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MDHG2_BRANA
ID   MDHG2_BRANA             Reviewed;         358 AA.
AC   Q9XFW3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Malate dehydrogenase 2, glyoxysomal;
DE            EC=1.1.1.37;
DE   Flags: Precursor;
GN   Name=MDH2;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Imhoff U., Voetz M., Wingender R., Schnabl H., Wolf N.;
RT   "Two genes encoding microbody malate dehydrogenase from Brassica napus.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10004};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Glyoxysome.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ242713; CAB43995.1; -; Genomic_DNA.
DR   RefSeq; XP_013678502.1; XM_013823048.1.
DR   RefSeq; XP_013678503.1; XM_013823049.1.
DR   AlphaFoldDB; Q9XFW3; -.
DR   SMR; Q9XFW3; -.
DR   PRIDE; Q9XFW3; -.
DR   GeneID; 106382950; -.
DR   KEGG; bna:106382950; -.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd01337; MDH_glyoxysomal_mitochondrial; 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; IPR010097; Malate_DH_type1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   Glyoxylate bypass; Glyoxysome; NAD; Oxidoreductase; Peroxisome;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..38
FT                   /note="Glyoxysome"
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..358
FT                   /note="Malate dehydrogenase 2, glyoxysomal"
FT                   /id="PRO_0000018637"
FT   ACT_SITE        222
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00346"
FT   BINDING         53..59
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P40926"
FT   BINDING         79
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P40926"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         139
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P40926"
FT   BINDING         162..164
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P40926"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         273
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P40926"
SQ   SEQUENCE   358 AA;  37725 MW;  B73B2CB3DC1D2877 CRC64;
     MEFRGDANKR IAMISAHLQP SFTPQMEAKN SVMGRENCRA KGGNPGFKVA ILGAAGGIGQ
     SLSLLMKMNP LVSLLHLYDV VNAPGVTADV SHMDTGAVVR GFLGAKQLED ALTGMDLVII
     PAGVPRKPGM TRDDLFKINA GIVKTLCEGV AKCCPNAIVN LISNPVNSTV AIAAEVFKKA
     GTYDPKKLLG VTTLDVARAN TFVAEVLGLD PREVDVPVVG GHAGVTILPL LSQVKPPSSF
     TPSEIEYLTN RIQNGGTEVV EAKAGAGSAT LSMAYAAAKF ADACLRGLRG DANVIECSFV
     ASQVTELAFF ATKVRLGRTG AEEVFQLGPL NEYERVGLEK AKEELAGSIQ KGVDFIRK
 
 
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