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MDHC_CANAL
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   03-AUG-2022, entry version 86.
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}.
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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   COMPLUYEAST-2DPAGE; P83778; -.
DR   PRIDE; P83778; -.
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; CAYVASH; -.
DR   OrthoDB; 1204514at2759; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IBA:GO_Central.
DR   CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR   Gene3D; 3.90.110.10; -; 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   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
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
 
 
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