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Database: UniProt
Entry: F7EM18_ORNAN
LinkDB: F7EM18_ORNAN
Original site: F7EM18_ORNAN 
ID   F7EM18_ORNAN            Unreviewed;       338 AA.
AC   F7EM18;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|RuleBase:RU003405};
DE            EC=1.1.1.37 {ECO:0000256|RuleBase:RU003405};
GN   Name=MDH2 {ECO:0000313|Ensembl:ENSOANP00000002188.3};
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000002188.3, ECO:0000313|Proteomes:UP000002279};
RN   [1] {ECO:0000313|Ensembl:ENSOANP00000002188.3, ECO:0000313|Proteomes:UP000002279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000002188.3,
RC   ECO:0000313|Proteomes:UP000002279};
RX   PubMed=18464734; DOI=10.1038/nature06936;
RA   Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA   Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA   Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA   Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA   Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA   Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA   Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA   Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA   Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA   Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA   Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA   Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA   Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA   Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA   Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA   Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA   Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA   Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA   de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT   "Genome analysis of the platypus reveals unique signatures of evolution.";
RL   Nature 453:175-183(2008).
RN   [2] {ECO:0000313|Ensembl:ENSOANP00000002188.3}
RP   IDENTIFICATION.
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000002188.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:ARBA00000774,
CC         ECO:0000256|RuleBase:RU003405};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008824}.
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DR   AlphaFoldDB; F7EM18; -.
DR   STRING; 9258.ENSOANP00000002188; -.
DR   Ensembl; ENSOANT00000002189.4; ENSOANP00000002188.3; ENSOANG00000001378.4.
DR   eggNOG; KOG1494; Eukaryota.
DR   GeneTree; ENSGT00390000016686; -.
DR   HOGENOM; CLU_047181_0_1_1; -.
DR   InParanoid; F7EM18; -.
DR   OMA; SHMDTPA; -.
DR   OrthoDB; 5059897at2759; -.
DR   TreeFam; TF300834; -.
DR   Proteomes; UP000002279; Chromosome 17.
DR   Bgee; ENSOANG00000001378; Expressed in heart and 7 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:Ensembl.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR   GO; GO:0006108; P:malate metabolic process; IEA:Ensembl.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   CDD; cd01337; MDH_glyoxysomal_mitochondrial; 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   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   NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
DR   PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 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:UP000002279};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU003405}.
FT   DOMAIN          26..168
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          170..333
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        200
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         31..37
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         57
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         117
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         140..142
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         251
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   338 AA;  35697 MW;  8DAB8CA7D4052E6C CRC64;
     MLSSFARPAG AVLRRSLTTS AQNHAKVAVL GAAGGIGQPL SLLLKNSPLV SRLTLYDIAH
     TPGVAADLSH IETRANAKGY LGPEQLPDCL KGCDVVVIPA GVPRKPGMTR DDLFNTNATI
     VATLASACAQ HCPEAMVCII ANPVNSTIPI TSEVFKKHGV YNPNRIFGVT TLDIVRANTF
     VAELKGLDPA RVNVPVIGGH AGKTIIPLIS QCTPKVDFPQ DQLTALTGRI QEAGTEVVKA
     KAGAGSATLS MAYAGARFVF SVVDAMNGKE GVVECSFVRS EETECSYFST PLLLGKKGIE
     KNLGMGKLSP FEEKMVAEAI PELKASIRKG EDFVKNMK
//
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