ID   MDH_AGRT5               Reviewed;         320 AA.
AC   Q7CWK7; Q8UC59;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=Malate dehydrogenase;
DE            EC=1.1.1.37;
GN   Name=mdh; OrderedLocusNames=Atu2639; ORFNames=AGR_C_4782;
OS   Agrobacterium tumefaciens (strain C58 / ATCC 33970).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21608550; PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P.,
RA   Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L.,
RA   Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr.,
RA   Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C.,
RA   Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A.,
RA   Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D.,
RA   Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M.,
RA   Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M.,
RA   Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V.,
RA   Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21608551; PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M.,
RA   Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L.,
RA   Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F.,
RA   Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B.,
RA   Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G.,
RA   Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate (By similarity).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE007869; AAK88360.2; -; Genomic_DNA.
DR   PIR; AF2900; AF2900.
DR   PIR; G97675; G97675.
DR   RefSeq; NP_355575.2; -.
DR   HSSP; P80040; 1GUY.
DR   GeneID; 1134677; -.
DR   GenomeReviews; AE007869_GR; Atu2639.
DR   KEGG; atc:AGR_C_4782; -.
DR   KEGG; atu:Atu2639; -.
DR   HOGENOM; Q7CWK7; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP.
DR   HAMAP; MF_00487; -; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR001236; Lactate/malate_DH.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR011275; Malate_DH_NAD-dep_bac.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   TIGRFAMs; TIGR01763; MalateDH_bact; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN         1    320       Malate dehydrogenase.
FT                                /FTId=PRO_0000113419.
FT   NP_BIND      10     15       NAD (By similarity).
FT   NP_BIND     119    121       NAD (By similarity).
FT   ACT_SITE    176    176       Proton acceptor (By similarity).
FT   BINDING      34     34       NAD (By similarity).
FT   BINDING      83     83       Substrate (By similarity).
FT   BINDING      89     89       Substrate (By similarity).
FT   BINDING      96     96       NAD (By similarity).
FT   BINDING     121    121       Substrate (By similarity).
FT   BINDING     152    152       Substrate (By similarity).
SQ   SEQUENCE   320 AA;  33537 MW;  3073A7C3BC0FCE5E CRC64;
     MARKKIALIG SGMIGGTLAH LASLKELGDI VLFDIADGIP QGKGLDIAQS GPVEGFNAKL
     SGASDYAAIE GADVCIVTAG VARKPGMSRD DLLGINLKVM EQVGAGIKKY APNAFVICIT
     NPLDAMVWAL QKFSGLPKNK VVGMAGVLDS ARFRLFLAEE FNVSVQDVTA FVLGGHGDTM
     VPLARYSTVG GVPLTDLVKM GWLTAERLEQ IIQRTRDGGA EIVGLLKTGS AYYAPAASAI
     EMAESYLKDK KRVLPAAAHL SGQYGVDDMY VGVPTIIGAG GIERVIEIEL NKEEEAAFQK
     SVGAVAGLCE ACINIAPSLK
//