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Database: UniProt/TrEMBL
Entry: F8MQT7_NEUT8
LinkDB: F8MQT7_NEUT8
Original site: F8MQT7_NEUT8 
ID   F8MQT7_NEUT8            Unreviewed;       521 AA.
AC   F8MQT7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   25-APR-2018, entry version 36.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=NEUTE1DRAFT_84197 {ECO:0000313|EMBL:EGO56717.1};
OS   Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO56717.1, ECO:0000313|Proteomes:UP000008065};
RN   [1] {ECO:0000313|Proteomes:UP000008065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC 2508 / P0657 {ECO:0000313|Proteomes:UP000008065};
RX   PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V.,
RA   Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to
RT   self-fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Genetics 189:55-69(2011).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; GL891305; EGO56717.1; -; Genomic_DNA.
DR   RefSeq; XP_009852290.1; XM_009853988.1.
DR   EnsemblFungi; EGO56717; EGO56717; NEUTE1DRAFT_84197.
DR   GeneID; 20830695; -.
DR   KEGG; nte:NEUTE1DRAFT84197; -.
DR   EuPathDB; FungiDB:NEUTE1DRAFT_84197; -.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000008065; Unassembled WGS sequence.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008065};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     301    301       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   521 AA;  58584 MW;  BB6F246573E1999B CRC64;
     MVHLTIIPKE DEIRDGLDIP LTGALKAVHL QLANDEDRFT TSVYGSKFAA ADLPRHEMPD
     EEMPKEVAYR MIKDELSLDG NPLLNLASFV TTYMEEEAEK LMTESLPKNF IDYEEYPQTA
     DIQNRCVSMI GRLFNAPVKD AEASSAVGTS SVGSSEAIML GVLAMKKRWK NKRIAEGKPV
     DKPNLIMSSA VQVCWEKATR YFEVEEKFVY CTPDRYVIDP KETVDLVDEN TIGICCILGT
     TYTGEYEDVK AVNDLLVERG LDTPIHVDAA SGGFVAPFVV PDLEWDFRLK NVVSINVSGH
     KYGLVYPGVG WVVWRSAEYL PQELVFNINY LGADQASFTL NFSKGASQVI GQYYQLIRLG
     KHGYRAIMSN LTRTADYLAE SLAALGFIIM SQKSGQGLPL VAFRLKEDPD RTYDEFALAH
     QLRVRGWIVP AYTMAPKTEG LKMLRIVVRE DFSRNRCDGL ISDIRSCQGI LEQMDKETVK
     KQQEFIHKHH VVSGKASHNH PKYHKEKHSL QGKTGKTHSI C
//
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