ID A0A484DTN6_BRELC Unreviewed; 618 AA. AC A0A484DTN6; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 19-JAN-2022, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:TDH65809.1}; GN ORFNames=CCR75_004056 {ECO:0000313|EMBL:TDH65809.1}; OS Bremia lactucae (Lettuce downy mildew). OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae; OC Bremia. OX NCBI_TaxID=4779 {ECO:0000313|EMBL:TDH65809.1, ECO:0000313|Proteomes:UP000294530}; RN [1] {ECO:0000313|EMBL:TDH65809.1, ECO:0000313|Proteomes:UP000294530} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SF5 {ECO:0000313|EMBL:TDH65809.1, RC ECO:0000313|Proteomes:UP000294530}; RA Fletcher K.; RT "Genomic signatures of somatic hybrid vigor due to heterokaryosis in the RT oomycete pathogen, Bremia lactucae."; RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases. 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:TDH65809.1}. 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 EMBL; SHOA01000118; TDH65809.1; -; Genomic_DNA. DR STRING; 4779.A0A484DTN6; -. DR VEuPathDB; FungiDB:CCR75_004056; -. DR Proteomes; UP000294530; 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 Gene3D; 3.40.50.10380; -; 1. 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 Pfam; PF00390; malic; 1. DR Pfam; PF03949; Malic_M; 1. DR PIRSF; PIRSF000106; ME; 1. DR PRINTS; PR00072; MALOXRDTASE. DR SMART; SM01274; malic; 1. DR SMART; SM00919; Malic_M; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 3: Inferred from homology; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3}; KW Reference proteome {ECO:0000313|Proteomes:UP000294530}. FT DOMAIN 141..321 FT /note="malic" FT /evidence="ECO:0000259|SMART:SM01274" FT DOMAIN 331..583 FT /note="Malic_M" FT /evidence="ECO:0000259|SMART:SM00919" FT ACT_SITE 164 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1" FT ACT_SITE 235 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1" FT METAL 306 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3" FT METAL 307 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3" FT METAL 330 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3" SQ SEQUENCE 618 AA; 68133 MW; A87F0EAD9E800773 CRC64; MLALQVRTQK RLLLNATTAS VALHKRFASA PVITEDHEEN EEALSVGEPS GFERDTLDTY LNSLQKYNPP IKTGLKGLNI IHDPLYNKGT GFPHVERDRL GLRGLVPPRR LSVEAQLSKL YDTFSQERDP LGKSRFLTDL HDRNETLFFR LLIKHMKEMA PIVYTPTVGV VCQKFGHLYR RPRGMFFSTR DRSQFGAMVY NWPCDDVEVI VVTDGSRILG LGDLGANGMG IPIGKLALYT AAGGIDPRKV LPVMLDTGTN NQTLLNDPYY LGVQQPRLTG EAFWSMVDEF MRAVRHRWPK VLVQFEDFSS EHAADVLNAY RLKQLCFNDD IQGTGATVLA GALSACERVK IPLKEQRIVI LGAGSAGLGV ASTLLQGMLR EGMTIPEARE RFYILDQYGL LGEARDSLNS GQQFFSRSDL ADKTNLVEVI KQAKPTMLMG LSAAAGAFTQ EAVEEMAKHA EQPIVFPLSN PTSVAECTAE QAYEWTTGKC VFASGSPFEP VTYNGTQYNI SQCNNMFIFP GVGLASSVIQ ATRVTDGMLY SAAKALSQCM TSDEIANGQV FPSVENIRDV SLKVATAVCE TALDEDVAGV RPKIRRGGTL EDFVASKMYF PAYHALVE //