ID   MDHM_CITLA              Reviewed;         347 AA.
AC   P17783;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   16-JUN-2009, entry version 71.
DE   RecName: Full=Malate dehydrogenase, mitochondrial;
DE            EC=1.1.1.37;
DE   Flags: Precursor;
GN   Name=MMDH;
OS   Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Cucurbitales; Cucurbitaceae; Citrullus.
OX   NCBI_TaxID=3654;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Sugar Baby; TISSUE=Cotyledon;
RX   MEDLINE=91346686; PubMed=2102869; DOI=10.1007/BF00019398;
RA   Gietl C., Lehnerer M., Olsen O.;
RT   "Mitochondrial malate dehydrogenase from watermelon: sequence of cDNA
RT   clones and primary structure of the higher-plant precursor protein.";
RL   Plant Mol. Biol. 14:1019-1030(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 28-55.
RA   Gietl C., Lottspeich F., Hock B.;
RT   "Sequence homologies between glyoxysomal and mitochondrial malate
RT   dehydrogenase.";
RL   Planta 169:555-558(1986).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
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DR   EMBL; X17362; CAA35239.1; -; mRNA.
DR   PIR; S10162; DEPUMW.
DR   HSSP; P00346; 1MLD.
DR   BRENDA; 1.1.1.37; 81664.
DR   GO; GO:0005759; C:mitochondrial matrix; 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; IPR010097; Malate_DH_NAD-dep_euk_g_bac.
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; PTHR11540:SF1; MDH_euk_g_bac; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     27       Mitochondrion.
FT   CHAIN        28    347       Malate dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000018625.
FT   NP_BIND      41     47       NAD (By similarity).
FT   NP_BIND     150    152       NAD (By similarity).
FT   ACT_SITE    210    210       Proton acceptor (By similarity).
FT   BINDING      67     67       NAD (By similarity).
FT   BINDING     114    114       Substrate (By similarity).
FT   BINDING     120    120       Substrate (By similarity).
FT   BINDING     127    127       NAD (By similarity).
FT   BINDING     152    152       Substrate (By similarity).
FT   BINDING     186    186       Substrate (By similarity).
FT   BINDING     261    261       NAD (By similarity).
SQ   SEQUENCE   347 AA;  36201 MW;  31474F15018D30CC CRC64;
     MKASILRSVR SAVSRSSSSN RLLSRSFATE SVPERKVAVL GAAGGIGQPL ALLMKLNPLV
     SKLALYDIAG TPGVAADVGH VNTRSEVTGY VGEEQLGKAL EGSDVVIIPA GVPRKPGMTR
     DDLFNINAGI VKSLCTAIAK YCPNALINMI SNPVNSTVPI AAEVFKKAGT YDEKKLFGVT
     TLDVVRAKTF YAGKANVPVA EVNVPVIGGH AGITILPLFS QATPRANLSD DTIVALTKRT
     QDGGTEVVEA KAGKGSATLS MAYAGALFAD ACLKGLNGVP DVVECSFVQS TVTELPFFAS
     KVKLGKNGVE SVLDLGPLSD FEKEGLEKLK PELKASIEKG IQFANAN
//