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Database: UniProt
Entry: A0A087SG45_AUXPR
LinkDB: A0A087SG45_AUXPR
Original site: A0A087SG45_AUXPR 
ID   A0A087SG45_AUXPR        Unreviewed;       313 AA.
AC   A0A087SG45;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=F751_2417 {ECO:0000313|EMBL:KFM24699.1};
OS   Auxenochlorella protothecoides (Green microalga) (Chlorella
OS   protothecoides).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Auxenochlorella.
OX   NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM24699.1, ECO:0000313|Proteomes:UP000028924};
RN   [1] {ECO:0000313|EMBL:KFM24699.1, ECO:0000313|Proteomes:UP000028924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0710 {ECO:0000313|EMBL:KFM24699.1,
RC   ECO:0000313|Proteomes:UP000028924};
RX   PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA   Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT   "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT   protothecoides revealed through its genome, transcriptomes, and
RT   proteomes.";
RL   BMC Genomics 15:582-582(2014).
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; KL662109; KFM24699.1; -; Genomic_DNA.
DR   RefSeq; XP_011397587.1; XM_011399285.1.
DR   AlphaFoldDB; A0A087SG45; -.
DR   STRING; 3075.A0A087SG45; -.
DR   GeneID; 23613808; -.
DR   KEGG; apro:F751_2417; -.
DR   eggNOG; KOG1494; Eukaryota.
DR   OrthoDB; 5059897at2759; -.
DR   Proteomes; UP000028924; 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   PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11540:SF47; MALATE DEHYDROGENASE; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 2.
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:UP000028924};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU003405}.
FT   DOMAIN          29..143
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          144..309
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         34..40
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         60
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         227
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   313 AA;  32707 MW;  565855990685E1B6 CRC64;
     MNSLFRASRD LLRASATRGY ASASFPDRKV AVLGAAGGIG QPLSLLLKLN PYVTELALYD
     IAGTPGVAAD ISHINSKGRV KGYAGEDQLG EALKGADVIV IPAGVPRKPG MTRDDLFKIN
     AGIVRALVLK AAGVYDKRKV LGVTTLDVVR AKTFYAEKAG VDVGKVDVPV VGGHAGITIL
     PLFSQTVPTP NVDLSPADID ALTKRTQEGG TEVVQAKAGK GSATLSMAYA GALMADACLR
     GLNGDSDVVE CAYVESTVTD LPFFASKVRL GRAGVEEVYG LGELNDYERA GLKSLVPELQ
     ASIDKGVKFM QEA
//
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