ID MDHC_CANAL Reviewed; 337 AA. AC P83778; A0A1D8PRT1; Q5AAK8; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2011, sequence version 2. DT 27-MAR-2024, entry version 92. DE RecName: Full=Malate dehydrogenase, cytoplasmic; DE EC=1.1.1.37; GN Name=MDH1; Synonyms=MDH2; OrderedLocusNames=CAALFM_CR00540CA; GN ORFNames=CaO19.7481; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., RA Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned RT on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates allele- RT specific measurements and provides a simple model for repeat and indel RT structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). RN [4] RP PROTEIN SEQUENCE OF 27-36; 39-55; 95-104 AND 231-244, SUBCELLULAR LOCATION, RP AND ANTIGENICITY. RC STRAIN=SC5314 / ATCC MYA-2876; TISSUE=Protoplast; RX PubMed=15378761; DOI=10.1002/pmic.200400903; RA Pitarch A., Abian J., Carrascal M., Sanchez M., Nombela C., Gil C.; RT "Proteomics-based identification of novel Candida albicans antigens for RT diagnosis of systemic candidiasis in patients with underlying hematological RT malignancies."; RL Proteomics 4:3084-3106(2004). 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:0000255|PROSITE-ProRule:PRU10004}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15378761}. CC -!- MISCELLANEOUS: Has antigenic properties. Elicits a specific immune CC response in systemic candidiasis human patients undergoing malignant CC hematological disorders. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family. CC {ECO:0000305}. 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; CP017630; AOW30823.1; -; Genomic_DNA. DR RefSeq; XP_718638.1; XM_713545.1. DR AlphaFoldDB; P83778; -. DR SMR; P83778; -. DR BioGRID; 1222761; 3. DR STRING; 237561.P83778; -. DR EnsemblFungi; CR_00540C_A-T; CR_00540C_A-T-p1; CR_00540C_A. DR GeneID; 3639667; -. DR KEGG; cal:CAALFM_CR00540CA; -. DR CGD; CAL0000181993; MDH1. DR VEuPathDB; FungiDB:CR_00540C_A; -. DR eggNOG; KOG1494; Eukaryota. DR HOGENOM; CLU_047181_1_0_1; -. DR InParanoid; P83778; -. DR OMA; CIVECAY; -. DR OrthoDB; 5059897at2759; -. DR Proteomes; UP000000559; Chromosome R. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; NAS:CGD. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0016615; F:malate dehydrogenase activity; NAS:CGD. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; NAS:CGD. 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:SF73; MALATE DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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. DR COMPLUYEAST-2DPAGE; P83778; -. PE 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; KW Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1..337 FT /note="Malate dehydrogenase, cytoplasmic" FT /id="PRO_0000113337" FT ACT_SITE 184 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P00346" FT BINDING 8..14 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 34 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 86 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 92 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 99 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 122..124 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 124 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 158 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 238 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT CONFLICT 28..29 FT /note="DE -> TD (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 33..36 FT /note="FDVV -> YDIR (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 42 FT /note="G -> A (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 45 FT /note="L -> V (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 48..55 FT /note="INSDSKTQ -> VPTNSTVK (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 98 FT /note="I -> T (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 104 FT /note="Q -> R (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 240 FT /note="Y -> Q (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 243 FT /note="Y -> A (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 337 AA; 36004 MW; 0BB466CAA0010CE4 CRC64; MVKVAILGAA GGIGQPLSLL TKLNPNVDEL ALFDVVNVPG VGADLSHINS DSKTQSYLPK DKEDKTALAA ALKGSDLVII PAGVPRKPGM TRDDLFNINA SIVQGLAEGI AANSPKAFVL VISNPVNSTV PIVAETLQAK GVYDPARLFG VTTLDIVRAN TFISQLFLDQ TKPSDFNINV VGGHSGETIV PLYSLGNSKQ YYDILSEEQK KELIKRVQFG GDEVVQAKNG AGSATLSMAY AGYRLAESIL AAVNGKTDIV ECTFLNLDSS IKGASEARKL VKDLDFFSLP VQLGKNGITE VKYDILNQIS DDEKKLLEVA IEQLQKNIEK GVSFAKK //