ID L9KSD1_TUPCH Unreviewed; 219 AA.
AC L9KSD1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Malate dehydrogenase, cytoplasmic {ECO:0000256|ARBA:ARBA00019899};
DE EC=1.1.1.96 {ECO:0000256|ARBA:ARBA00034331};
DE AltName: Full=Aromatic alpha-keto acid reductase {ECO:0000256|ARBA:ARBA00034373};
DE AltName: Full=Cytosolic malate dehydrogenase {ECO:0000256|ARBA:ARBA00030284};
DE Flags: Fragment;
GN ORFNames=TREES_T100010661 {ECO:0000313|EMBL:ELW65399.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW65399.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(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; KB320689; ELW65399.1; -; Genomic_DNA.
DR AlphaFoldDB; L9KSD1; -.
DR STRING; 246437.L9KSD1; -.
DR eggNOG; KOG1496; Eukaryota.
DR InParanoid; L9KSD1; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
DR GO; GO:0016615; F:malate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
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; IPR010945; Malate_DH_type2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518}.
FT DOMAIN 29..83
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 82..217
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ELW65399.1"
SQ SEQUENCE 219 AA; 24885 MW; 2243B93A7064DA01 CRC64;
HWKWICLWQK PAHNSHAVGY HFMMGILDDV LMELQDCALP LLKDVIVTDK EDVAFKDLDV
AILVGSMPRR KGMERKDLLK ANYPDVNHAK VKLQGRKVGV YEALKNDSWL KEEFITLVQQ
RGADIIKAGK LSGATPAVKA ITDHVRDIWF GTPEGEIVSM GVISDGNSYH ISDDLLYSFP
VILENKTWKF IEGLPINDFS HEKMDFTAKE LAEEKKNCF
//