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Database: UniProt
Entry: U5HIM0_USTV1
LinkDB: U5HIM0_USTV1
Original site: U5HIM0_USTV1 
ID   U5HIM0_USTV1            Unreviewed;       346 AA.
AC   U5HIM0;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 60.
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=MVLG_06870 {ECO:0000313|EMBL:KDE02587.1};
OS   Microbotryum lychnidis-dioicae (strain p1A1 Lamole / MvSl-1064) (Anther
OS   smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=683840 {ECO:0000313|EMBL:KDE02587.1};
RN   [1] {ECO:0000313|Proteomes:UP000017200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200};
RA   Cuomo C., Perlin M., Young S.K., Zeng Q., Gargeya S., Alvarado L.,
RA   Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Mehta T.,
RA   Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Microbotryum violaceum strain p1A1 Lamole.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KDE02587.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE02587.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Butler R., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA   Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   White J., Yandava C., Wortman J., Nusbaum C., Birren B.;
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KDE02587.1, ECO:0000313|Proteomes:UP000017200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE02587.1}, and p1A1 Lamole
RC   {ECO:0000313|Proteomes:UP000017200};
RX   PubMed=26076695; DOI=10.1186/s12864-015-1660-8;
RA   Perlin M.H., Amselem J., Fontanillas E., Toh S.S., Chen Z., Goldberg J.,
RA   Duplessis S., Henrissat B., Young S., Zeng Q., Aguileta G., Petit E.,
RA   Badouin H., Andrews J., Razeeq D., Gabaldon T., Quesneville H., Giraud T.,
RA   Hood M.E., Schultz D.J., Cuomo C.A.;
RT   "Sex and parasites: genomic and transcriptomic analysis of Microbotryum
RT   lychnidis-dioicae, the biotrophic and plant-castrating anther smut
RT   fungus.";
RL   BMC Genomics 16:461-461(2015).
RN   [4] {ECO:0000313|EnsemblFungi:MVLG_06870T0}
RP   IDENTIFICATION.
RG   EnsemblFungi;
RL   Submitted (JUN-2015) 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   EMBL; AEIJ01000918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GL541803; KDE02587.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5HIM0; -.
DR   STRING; 683840.U5HIM0; -.
DR   EnsemblFungi; MVLG_06870T0; MVLG_06870T0; MVLG_06870.
DR   HOGENOM; CLU_047181_1_0_1; -.
DR   InParanoid; U5HIM0; -.
DR   OMA; MGWTSQA; -.
DR   OrthoDB; 5059897at2759; -.
DR   Proteomes; UP000017200; 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:SF73; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017200};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU003405}.
FT   DOMAIN          23..167
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          169..339
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        199
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         29..35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         55
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         116
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         139..141
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         253
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   346 AA;  35883 MW;  C64BB9CEAF83DB16 CRC64;
     MISPIATRAL GRRAFSTSRS AATKVAVLGA AGGIGQPLSL LLKLNPRVTE LSLYDIRGCP
     GVAADLSHVN TPSPVAGYAA ENNGLEKALT GAEVIIIPAG MPRKPGMTRD DLFNTNASIV
     RDLAIAAAKV APKARIGIIA NPVNSTVPIV AEVFKKAGVY DPKRLFGVTT LDIVRASAFV
     SGIAGTHPKD TNIPVVGGHS GVTIVPLFSQ TPEGKKIVEK GGEELAALVK RTQFGGDEVV
     KAKDGAGSAT LSMAYAGAEF TDAILRAIDG EKNVTLCTYV ESPLYAKDGV DFFSSPVTLN
     SEGIVGEIHP VGKLHPSEEE LLKACLPDLA KNIKAGVDFV AKNPGN
//
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