ID   MDHG_ORYSJ              Reviewed;         356 AA.
AC   Q42972; Q2QLQ8; Q2QLQ9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 3.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=Malate dehydrogenase, glyoxysomal;
DE            EC=1.1.1.37;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os12g0632700, LOC_Os12g43630;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nipponbare;
RA   Kaminaka H., Morita S., Masumura T., Tanaka K.;
RT   "Molecular cloning and characterization of a cDNA encoding Glyoxysomal
RT   malate dehydrogenase from rice (Oryza sativa L.).";
RL   (er) Plant Gene Register PGR98-161.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease
RT   resistance genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [3]
RP   PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 37-43, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16758443; DOI=10.1002/pmic.200600043;
RA   Nozu Y., Tsugita A., Kamijo K.;
RT   "Proteomic analysis of rice leaf, stem and root tissues during growth
RT   course.";
RL   Proteomics 6:3665-3670(2006).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Glyoxysome.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABA99939.2; Type=Erroneous gene model prediction;
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DR   EMBL; D85763; BAA12870.1; -; mRNA.
DR   EMBL; DP000011; ABA99938.2; -; Genomic_DNA.
DR   EMBL; DP000011; ABA99939.2; ALT_SEQ; Genomic_DNA.
DR   PIR; T03272; T03272.
DR   RefSeq; NP_001067346.1; -.
DR   UniGene; Os.4155; -.
DR   HSSP; P00346; 1MLD.
DR   SMR; Q42972; 44-354.
DR   GeneID; 4352871; -.
DR   KEGG; osa:4352871; -.
DR   Gramene; Q42972; -.
DR   GO; GO:0009514; C:glyoxysome; 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:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
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; Glyoxylate bypass; Glyoxysome; NAD;
KW   Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     36       Glyoxysome.
FT   CHAIN        37    356       Malate dehydrogenase, glyoxysomal.
FT                                /FTId=PRO_0000018640.
FT   NP_BIND      51     57       NAD (By similarity).
FT   NP_BIND     160    162       NAD (By similarity).
FT   ACT_SITE    220    220       Proton acceptor (By similarity).
FT   BINDING      77     77       NAD (By similarity).
FT   BINDING     124    124       Substrate (By similarity).
FT   BINDING     130    130       Substrate (By similarity).
FT   BINDING     137    137       NAD (By similarity).
FT   BINDING     162    162       Substrate (By similarity).
FT   BINDING     196    196       Substrate (By similarity).
FT   BINDING     271    271       NAD (By similarity).
SQ   SEQUENCE   356 AA;  37385 MW;  D57BD93E93F381FB CRC64;
     MEDAAAAARR MERLASHLRP PASQMEESPL LRGSNCRAKG AAPGFKVAIL GASGGIGQPL
     ALLMKMNPLV SVLHLYDVVN TPGVTADISH MNTGAVVRGF LGQPQLENAL TGMDLVIIPA
     GVPRKPGMTR DDLFNINAGI VRTLCEGIAK CCPNAIVNVI SNPVNSTVPI AAEVFKKAGT
     YDPKRLLGVT TLDVVRANTF VAEVLGLDPR DVNVPVIGGH AGVTILPLLS QVNPPCSFTS
     EEISYLTTRI QNGGTEVVEA KAGAGSATLS MAYAASKFAD ACLRGLRGDA GIVECSFVAS
     QVTELPFFAS KVRLGRCGIE EILSLGPLNE FERAGLEKAK KELAESIQKG VAFINK
//