ID   MDHC_CHICK              Reviewed;         334 AA.
AC   Q5ZME2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Malate dehydrogenase, cytoplasmic;
DE            EC=1.1.1.37;
DE   AltName: Full=Cytosolic malate dehydrogenase;
GN   Name=MDH1; ORFNames=RCJMB04_2g5;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Catalyzes the reduction of aromatic alpha-keto acids in the
CC       presence of NADH. Plays essential roles in the malate-aspartate shuttle
CC       and the tricarboxylic acid cycle, important in mitochondrial NADH
CC       supply for oxidative phosphorylation. Catalyzes the reduction of 2-
CC       oxoglutarate to 2-hydroxyglutarate, leading to elevated reactive oxygen
CC       species (ROS). {ECO:0000250|UniProtKB:P40925}.
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   -!- 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:0000250|UniProtKB:P40925};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:57174;
CC         Evidence={ECO:0000250|UniProtKB:P40925};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11708}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P40925}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ719442; CAG31101.1; -; mRNA.
DR   RefSeq; NP_001006395.1; NM_001006395.2.
DR   AlphaFoldDB; Q5ZME2; -.
DR   SMR; Q5ZME2; -.
DR   BioGRID; 682121; 1.
DR   IntAct; Q5ZME2; 1.
DR   STRING; 9031.ENSGALP00000014374; -.
DR   PaxDb; 9031-ENSGALP00000014374; -.
DR   Ensembl; ENSGALT00010040102.1; ENSGALP00010023245.1; ENSGALG00010016624.1.
DR   Ensembl; ENSGALT00015044285; ENSGALP00015026208; ENSGALG00015018072.
DR   GeneID; 421281; -.
DR   KEGG; gga:421281; -.
DR   CTD; 4190; -.
DR   VEuPathDB; HostDB:geneid_421281; -.
DR   eggNOG; KOG1496; Eukaryota.
DR   GeneTree; ENSGT00530000063410; -.
DR   HOGENOM; CLU_040727_2_0_1; -.
DR   InParanoid; Q5ZME2; -.
DR   OMA; TKGMERG; -.
DR   PhylomeDB; Q5ZME2; -.
DR   TreeFam; TF105826; -.
DR   Reactome; R-GGA-352875; Gluconeogenesis.
DR   PRO; PR:Q5ZME2; -.
DR   Proteomes; UP000000539; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR   GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..334
FT                   /note="Malate dehydrogenase, cytoplasmic"
FT                   /id="PRO_0000226738"
FT   ACT_SITE        187
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         11..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         129..131
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   334 AA;  36543 MW;  2AD5D831DC812332 CRC64;
     MGEPIRVLVT GAAGQIAYSL LYSIAKGDVF GKEQPLVLVL LDITPMMTVL EGVVMELQDC
     ALPLLREVIP TDKEEVAFKD LDIAILVGSM PRREGMERKD LLKANVKIFK SQGAALDKYA
     KKTVKVVVVG NPANTNCLIA SKSAPSIPKE NFSCLTRLDH NRAKSQIALK LGVTSNDVKN
     VIIWGNHSST QYPDVNHAKV NVKGKEVGVY EAIKDDSWLK GDFILTVQQR GAAVIKARKL
     SSAMSAAKAI CDHVRDIWFG TPAGEFVSMG VISDGNSYGV PEDLLYSFPV VIKDKTWKFV
     EGLPINDFSR EKMDLTAKEL TEEKETAVEF LSSA
//