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Database: UniProt
Entry: A0A0G4PFX8_PENCA
LinkDB: A0A0G4PFX8_PENCA
Original site: A0A0G4PFX8_PENCA 
ID   A0A0G4PFX8_PENCA        Unreviewed;       602 AA.
AC   A0A0G4PFX8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN   ORFNames=PCAMFM013_S014g000107 {ECO:0000313|EMBL:CRL25211.1};
OS   Penicillium camemberti FM 013.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1429867 {ECO:0000313|EMBL:CRL25211.1, ECO:0000313|Proteomes:UP000053732};
RN   [1] {ECO:0000313|Proteomes:UP000053732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM 013 {ECO:0000313|Proteomes:UP000053732};
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F.,
RA   Goarin A., Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T.,
RA   Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in
RT   cheesemaking fungi.";
RL   Submitted (NOV-2013) 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|RuleBase:RU003426}.
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DR   EMBL; HG793147; CRL25211.1; -; Genomic_DNA.
DR   EnsemblFungi; CRL25211; CRL25211; PCAMFM013_S014g000107.
DR   Proteomes; UP000053732; 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; 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   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.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000053732};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW   ECO:0000256|RuleBase:RU003426};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003426};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053732}.
FT   DOMAIN       86    264       malic. {ECO:0000259|SMART:SM01274}.
FT   DOMAIN      274    534       Malic_M. {ECO:0000259|SMART:SM00919}.
FT   ACT_SITE    109    109       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   ACT_SITE    180    180       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   METAL       251    251       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       252    252       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       273    273       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
SQ   SEQUENCE   602 AA;  66828 MW;  4527F6914C13013F CRC64;
     MARYPSLPTQ QSRPVHATPA PFVNHASPAD ANYDTANPAY IRKYLRTYGL TPPRAEGYET
     QKTRCLAQLG LKSTPIEKFL YLSSLRKNNV HLFYRLVTDH LREMTPLIYT PVVGEACQRW
     SEIYQQAEGM YLSWEDRGNL ASVISNWPES SVEITCITDG SRILGLGDLG INGMGIPIGK
     LALYTACAGI RPEATLPLTL DLGTSNKALR EDPLYMGSRR EKISPEEERE FLDELMGALT
     ERWPGIVIQF EDFKNPFPAL ERYRDLYTCF NDDIQGTGAV ILGGVINAVK RSGLPCKDHR
     AVFFGAGSAG VGVARQIVEF FMREGMTEDE ARNCFYLVDT KGLVTADRGD KLADHKVYFA
     RQDNNGEQYK TLDEVVDYVK PSILMGLSTM GGVFTPEILR KMADWNTAPL IFPLSNPSSK
     SECDFETAVT HTDGRCLFAS GSPFPNFTFT NSAGETRTYY PGQGNNMYVF PGIGLGSILS
     KAVRVTDSMI YASGASLSTA LTGEELERGL LYPDITRIRE VSVVVTRKVM RAAQEDKVDR
     EIALRSMSDI ELDNWIKARM YDPHTEVRAL EREVGHLLSS LGTISPPMTA SGSPTEEKNA
     KL
//
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