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Database: UniProt
Entry: S7QD62_MYOBR
LinkDB: S7QD62_MYOBR
Original site: S7QD62_MYOBR 
ID   S7QD62_MYOBR            Unreviewed;       352 AA.
AC   S7QD62;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|RuleBase:RU003405};
DE            EC=1.1.1.37 {ECO:0000256|RuleBase:RU003405};
GN   ORFNames=D623_10034288 {ECO:0000313|EMBL:EPQ19142.1};
OS   Myotis brandtii (Brandt's bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ19142.1, ECO:0000313|Proteomes:UP000052978};
RN   [1] {ECO:0000313|Proteomes:UP000052978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23962925; DOI=10.1038/ncomms3212;
RA   Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA   Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA   Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA   Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA   Krogh A., Wang J., Gladyshev V.N.;
RT   "Genome analysis reveals insights into physiology and longevity of the
RT   Brandt's bat Myotis brandtii.";
RL   Nat. Commun. 4:2212-2212(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD(+) = 3-(4-
CC         hydroxyphenyl)pyruvate + H(+) + NADH; Xref=Rhea:RHEA:10780,
CC         ChEBI:CHEBI:10980, ChEBI:CHEBI:15378, ChEBI:CHEBI:36242,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.96;
CC         Evidence={ECO:0000256|ARBA:ARBA00034226};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10782;
CC         Evidence={ECO:0000256|ARBA:ARBA00034226};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) +
CC         NADH; Xref=Rhea:RHEA:57172, ChEBI:CHEBI:15378, ChEBI:CHEBI:16782,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000256|ARBA:ARBA00036471};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:57174;
CC         Evidence={ECO:0000256|ARBA:ARBA00036471};
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:0000256|ARBA:ARBA00034254};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21433;
CC         Evidence={ECO:0000256|ARBA:ARBA00034254};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21434;
CC         Evidence={ECO:0000256|ARBA:ARBA00034254};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|ARBA:ARBA00009613}.
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DR   EMBL; KE164608; EPQ19142.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7QD62; -.
DR   eggNOG; KOG1496; Eukaryota.
DR   Proteomes; UP000052978; Unassembled WGS sequence.
DR   GO; GO:0047995; F:hydroxyphenylpyruvate reductase activity; IEA:RHEA.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd01336; MDH_cytoplasmic_cytosolic; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_01517; Malate_dehydrog_2; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR   NCBIfam; TIGR01758; MDH_euk_cyt; 1.
DR   PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23382:SF3; MALATE DEHYDROGENASE, CYTOPLASMIC; 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; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU003405}.
FT   DOMAIN          23..170
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          174..348
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        205
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         60
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         123
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         147..149
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   352 AA;  38660 MW;  000DF94CE9E7B055 CRC64;
     MQVWRHFKVL ELSAQFPIMP EPVRVLVTGA AGQIAYSLLY SIGNGSVFGK DQPIILVLLD
     ITPMMGVLDG VLMELQDCAL PLLKDVIATD KEEVAFKDLD VAVLVGSMPR RDGMERKDLL
     KANVKIFKSQ GAALDKYAKK SVKVIVVGNP ANTNCLTASK SAPSIPKENF SCLTRLDHNR
     AKAQIALKLG VTSEDVKNVI IWGNHSSTQY PDVNHAKVKL QGKEVGVYEA LKNDSWLKGE
     FITTVQQRGA AVIKARKLSS AMSAAKAICD HIRDIWFGTP EGEFVSMGII SDGNSYGVPD
     DLLYSFPVTI KNKTWKIVEG LPINDFSREK MDLTAKELSE EKETAFEFLS SA
//
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