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Database: UniProt/SWISS-PROT
Entry: MDH_TERTT
LinkDB: MDH_TERTT
Original site: MDH_TERTT 
ID   MDH_TERTT               Reviewed;         327 AA.
AC   C5BU70;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   28-FEB-2018, entry version 60.
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=TERTU_1732;
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901;
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G.,
RA   Elshahawi S., Hanora A., Schmidt E.W., Haygood M.G., Posfai J.,
RA   Benner J., Madinger C., Nove J., Anton B., Chaudhary K., Foster J.,
RA   Holman A., Kumar S., Lessard P.A., Luyten Y.A., Slatko B., Wood N.,
RA   Wu B., Teplitski M., Mougous J.D., Ward N., Eisen J.A., Badger J.H.,
RA   Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an
RT   intracellular endosymbiont of marine wood-boring bivalves
RT   (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
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; CP001614; ACR13034.1; -; Genomic_DNA.
DR   RefSeq; WP_015819147.1; NC_012997.1.
DR   ProteinModelPortal; C5BU70; -.
DR   SMR; C5BU70; -.
DR   STRING; 377629.TERTU_1732; -.
DR   EnsemblBacteria; ACR13034; ACR13034; TERTU_1732.
DR   GeneID; 29650964; -.
DR   KEGG; ttu:TERTU_1732; -.
DR   eggNOG; ENOG4105D9Z; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000220953; -.
DR   KO; K00024; -.
DR   OMA; RPRTKGM; -.
DR   OrthoDB; POG091H03R4; -.
DR   BioCyc; TTUR377629:G1GVH-1557-MONOMER; -.
DR   Proteomes; UP000009080; 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   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; NAD; Oxidoreductase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    327       Malate dehydrogenase.
FT                                /FTId=PRO_1000215356.
FT   NP_BIND      11     17       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   NP_BIND     129    131       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    187    187       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING      92     92       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING      98     98       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     105    105       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   BINDING     112    112       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   BINDING     131    131       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     162    162       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
SQ   SEQUENCE   327 AA;  35192 MW;  A8E590EDDC10E023 CRC64;
     MKAPVRVTVT GAAGQISYSL LFRIAAGEML GADQPVILQM LEITPALEAL KGVAMELDDC
     AFPLLHSMVC TDDANVAFKD SDYALLVGAR PRGPGMERND LLEANAAIFS VQGKAINDHA
     SRGIKVLVVG NPANTNALIA QRNAPDIDPR QFTAMTRLDH NRGMSQLASK LDVSINDITK
     MTIWGNHSST QYPDLYHALV KGDAAIDKVD STWYAEEYIP TVQQRGAAII KARGASSAAS
     AANAAIFHMR DWALGSPEGD WVSMGVYSDG SYGIEKGLIY SFPCVCKNGD WEIVQGLSID
     EFSQARMTAT ETELQGERDA VKALLPA
//
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