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Database: UniProt
Entry: A0A0G4IMK2_PLABS
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ID   A0A0G4IMK2_PLABS        Unreviewed;       374 AA.
AC   A0A0G4IMK2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=PBRA_005074 {ECO:0000313|EMBL:CEO96403.1};
OS   Plasmodiophora brassicae (Clubroot disease agent).
OC   Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC   Plasmodiophoridae; Plasmodiophora.
OX   NCBI_TaxID=37360 {ECO:0000313|EMBL:CEO96403.1, ECO:0000313|Proteomes:UP000039324};
RN   [1] {ECO:0000313|EMBL:CEO96403.1, ECO:0000313|Proteomes:UP000039324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3 {ECO:0000313|EMBL:CEO96403.1};
RA   Chooi Y.-H.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU003405};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|ARBA:ARBA00009613}.
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DR   EMBL; CDSF01000057; CEO96403.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4IMK2; -.
DR   STRING; 37360.A0A0G4IMK2; -.
DR   EnsemblProtists; CEO96403; CEO96403; PBRA_005074.
DR   OMA; GMIGSNM; -.
DR   OrthoDB; 501358at2759; -.
DR   Proteomes; UP000039324; 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; cd01338; MDH_choloroplast_like; 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   HAMAP; MF_01517; Malate_dehydrog_2; 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; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR   PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 2.
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:UP000039324};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU003405}.
FT   DOMAIN          35..99
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          115..199
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          203..367
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        234
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         40..46
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         152
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         176..178
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   374 AA;  39930 MW;  BB48F816C6DAE1C1 CRC64;
     MLSSGMWRNI GRVVSAGASS RGLAARAMST KPAKRVAVTG AAGQIGYSLL FRIASGELFG
     PDQPVIIHAI ELEAALKNLA GVAMELDDCA FPLLKGSKDA PDSFAAVRFV ESYAVVQTSD
     LNEGFDDIDY ALLVGSRPRG KGMERKDLLA INGKIFVGTG EALNKNAKKT AKVLVVGNPA
     NTNCLVAASN APNIPRSNFS AMTRLDHDRA VAQVAIKTQS HCTDVAKVAI WGNHSATQYP
     DITHATVKGK PAKSLINDEK WVRETFIPTV QQRGAAIIAA RGLSSAASAA NAAIMQTRDR
     ALGTNGKWVS MAVPSDGSYG IEEGIFFSYP VTTAKDEYKI VQGLEIDSFS AEMIEKTKKE
     LLEERDMVAD LLKD
//
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