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Database: UniProt
Entry: C1EDY1_MICCC
LinkDB: C1EDY1_MICCC
Original site: C1EDY1_MICCC 
ID   C1EDY1_MICCC            Unreviewed;       716 AA.
AC   C1EDY1;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=NADP dependent malic enzyme, chloroplast {ECO:0000313|EMBL:ACO66442.1};
GN   ORFNames=MICPUN_62430 {ECO:0000313|EMBL:ACO66442.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO66442.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO66442.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
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   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785}.
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DR   EMBL; CP001330; ACO66442.1; -; Genomic_DNA.
DR   RefSeq; XP_002505184.1; XM_002505138.1.
DR   AlphaFoldDB; C1EDY1; -.
DR   STRING; 296587.C1EDY1; -.
DR   GeneID; 8247606; -.
DR   KEGG; mis:MICPUN_62430; -.
DR   eggNOG; KOG1257; Eukaryota.
DR   InParanoid; C1EDY1; -.
DR   OMA; MVYAACG; -.
DR   OrthoDB; 1069499at2759; -.
DR   Proteomes; UP000002009; Chromosome 11.
DR   GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000002009}.
FT   DOMAIN          211..391
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          402..658
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   716 AA;  74251 MW;  423BDFDBE787A934 CRC64;
     MTSALTCATA SRPVTRAGPR PRSTRADARH PRVVNARARS TSAPGDAIGR DVVPEPASSE
     TIEGIVVDDD RDGSPVRISG NVRASRRGVL GGLGGVGAAL GLTSSTSAIV GPGAAEAAAA
     PASSPAPIAE IAAASSRATS ASPASSIVGY ANLHDPRVFN GLATPDRTNR SLDGLIPAGE
     APPDVEVARA AAALEACDTP MQKYRQLVSL QNTDETTFYA LLELKTAELL PVLYTPTVGD
     ACLQFGTLTQ RPPGLYVSLE NIGNVRALVD NWPANDVRIA VLTDGERILG LGDQGVNGMG
     ISAGKSMVYA ACGIKPGWLL PVQVDNGTNN TKLLADPLYV GTRRERVRGE AYDRLLDETV
     QAIQGRYGAR TVIHWEDFAP RNAFRNLQRF RTKGAITYND DIQGTAAVTV AGILASLRVT
     KRALREQRVL FFGAGQANIG AAELLVRALT EEGVDESLAR SNVFLFDSKG LVVDGRPAEY
     TISDDKAPFA AKVGTPFTSS LEEAVKSVRP TALVGAAAQP QVFTKRVIES MCAFNPRPVI
     FALSNPTSKA ECTATQAYEW SKGKAVFASG TLFAPVNYKG VRFAPGFANN AFIFPGVALG
     SLASGASSVT DAMFLAAARS LASQVSEENL AVGAVYPPTS TIREAAVVVG AAVAAAADEG
     GVAAPGACRG GAIPGRDGGR SVVVPSLDAL TGGGNPGDGT CANWEACVRD YLKTCV
//
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