ID   MDH_ACICJ               Reviewed;         327 AA.
AC   A5G320;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-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=Acry_3063;
OS   Acidiphilium cryptum (strain JF-5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=349163;
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., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) 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; CP000697; ABQ32252.1; -; Genomic_DNA.
DR   RefSeq; YP_001236171.1; -.
DR   GeneID; 5161153; -.
DR   GenomeReviews; CP000697_GR; Acry_3063.
DR   KEGG; acr:Acry_3063; -.
DR   OMA; A5G320; 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    327       Malate dehydrogenase.
FT                                /FTId=PRO_1000068598.
FT   NP_BIND      12     18       NAD (By similarity).
FT   NP_BIND     130    132       NAD (By similarity).
FT   ACT_SITE    188    188       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     163    163       Substrate (By similarity).
SQ   SEQUENCE   327 AA;  34474 MW;  F60BC6BF6DD37EFB CRC64;
     MAKSPVRIAV TGAAGQIAYA LVFRIASGAL LGPDQPVILH LLDLPQMQGA LGGVMMELED
     CAFPLLAGMV ATDDPKVAFK DIDIGFLVGA RPRGKGMERK DLLGANAEIF TVQGRALNEV
     AKRSARVLVV GNPANTNAYI AMKSAPDLSP DCFSAMIRLD HNRAASMLAA KAGVNVGDVG
     KLIVWGNHSP TMYPDYRFAE AGGRKLAEAI NDEAWNRDVF IPTVGKRGAA VIEARGASSA
     ASAANAAIDQ VRDWVVGSDG RWVSMAIPSD GSYGIPEGIM FGVPVTTQGG VVTRVPNLAI
     DAFAQSRLDI TLNELKEERE AIAHLLA
//