ID   MDH_ACIAC               Reviewed;         328 AA.
AC   A1TP96;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-NOV-2008, entry version 16.
DE   RecName: Full=Malate dehydrogenase;
DE            EC=1.1.1.37;
GN   Name=mdh; OrderedLocusNames=Aave_2206;
OS   Acidovorax avenae subsp. citrulli (strain AAC00-1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D.,
RA   Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000512; ABM32784.1; -; Genomic_DNA.
DR   RefSeq; YP_970558.1; -.
DR   SMR; A1TP96; 3-328.
DR   GeneID; 4668190; -.
DR   GenomeReviews; CP000512_GR; Aave_2206.
DR   KEGG; aav:Aave_2206; -.
DR   NMPDR; fig|397945.5.peg.1904; -.
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_DHase.
DR   InterPro; IPR001236; Lactate/malate_DHase.
DR   InterPro; IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
DR   InterPro; IPR001252; Malate_DHase_AS.
DR   InterPro; IPR010945; Malate_DHase_SF1.
DR   InterPro; IPR016040; NAD(P)-bd.
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   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    328       Malate dehydrogenase.
FT                                /FTId=PRO_0000294370.
FT   NP_BIND      12     18       NAD (By similarity).
FT   NP_BIND     132    134       NAD (By similarity).
FT   ACT_SITE    190    190       Proton acceptor (By similarity).
FT   BINDING      95     95       Substrate (By similarity).
FT   BINDING     101    101       Substrate (By similarity).
FT   BINDING     108    108       NAD (By similarity).
FT   BINDING     115    115       NAD (By similarity).
FT   BINDING     134    134       Substrate (By similarity).
FT   BINDING     165    165       Substrate (By similarity).
SQ   SEQUENCE   328 AA;  34977 MW;  A6D2BC04ED5AD6E2 CRC64;
     MSKKPVRVAV TGAAGQIGYA LLFRIASGEM LGKDQPVILQ LLEIPDEKAQ KALKGVMMEL
     EDCAFPLLAG MEAHSDPMTA FKDTDYALLV GARPRGPGME RADLLAANAQ IFTAQGKALN
     AVASRNVKVL VVGNPANTNA YIAMKSAPDL PAKNFTAMLR LDHNRAASQI AAKTGGKVGE
     IEKLTVWGNH SPTMYADYRF ATIGGKSVKD AINDQVWNAD VFLPTVGKRG AAIIEARGLS
     SAASAANAAI DHMRDWALGS NGKWVTMGVP SKGEYGIPEG IVFGFPVITE NGEYKIVEGL
     EIDAFSQERI NKTLAELQGE QDGVKHLL
//