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Database: UniProt
Entry: A0A0D1YYU3_9EURO
LinkDB: A0A0D1YYU3_9EURO
Original site: A0A0D1YYU3_9EURO 
ID   A0A0D1YYU3_9EURO        Unreviewed;       623 AA.
AC   A0A0D1YYU3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   20-DEC-2017, entry version 17.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN   ORFNames=PV08_01026 {ECO:0000313|EMBL:KIW20451.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW20451.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW20451.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW20451.1,
RC   ECO:0000313|Proteomes:UP000053328};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala spinifera CBS89968.";
RL   Submitted (JAN-2015) 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; KN847492; KIW20451.1; -; Genomic_DNA.
DR   RefSeq; XP_016240667.1; XM_016375391.1.
DR   EnsemblFungi; KIW20451; KIW20451; PV08_01026.
DR   GeneID; 27328109; -.
DR   Proteomes; UP000053328; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053328};
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:UP000053328}.
FT   DOMAIN      127    305       malic. {ECO:0000259|SMART:SM01274}.
FT   DOMAIN      315    570       Malic_M. {ECO:0000259|SMART:SM00919}.
FT   COILED      263    283       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    150    150       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   ACT_SITE    221    221       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   METAL       292    292       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       293    293       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       314    314       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
SQ   SEQUENCE   623 AA;  69504 MW;  EB6C9F053096AA5E CRC64;
     MLYKLSRHSK SRANLNTLIQ SANMTTTSTT QAPIAQSVGS LAAATSSTKA HPPAHHKPKH
     NLPAAHVPNR AAHFDTSLSI PVRKYLQTYG LTPPRAESYE TQKKRCLAQL ASKTTDIERF
     LYLSTLRYNN VHLFYRLLTD HFTELTPLVY TPVVGEACQR WSEIYQQPEG MYLSFEDKGH
     ISAIIQNWPQ KNVEITVVTD GSRILGLGDL GVGGMGIPIG KLALYTGCAG IRPEGTLPLT
     IDLGTSNKAL QEDPLYMGSR RDKVTQQEEI EFLDELMVAL KERWPDIVIQ FEDWKNPFPS
     LERYREDYAM FNDDIQGTGA VIMGGVIGAV KQSGVAAKDH RAVFLGSGSA GVGVAKQIVD
     YFVHEGMTED EAKSCFWLVD SKGLVTQDRG DKLAEHKIYF SRTDNNGQQF KNLDEVIEYV
     KPTIIMGLST IGGAFTPEIL QKMAKWNERP IIFPLSNPSS KSECTFEEAI VNTEGRALFA
     SGSPFQPFTY NGQTYHPGQG NNMYVFPGIG LGTILSKSVQ VTSRMIYASG EALPTMITEE
     EKQLALLYPS VTRIRDVSAR VALYVIRAAQ KDNVDRVHHL RDMDDQTLEA WIKDKMYDPH
     KETQGLEDEV RELVEDFSAV PRL
//
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