ID   MDHC_MEDSA              Reviewed;         332 AA.
AC   O48905;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=Malate dehydrogenase, cytoplasmic;
DE            EC=1.1.1.37;
GN   Name=CMDH;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Trifolieae;
OC   Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Saranac; TISSUE=Root nodule;
RX   MEDLINE=98388648; PubMed=9721676;
RX   DOI=10.1046/j.1365-313X.1998.00192.x;
RA   Miller S.S., Driscoll B.T., Gregerson R.G., Gantt J.S., Vance C.P.;
RT   "Alfalfa malate dehydrogenase (MDH): molecular cloning and
RT   characterization of five different forms reveals a unique nodule-
RT   enhanced MDH.";
RL   Plant J. 15:173-184(1998).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
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DR   EMBL; AF020272; AAB99756.1; -; mRNA.
DR   PIR; T09291; T09291.
DR   HSSP; P11708; 4MDH.
DR   BRENDA; 1.1.1.37; 815.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:EC.
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:UniProtKB-KW.
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; IPR011274; Malate_DH_NAD-dep_euk.
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   TIGRFAMs; TIGR01758; MDH_euk_cyt; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN         1    332       Malate dehydrogenase, cytoplasmic.
FT                                /FTId=PRO_0000113416.
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   332 AA;  35547 MW;  D9F38F868DE3D628 CRC64;
     MAKDPVRVLV TGAAGQIGYA LVPMIARGVM LGPDQPVILH MLDIAPAAES LNGVKMELVD
     AAFPLLKGVV ATTDVVEACT GVNIAVMVGG FPRKEGMERK DVMSKNVSIY KSQASALEKH
     AAANCKVLVV ANPANTNALI LKEFAPSIPE RNISCLTRLD HNRALGQISE RLNVQVSDVK
     NVIIWGNHSS TQYPDVNHAT VNTPAGEKPV RQLVSDDAWL NGEFISTVQQ RGAAIIKARK
     LSSALSAASA ACDHIRDWVL GTPQGTFVSM GVYSDGSYNV PSGLIYSFPV TCANGEWKIV
     QGLSIDEFSR KKLDLTAEEL TEEKNLAHSC LS
//