW.
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    334       Malate dehydrogenase.
FT                                /FTId=PRO_0000292372.
FT   NP_BIND      17     23       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   NP_BIND     135    137       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    193    193       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING      98     98       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     104    104       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     111    111       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   BINDING     118    118       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   BINDING     137    137       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     168    168       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
SQ   SEQUENCE   334 AA;  35928 MW;  E011483F19313371 CRC64;
     MTMNQGTKQP VRVAVTGAAG QIGYSLLFRI AAGDMLGKDQ PVILQLLEIT PALKALAGVV
     MELRDCAFPL LADIVTSDDP LVAFKDADYA LLVGAMPRKA GMERGDLLGA NGGIFKPQGE
     ALNKVASRDV KVLVVGNPAN TNALIAQQNA PDLDPKQFTA MVRLDHNRAI SQLAEKTGQP
     VSAIKNITIW GNHSSTQYPD LSQATVNGQP ALDLVDREWY EKEYIPTVAK RGAAIIEARG
     ASSAASAASA AIDHMRDWAL GTPEGEWVSM AVPSDGSYGI PEGLIYGFPV RCRNGQYEIV
     QGLEISDFSR QKMDATAKEL EEEREEVRRL GLVK
//
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