ID C4Y9Q7_CLAL4 Unreviewed; 343 AA. AC C4Y9Q7; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 80. DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU003405}; DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU003405}; GN ORFNames=CLUG_05128 {ECO:0000313|EMBL:EEQ41000.1}; OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Metschnikowiaceae; Clavispora. OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ41000.1, ECO:0000313|Proteomes:UP000007703}; RN [1] {ECO:0000313|EMBL:EEQ41000.1, ECO:0000313|Proteomes:UP000007703} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ41000.1, RC ECO:0000313|Proteomes:UP000007703}; RX PubMed=19465905; DOI=10.1038/nature08064; RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S., RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C., RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M., RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R., RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J., RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M., RA Cuomo C.A.; RT "Evolution of pathogenicity and sexual reproduction in eight Candida RT genomes."; RL Nature 459:657-662(2009). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH408081; EEQ41000.1; -; Genomic_DNA. DR RefSeq; XP_002615113.1; XM_002615067.1. DR AlphaFoldDB; C4Y9Q7; -. DR STRING; 306902.C4Y9Q7; -. DR GeneID; 8495697; -. DR KEGG; clu:CLUG_05128; -. DR VEuPathDB; FungiDB:CLUG_05128; -. DR HOGENOM; CLU_047181_1_0_1; -. DR InParanoid; C4Y9Q7; -. DR OMA; IVNAHGV; -. DR OrthoDB; 5059897at2759; -. DR Proteomes; UP000007703; Unassembled WGS sequence. 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; 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|PIRSR:PIRSR000102-3, ECO:0000256|RuleBase:RU003405}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003369}; KW Reference proteome {ECO:0000313|Proteomes:UP000007703}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, KW ECO:0000256|RuleBase:RU003405}. FT DOMAIN 2..150 FT /note="Lactate/malate dehydrogenase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00056" FT DOMAIN 152..337 FT /note="Lactate/malate dehydrogenase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02866" FT ACT_SITE 184 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1" FT BINDING 8..14 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 34 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 86 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 92 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 99 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 122..124 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 124 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 158 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 239 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3" SQ SEQUENCE 343 AA; 35872 MW; 0C174B42A59C1B92 CRC64; MVKVTVCGAA GGIGQPLSML LKLNPRVSRL ALYDIVNAVG VAADLSHINT PAVVTGHQPA AKNDSSALVE ALQDSDIVVI PAGVPRKPGM SRADLFNINA SIVRDLVAHA GRTCPNAAIL IISNPVNATV AIAAAVLKKL GVFNPRKLFG VTTLDSVRAE TFLAQILDVP PASLRGKISV VGGHSGDTIV PLVHFDRALE SKMKTVSASD YANFVHRVQY GGDEVVKAKI GAGSATLSMA YAGYRFASNV LASLVDAAEY SAVPDSAYIY LDGAAGGAEI ATTLQDTPFF SVPVHLKKGE VSSVVDPWHL VRTHEEKKMI AVALEGLEKS VSQGTNFVEG SKI //