ID   MDH1_ANADE              Reviewed;         312 AA.
AC   Q2IIC2;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-NOV-2008, entry version 24.
DE   RecName: Full=Malate dehydrogenase 1;
DE            EC=1.1.1.37;
GN   Name=mdh1; OrderedLocusNames=Adeh_1626;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-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   -!- 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; CP000251; ABC81399.1; -; Genomic_DNA.
DR   RefSeq; YP_464836.1; -.
DR   GeneID; 3888125; -.
DR   GenomeReviews; CP000251_GR; Adeh_1626.
DR   KEGG; ade:Adeh_1626; -.
DR   HOGENOM; Q2IIC2; -.
DR   BioCyc; ADEH290397:ADEH_1626-MON; -.
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_DHase.
DR   InterPro; IPR001236; Lactate/malate_DHase.
DR   InterPro; IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
DR   InterPro; IPR011275; Malate_DHase_NAD-dep_bac.
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   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    312       Malate dehydrogenase 1.
FT                                /FTId=PRO_0000241939.
FT   NP_BIND      11     16       NAD (By similarity).
FT   NP_BIND     122    124       NAD (By similarity).
FT   ACT_SITE    179    179       Proton acceptor (By similarity).
FT   BINDING      35     35       NAD (By similarity).
FT   BINDING      86     86       Substrate (By similarity).
FT   BINDING      92     92       Substrate (By similarity).
FT   BINDING      99     99       NAD (By similarity).
FT   BINDING     124    124       Substrate (By similarity).
FT   BINDING     155    155       Substrate (By similarity).
SQ   SEQUENCE   312 AA;  32915 MW;  EC486A2D26D3E1CC CRC64;
     MAQRKKIALI GAGQIGGTLA LLAGQKELGD VVLVDIMEGV AKGKALDLQE TRGVGKWDVD
     VTGGGTTDYS VIRDADVCIV TAGVPRKPGM SREDLLKVNL DAITKVAHGI KQYAPNAFVI
     VITNPLDSMV YAMYKVTGFP KNRVVGMAGV LDTARFQYFV GDAAGVSPQD VQAMVLGGHG
     DDMVPLLRYS SVAGVPLTRL LDKAKLDAIV ERTRKGGGEI VALLGTGSAF YAPAASAIAM
     AESYLRDKKR VLPCSALLEG QYGVKGLFVG VPVVIGAGGV ERVLELELND DERAMLQRSV
     DSVKKSVAET KL
//