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Database: UniProt
Entry: C5M156_PERM5
LinkDB: C5M156_PERM5
Original site: C5M156_PERM5 
ID   C5M156_PERM5            Unreviewed;       316 AA.
AC   C5M156;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995};
GN   ORFNames=Pmar_PMAR024729 {ECO:0000313|EMBL:EEQ97286.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EEQ97286.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) 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|ARBA:ARBA00000774};
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; GG687290; EEQ97286.1; -; Genomic_DNA.
DR   RefSeq; XP_002764569.1; XM_002764523.1.
DR   AlphaFoldDB; C5M156; -.
DR   EnsemblProtists; EEQ97286; EEQ97286; Pmar_PMAR024729.
DR   GeneID; 9054511; -.
DR   InParanoid; C5M156; -.
DR   OMA; FGCAVEL; -.
DR   OrthoDB; 276094at2759; -.
DR   Proteomes; UP000007800; Unassembled WGS sequence.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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; 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:SF16; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007800};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          2..149
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          151..313
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        181
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         8..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         98
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         121..123
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         232
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   316 AA;  33565 MW;  AEC17D61F22D3635 CRC64;
     MTKVSLLGAS GGIGQPLSML LKLNPMITKL ALYDIKQAMV PCAGVAADVS HINTPAKVVG
     YAGDDEIESA LSGANVIVMT AGVPRKPGMT RDDLFKINAG IVRGLATASA KYAPNATLCI
     VSNPVNSTVP IAAEIYKKAG VFDPKKIVGV TQLDITRANT FVSEKTGMDV QHMDVPVIGG
     HAGETIMTLF SQARPEVKLD QATIEELDKR IQNAGTEVVE AKNGAGSATL SMAYAAAKFV
     DVVIRGQCGQ ISTACAYINE PFEDVSYFSY RCDFGPEGVS RIHPLEGLTP YEKGRLEEVK
     RKLKGDIQNG ITFANN
//
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