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Database: UniProt
Entry: C1MJJ1_MICPC
LinkDB: C1MJJ1_MICPC
Original site: C1MJJ1_MICPC 
ID   C1MJJ1_MICPC            Unreviewed;       362 AA.
AC   C1MJJ1;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 73.
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   Name=MDH {ECO:0000313|EMBL:EEH59206.1};
GN   ORFNames=MICPUCDRAFT_63993 {ECO:0000313|EMBL:EEH59206.1};
OS   Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876};
RN   [1] {ECO:0000313|EMBL:EEH59206.1, ECO:0000313|Proteomes:UP000001876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH59206.1,
RC   ECO:0000313|Proteomes:UP000001876};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA   John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA   Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA   Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA   Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the marine
RT   picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
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; GG663736; EEH59206.1; -; Genomic_DNA.
DR   RefSeq; XP_003055830.1; XM_003055784.1.
DR   AlphaFoldDB; C1MJJ1; -.
DR   STRING; 564608.C1MJJ1; -.
DR   GeneID; 9681619; -.
DR   KEGG; mpp:MICPUCDRAFT_63993; -.
DR   eggNOG; KOG1494; Eukaryota.
DR   OMA; CIVECAY; -.
DR   OrthoDB; 5059897at2759; -.
DR   Proteomes; UP000001876; 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: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.
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:UP000001876};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU003405}.
FT   DOMAIN          52..194
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          196..359
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        226
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         57..63
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         83
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         143
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         166..168
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         277
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   362 AA;  37439 MW;  743FC37B1AFEAC16 CRC64;
     MAAAAMPVAA PVLSARASFR GSSKSSVRRS TAKAAATTTR RRVATATTSE YKVAVLGAAG
     GIGQSLSLLL KMNPMIAQLN LYDIQGTPGV AADLSHTNTQ TKVTGYAGAD SLADALKGCD
     LVIIPAGVPR KPGMTRDDLF EINAGIVKTL CEAVAANCPG ALVNIISNPV NSTVPIAAEV
     FKKAGTYDPK KVFGVTTLDV VRSNTFVAEA KGLDVNDVDI PVVGGHAGIT ILPLLSQSYP
     ATKFDADELE AMTVRIQNAG TEVVEAKAGA GSATLSMAYA AARMAEACLR GLSGEADVYE
     CSYVASSVTE LPFFATKVRL GPGGAEEVLP VGDLTEYEKG WLEKLIPELK GSIDKGIAFA
     NK
//
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