(data stored in ACNUC7421 zone)

SWISSPROT: Q750Z9_ASHGO

ID   Q750Z9_ASHGO            Unreviewed;       621 AA.
AC   Q750Z9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 114.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN   ORFNames=AGOS_AGL068W {ECO:0000313|EMBL:AAS54422.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54422.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54422.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54422.2; -; Genomic_DNA.
DR   RefSeq; NP_986598.2; NM_211660.2.
DR   SMR; Q750Z9; -.
DR   STRING; 33169.AAS54422; -.
DR   EnsemblFungi; AAS54422; AAS54422; AGOS_AGL068W.
DR   GeneID; 4622897; -.
DR   KEGG; ago:AGOS_AGL068W; -.
DR   HOGENOM; HOG000042487; -.
DR   InParanoid; Q750Z9; -.
DR   KO; K00027; -.
DR   OMA; WIREQMW; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0004470; F:malic enzyme activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR   GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
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;
DR   PRODOM; Q750Z9.
DR   SWISS-2DPAGE; Q750Z9.
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:UP000000591}.
FT   DOMAIN          116..297
FT                   /note="malic"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          307..561
FT                   /note="Malic_M"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        139
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        211
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   METAL           282
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   METAL           283
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   METAL           306
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
SQ   SEQUENCE   621 AA;  68643 MW;  E2BF4EC653B5C2C8 CRC64;
     MLRCIRRFSS RGAAASAVAT GIPVGREAKR LMSKPLVTRL SVDGPIECPL SGMQLLNSPL
     FNKGSAFTQE ERAAFGLEGL LPPQVNTLDE QVERAYKQLC YLKTPLAKND FMTSMRMQNK
     VLFFELVRRH IRELVPIIYT PTEGDAIAAY SHRFRRPEGV FLDITEPDSI EERLASYGED
     KDVDYVVVSD GEGILGIGDQ GIGGIRIAIS KLALMTLCGG IHPGRVMAVT LDVGTNNKKL
     ARDELYMGNR FARVRGKQYD EFLDKFIKAL KKRFPSAVLH FEDFGVENGR PLLDRYRNEL
     PCFNDDIQGT GAVVMASFLA ALKHTDRNLL DSKVLVYGAG SAGIGIADQI VNHMVSYGAS
     VDEARSKIFT MDRRGLIMDS MRAGSTRAQQ AYAKPDDEWE GVNTKSLVEV VSRIKPTCLI
     GCSTQAGAFN KAVVQEMHKH NERPIIFPLS NPTRLHEAVP EDLLEWTNYQ ALVATGSPFH
     PVNGYRISEN NNCFSFPGIG LGAVLARATI ISDKMISAAV DQLASLSPLK PGDSRPGLLP
     PLEVINDTSA KVATAVILQA LEEGLARVEH EAVPNSTLGE RVRVPRDFDK CLEWVKVQMW
     KPVYRPLLKV QHDPSVHTFQ H
//

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