ID   MDHC_RAT                Reviewed;         334 AA.
AC   O88989; O88585; Q6PCV2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-DEC-2008, entry version 56.
DE   RecName: Full=Malate dehydrogenase, cytoplasmic;
DE            EC=1.1.1.37;
DE   AltName: Full=Cytosolic malate dehydrogenase;
GN   Name=Mdh1; Synonyms=Mdh;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Achenbach P., Steinbrenner H., Reindl G., Seissler J.;
RT   "Cloning of rat cytosolic malate dehydrogenase.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 7-32; 80-92; 126-157; 171-199; 206-230; 239-255;
RP   299-310 AND 319-334, AND MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 251-284.
RA   Earley S.;
RT   "Partial sequence of rat malate dehydrogenase (MDH) mRNA.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
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; AF093773; AAC64180.1; -; mRNA.
DR   EMBL; BC059124; AAH59124.1; -; mRNA.
DR   EMBL; AF075574; AAC26799.1; -; mRNA.
DR   RefSeq; NP_150238.1; -.
DR   UniGene; Rn.13492; -.
DR   HSSP; P11708; 4MDH.
DR   SMR; O88989; 1-333, 2-334.
DR   PhosphoSite; O88989; -.
DR   PRIDE; O88989; -.
DR   Ensembl; ENSRNOG00000008103; Rattus norvegicus.
DR   GeneID; 24551; -.
DR   KEGG; rno:24551; -.
DR   NMPDR; fig|10116.3.peg.10844; -.
DR   RGD; 3072; Mdh1.
DR   HOVERGEN; O88989; -.
DR   NextBio; 603654; -.
DR   ArrayExpress; O88989; -.
DR   GermOnline; ENSRNOG00000008103; Rattus norvegicus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:InterPro.
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_DHase.
DR   InterPro; IPR001236; Lactate/malate_DHase.
DR   InterPro; IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
DR   InterPro; IPR001252; Malate_DHase_AS.
DR   InterPro; IPR011274; Malate_DHase_NAD-dep_euk.
DR   InterPro; IPR010945; Malate_DHase_SF1.
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   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   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; NAD;
KW   Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    334       Malate dehydrogenase, cytoplasmic.
FT                                /FTId=PRO_0000226737.
FT   NP_BIND      11     17       NAD (By similarity).
FT   NP_BIND     129    131       NAD (By similarity).
FT   ACT_SITE    187    187       Proton acceptor (By similarity).
FT   BINDING      92     92       Substrate (By similarity).
FT   BINDING      98     98       Substrate (By similarity).
FT   BINDING     105    105       NAD (By similarity).
FT   BINDING     112    112       NAD (By similarity).
FT   BINDING     131    131       Substrate (By similarity).
FT   BINDING     162    162       Substrate (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     210    210       Phosphotyrosine (By similarity).
FT   CONFLICT    251    251       S -> A (in Ref. 4; AAC26799).
FT   CONFLICT    276    276       N -> D (in Ref. 2; AAH59124).
SQ   SEQUENCE   334 AA;  36483 MW;  8F6778722A607B3C CRC64;
     MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL DGVLMELQDC
     ALPLLQDVIA TDKEEVAFKD LDVAVLVGSM PRREGMERKD LLKANVKIFK SQGAALEKYA
     KKSVKVIVVG NPANTNCLTA SKSAPSIPKE NFSCLTRLDH NRAKSQIALK LGVTADDVKN
     VIIWGNHSST QYPDVNHAKV KLQGKEVGVY EALKDDSWLK GEFITTVQQR GAAVIKARKL
     SSAMSAAKAI SDHIRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV
     EGLPINDFSR EKMDLTAKEL TEEKETAFEF LSSA
//