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 03-APR-2013, entry version 93.
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 -!- PTM: ISGylated (By similarity).
CC -!- PTM: Acetylation at Lys-118 dramatically enhances enzymatic
CC activity and promotes adipogenic differentiation (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 IPI; IPI00198717; -.
DR RefSeq; NP_150238.1; NM_033235.1.
DR UniGene; Rn.13492; -.
DR ProteinModelPortal; O88989; -.
DR SMR; O88989; 2-334.
DR IntAct; O88989; 1.
DR STRING; 10116.ENSRNOP00000011429; -.
DR PhosphoSite; O88989; -.
DR World-2DPAGE; 0004:O88989; -.
DR PaxDb; O88989; -.
DR PRIDE; O88989; -.
DR Ensembl; ENSRNOT00000011429; ENSRNOP00000011429; ENSRNOG00000008103.
DR GeneID; 24551; -.
DR KEGG; rno:24551; -.
DR UCSC; RGD:3072; rat.
DR CTD; 4190; -.
DR RGD; 3072; Mdh1.
DR eggNOG; COG0039; -.
DR GeneTree; ENSGT00530000063410; -.
DR HOGENOM; HOG000220953; -.
DR HOVERGEN; HBG006340; -.
DR InParanoid; O88989; -.
DR KO; K00025; -.
DR OrthoDB; EOG4CVG78; -.
DR NextBio; 603654; -.
DR Genevestigator; O88989; -.
DR GermOnline; ENSRNOG00000008103; Rattus norvegicus.
DR GO; GO:0005813; C:centrosome; IEA:Compara.
DR GO; GO:0005739; C:mitochondrion; IEA:Compara.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IDA:RGD.
DR GO; GO:0051287; F:NAD binding; IDA:RGD.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006108; P:malate metabolic process; IDA:RGD.
DR GO; GO:0006734; P:NADH metabolic process; IDA:RGD.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IDA:RGD.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; -; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
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_type2.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR PANTHER; PTHR23382; PTHR23382; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF56327; Lactate_DH/Glyco_hydro_4_C; 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; Complete proteome; Cytoplasm; Direct protein sequencing;
KW NAD; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Tricarboxylic acid cycle; Ubl conjugation.
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 118 118 N6-acetyllysine (By similarity).
FT MOD_RES 121 121 N6-acetyllysine (By similarity).
FT MOD_RES 210 210 Phosphotyrosine (By similarity).
FT MOD_RES 241 241 Phosphoserine (By similarity).
FT MOD_RES 298 298 N6-acetyllysine (By similarity).
FT MOD_RES 333 333 Phosphoserine (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
//
