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Database: UniProt/TrEMBL
Entry: G0S226_CHATD
LinkDB: G0S226_CHATD
Original site: G0S226_CHATD 
ID   G0S226_CHATD            Unreviewed;       579 AA.
AC   G0S226;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   25-OCT-2017, entry version 29.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=CTHT_0015750 {ECO:0000313|EMBL:EGS23086.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Chaetomium.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS23086.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R.,
RA   Devos D.P., Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; GL988039; EGS23086.1; -; Genomic_DNA.
DR   RefSeq; XP_006692078.1; XM_006692015.1.
DR   EnsemblFungi; EGS23086; EGS23086; CTHT_0015750.
DR   GeneID; 18255613; -.
DR   KEGG; cthr:CTHT_0015750; -.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000008066; 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   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
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:UP000008066};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008066}.
FT   MOD_RES     295    295       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   579 AA;  65602 MW;  5128CFDC87CE89E4 CRC64;
     MVHLASVPGP DTRQLAERPK KVQLQLSNDE DDFTTSVYGS RYAAQDLPRH EMPEREMPKE
     VAYRMIKDEL SLDGNPMLNL ASFVTTYMEE EAEKLMTEAF PKNFIDYEEY PQSAEIQNRC
     VSMIARLFHA PEGNSEHAGA IGTSCVGSSE AIMLAVLAMK KRWKNRRLAE GKPCDRPNLV
     MSSAVQVCWE KACRYFEIEE KLVYCTPERY VIDPEETVKL VDENTIGICC ILGTTYTGEY
     EDVKGVNDLL MKKGLNVPIH VDAASGGFVA PFVVPDLEWD FRLEHVVSIN VSGHKYGLVY
     PGIGWVVWRS AEYLPQELVF NINYLGADQA SFTLNFSKGA SQVIGQYYQF IRLGKHGYRA
     IMSNLTRIAD YLSDSLEALG FIIMSKKSGE GLPLVAFRLP PKEDRHYDEF SLAHQLRVRG
     WVVPAYTMAP HTGNMKMLRV VVREDFTKNR CDNLINDIRS SQALLEQMDR ESIKRQEEFI
     HKHHTASGKA THNHPKFRGY RERNTRSKAR QARLTLSAKT AAHHERSFSI EQKRDIKTGQ
     VVSSKTTAVQ TANVGQQATL SLELPGGRQL MTFRISCPM
//
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