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Database: UniProt
Entry: A0A094JT20_9PEZI
LinkDB: A0A094JT20_9PEZI
Original site: A0A094JT20_9PEZI 
ID   A0A094JT20_9PEZI        Unreviewed;       599 AA.
AC   A0A094JT20;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   23-MAY-2018, entry version 17.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN   ORFNames=V502_07203 {ECO:0000313|EMBL:KFZ12233.1};
OS   Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ12233.1, ECO:0000313|Proteomes:UP000029308};
RN   [1] {ECO:0000313|EMBL:KFZ12233.1, ECO:0000313|Proteomes:UP000029308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A.,
RA   Gerasimov E.S., Kochkina G.A., Ivanushkina N.E., Vasilenko O.V.,
RA   Kondrashov A.S., Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence
RT   of horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KFZ12233.1}.
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DR   EMBL; JPKE01002616; KFZ12233.1; -; Genomic_DNA.
DR   EnsemblFungi; KFZ12233; KFZ12233; V502_07203.
DR   Proteomes; UP000029308; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:EnsemblFungi.
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:UP000029308};
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:UP000029308}.
FT   DOMAIN       92    273       malic. {ECO:0000259|SMART:SM01274}.
FT   DOMAIN      283    541       Malic_M. {ECO:0000259|SMART:SM00919}.
FT   COILED       61     81       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    115    115       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   ACT_SITE    187    187       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   METAL       258    258       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       259    259       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       282    282       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
SQ   SEQUENCE   599 AA;  65626 MW;  54673551EA82B12C CRC64;
     MPPSKDHPSK FSHLPLISSG PEDCAISGTA LLNTPYFNKG SAFPPEERVE FNLTGLLPHN
     VQTLEQQVQR AYQQYSEQQG DLAKNTFMTS MGDQNEVLFY RLIQDHIKEM YPIIYTPTEG
     TAIQNFSRIF RRPVGCFLNI DDTDRVYHDL AQWGEPDDID YIVVTDGEEI LGIGDQGVGG
     ILISTAKLVL TTLCAGIHAN RTLAVGLDCG TDNEKLRNDE LYLGLKQPRV RGEKYDKFVD
     TFVQSARKLY PKAYIHFEDF GLPNARRILD KYRPTMACFN DDVQGTGCVT LAAIMAGLHV
     SKTNLEDVKV VIFGAGTAGI GVADQVRDAI ATESGKSKEE AAKHIWCVDK PGLLLKRHGD
     KINPAQKPYA REDSGWDSDK DIDLLSVIKA VKPHVLIGTS TKPGSFTEEI VKEMASHVPR
     PIIFPLSNPT SLHEANPADL NAWTDGKVLL ATGSPFPPVT LNGTTRDVAE CNNALVFPGI
     GLGAVLSRAH LLSDKMLVAA VKALSAQSPA LKDPARPLLP DVEDVREVSV QIAKAVVRQA
     VKEGLAREEG IPEDEGELDE WIRVQMWEPV YRPLRKVSKK VASRKASGEM GIAGSAAQV
//
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