ID   MDH_AZOSB               Reviewed;         330 AA.
AC   A1K5Q9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 16.
DE   RecName: Full=Malate dehydrogenase;
DE            EC=1.1.1.37;
GN   Name=mdh; OrderedLocusNames=azo1547;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Azoarcus.
OX   NCBI_TaxID=62928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte
RT   Azoarcus sp. strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(2006).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate (By similarity).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
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DR   EMBL; AM406670; CAL94164.1; -; Genomic_DNA.
DR   RefSeq; YP_933051.1; -.
DR   SMR; A1K5Q9; 3-330.
DR   GeneID; 4608485; -.
DR   GenomeReviews; AM406670_GR; azo1547.
DR   KEGG; azo:azo1547; -.
DR   OMA; A1K5Q9; MIIWGNH.
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_01517; -; 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; IPR001252; Malate_DH_AS.
DR   InterPro; IPR010945; Malate_DH_SF1.
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   PANTHER; PTHR23382; MDH_SF1; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   ProDom; PD003052; Mal_dehydrog; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR   PROSITE; PS00068; MDH; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN         1    330       Malate dehydrogenase.
FT                                /FTId=PRO_0000294374.
FT   NP_BIND      12     18       NAD (By similarity).
FT   NP_BIND     130    132       NAD (By similarity).
FT   ACT_SITE    191    191       Proton acceptor (By similarity).
FT   BINDING      93     93       Substrate (By similarity).
FT   BINDING      99     99       Substrate (By similarity).
FT   BINDING     106    106       NAD (By similarity).
FT   BINDING     113    113       NAD (By similarity).
FT   BINDING     132    132       Substrate (By similarity).
FT   BINDING     166    166       Substrate (By similarity).
SQ   SEQUENCE   330 AA;  35527 MW;  DEC4AA51D738E299 CRC64;
     MSKAPVRVAV TGAAGQIGYS LLFRIASGEM LGKDQPVILQ LLDLPQAQKA VKGVMMELED
     CAFPLLAGMI ATDDPNVAFK DAKVALLVGA RPRGPGMERK DLLTENAKIF TVQGAAIGQY
     ADPDCKVLVV GNPCNTNAYI AKEVAQKYGR VPAKNFTGML RLDHNRALSQ LAGKSGREVS
     SLKNLVVWGN HSPTMYADYR FVKSNGDSVK DLINDAAWNK DVFLPTVGKR GAAIIEARGL
     SSAASAANAA IDHIRDWVLG SNGEWVTMGI PSDGSYGIPE GVIYGFPVTT ENGEYKIVQG
     LEIDEFSRER MTVTLNELLE EREGVKDLLA
//