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Database: UniProt
Entry: A0A0D2MX08_9CHLO
LinkDB: A0A0D2MX08_9CHLO
Original site: A0A0D2MX08_9CHLO 
ID   A0A0D2MX08_9CHLO        Unreviewed;       511 AA.
AC   A0A0D2MX08;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0000313|EMBL:KIY98765.1};
DE            EC=1.1.1.40 {ECO:0000313|EMBL:KIY98765.1};
GN   ORFNames=MNEG_9195 {ECO:0000313|EMBL:KIY98765.1};
OS   Monoraphidium neglectum.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX   NCBI_TaxID=145388 {ECO:0000313|EMBL:KIY98765.1, ECO:0000313|Proteomes:UP000054498};
RN   [1] {ECO:0000313|EMBL:KIY98765.1, ECO:0000313|Proteomes:UP000054498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIY98765.1,
RC   ECO:0000313|Proteomes:UP000054498};
RX   PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA   Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA   Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA   Mussgnug J.H., Kruse O.;
RT   "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT   neglectum from its genome sequence reveals characteristics suitable for
RT   biofuel production.";
RL   BMC Genomics 14:926-926(2013).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000256|PIRSR:PIRSR000106-3};
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785}.
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DR   EMBL; KK102070; KIY98765.1; -; Genomic_DNA.
DR   RefSeq; XP_013897785.1; XM_014042331.1.
DR   AlphaFoldDB; A0A0D2MX08; -.
DR   STRING; 145388.A0A0D2MX08; -.
DR   GeneID; 25742070; -.
DR   KEGG; mng:MNEG_9195; -.
DR   OrthoDB; 1069499at2759; -.
DR   Proteomes; UP000054498; Unassembled WGS sequence.
DR   GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR012301; Malic_N_dom.
DR   InterPro; IPR037062; Malic_N_dom_sf.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23406:SF79; MALATE DEHYDROGENASE (OXALOACETATE-DECARBOXYLATING); 1.
DR   PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 2.
DR   PIRSF; PIRSF000106; ME; 3.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3};
KW   Oxidoreductase {ECO:0000313|EMBL:KIY98765.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054498}.
FT   DOMAIN          4..161
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          172..496
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          392..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        28
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        99
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         171
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         427
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   511 AA;  52306 MW;  1B967FF6B18DCB8F CRC64;
     MALKESSRDV FYALLQGPDL EALLRVVYTP TIGEACLRFG SLIPRPSCLY VSAAMAGSVA
     EAVANWPQQG VRLAVVTDGE RILGLGDLGC HGAGIPIGKC IVYAAAGLPP DWLLPIVVDV
     GTENAGLREG DPLYVGLPQR RLRGDAYYSL MEAFSMLQRL RASGTPTFND DIECTAGVTV
     AALLGALRVQ GVLPLEQQRF LFFGAGQASL GTARLIVRLM QRRGVPESVA RSAIWMIDSR
     GLITTARKGL TPEKAEFAQD PTGQLPPDLA QASAGEGTPI AARGGRSQAQ VAAALLQRAI
     AALRPTALVG AATVGGAFDR GVLEALVQSA AAEAGPDARP LCFALSNPTE KAEVRFGDAW
     EWSGGRVVYA SGTAFPGLAV ASDGSAVPLE APPNPWASQA TSAGGVEPGG SRGAGAGARV
     LRPAQCNNSH VFPGLALGCI ATGASAVNDD MLLAAAGAIA GMVTPGELAS ECVLPSMARL
     RETTAAVAAA VAAVAFGDEL GTVTVDSARC A
//
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