ID   MDHM_CAEEL              Reviewed;         341 AA.
AC   O02640;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   16-JUN-2009, entry version 68.
DE   RecName: Full=Probable malate dehydrogenase, mitochondrial;
DE            EC=1.1.1.37;
DE   Flags: Precursor;
GN   Name=mdh-1; ORFNames=F20H11.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (Potential).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
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DR   EMBL; AF002197; AAB53985.1; -; Genomic_DNA.
DR   PIR; C88486; C88486.
DR   RefSeq; NP_498457.1; -.
DR   UniGene; Cel.5076; -.
DR   HSSP; P00346; 1MLD.
DR   Ensembl; F20H11.3; Caenorhabditis elegans.
DR   GeneID; 175936; -.
DR   KEGG; cel:F20H11.3; -.
DR   WormBase; WBGene00003162; mdh-1.
DR   WormPep; F20H11.3; CE09512.
DR   OMA; O02640; TNSYEDI.
DR   BRENDA; 1.1.1.37; 672.
DR   NextBio; 890380; -.
DR   ArrayExpress; O02640; -.
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:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase.
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:0040010; P:positive regulation of growth rate; IMP:WormBase.
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   2: Evidence at transcript level;
KW   Complete proteome; Mitochondrion; NAD; Oxidoreductase;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1      ?       Mitochondrion.
FT   CHAIN         ?    341       Probable malate dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000018632.
FT   NP_BIND      35     41       NAD (By similarity).
FT   NP_BIND     144    146       NAD (By similarity).
FT   ACT_SITE    204    204       Proton acceptor (By similarity).
FT   BINDING      61     61       NAD (By similarity).
FT   BINDING     108    108       Substrate (By similarity).
FT   BINDING     114    114       Substrate (By similarity).
FT   BINDING     121    121       NAD (By similarity).
FT   BINDING     146    146       Substrate (By similarity).
FT   BINDING     180    180       Substrate (By similarity).
FT   BINDING     255    255       NAD (By similarity).
SQ   SEQUENCE   341 AA;  35120 MW;  7515F9C1727AEFB5 CRC64;
     MSLPAKTLVQ AAANSGLRAV SVRHSSQAPK VALLGAAGGI GQPLGLLLKQ DPLVAHLALY
     DVVNTPGVAA DLSHIDSNAK VTAHTGPKEL YAAVENADVI VIPAGVPRKP GMTRDDLFNT
     NAGIVRDLAA VIAKASPKAL IAIITNPVNS TVPIASEVLK KAGVYDPKRV FGVTTLDVVR
     SQAFVSELKG HDASKTVVPV VGGHAGITII PLLSQVKPST KFSEEEISKL TPRIQDAGTE
     VVNAKAGAGS ATLSMALAGA RFANALVRGI KGEKNVQCAY VASDAVKGVE YFSTPVELGP
     NGVEKILGVG KVSAYEQKLI DASVPELNKN IAKGVAFVKG N
//