GenomeNet

Database: UniProt
Entry: A0A0E0N1V9_ORYRU
LinkDB: A0A0E0N1V9_ORYRU
Original site: A0A0E0N1V9_ORYRU 
ID   A0A0E0N1V9_ORYRU        Unreviewed;       561 AA.
AC   A0A0E0N1V9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI01G32430.1, ECO:0000313|Proteomes:UP000008022};
RN   [1] {ECO:0000313|Proteomes:UP000008022}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA   Zhao Q.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORUFI01G32430.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003426}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A0E0N1V9; -.
DR   STRING; 4529.A0A0E0N1V9; -.
DR   EnsemblPlants; ORUFI01G32430.1; ORUFI01G32430.1; ORUFI01G32430.
DR   Gramene; ORUFI01G32430.1; ORUFI01G32430.1; ORUFI01G32430.
DR   eggNOG; KOG1257; Eukaryota.
DR   HOGENOM; CLU_011405_5_1_1; -.
DR   OMA; PVIMPMS; -.
DR   Proteomes; UP000008022; Unassembled WGS sequence.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:UniProt.
DR   CDD; cd05312; NAD_bind_1_malic_enz; 1.
DR   Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR015884; Malic_enzyme_CS.
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; MALIC ENZYME-RELATED; 1.
DR   PANTHER; PTHR23406:SF89; NADP-DEPENDENT MALIC ENZYME 1; 1.
DR   Pfam; PF00390; malic; 2.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 2.
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.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000106-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003426};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008022};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          118..267
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          277..530
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        141
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        212
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         252
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         253
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         276
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         417
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         461
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   561 AA;  61837 MW;  1531ED30D100F34F CRC64;
     MESTMKGIRG DNAPCVLDLD DAATVGGGVG DTYGEDCATE EQLVTPWTVS VASGYNLLRD
     PRYNKGLAFN ERERETHYLR GLLPPAIVSQ ELQERKIMHN IRQYQLPLQK YMAMMDLQEG
     NERLFYKLLI DNVEELLPVV YTPTVGEACQ KYGSIFSRPQ GLYISLKEKG KILEVLKNWP
     ERSIQVIVVT DGERILGLGD LGCQGMGIPV GKLALYTALG GVRPSAEYAD FLHEFMTAVK
     QNYGEKVLIQ FEDFANHNAF ELLAKYGTTH LVFNDDIQGT ASVVLSGLVA ALKLVGGSLS
     EHSYLFLGAG EAGTGIAELI ALEISRQTKA PIEECRKKIW LVDSKGLIVS SRKETLQHFK
     KPWAHEHEPV GNLLDAVKTI KPTVLIGTSG KGQTFTQEVV EAISSFNERP VIFALSNPTS
     QSECTAEQAY TWSKGRAVFA SGSPFDPVEY DGKIYVPGQA NNAYIFPGFG LGVVMSGAIR
     VHDDMLLAAS EALAQQVTQE NFDKGLTYPP FSNIRKISAH IAANVAAKAY ELGLASRRPR
     PKDLVKYAES CMYSPLYRNY R
//
DBGET integrated database retrieval system