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Database: UniProt/TrEMBL
Entry: G0S000_CHATD
LinkDB: G0S000_CHATD
Original site: G0S000_CHATD 
ID   G0S000_CHATD            Unreviewed;       824 AA.
AC   G0S000;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   07-JUN-2017, entry version 26.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=CTHT_0008220 {ECO:0000313|EMBL:EGS23161.1};
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:EGS23161.1, 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; GL988037; EGS23161.1; -; Genomic_DNA.
DR   RefSeq; XP_006691352.1; XM_006691289.1.
DR   EnsemblFungi; EGS23161; EGS23161; CTHT_0008220.
DR   GeneID; 18254860; -.
DR   KEGG; cthr:CTHT_0008220; -.
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     300    300       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   824 AA;  93575 MW;  4B62DF4A4569311B CRC64;
     MSLARHVNPE DIIHHLQHED TGPLIAQAIP GSSHLTPFST PYASRRDIPK YRIPQHGTPG
     DTVYQMLKDE LDLDGRPNLN LASFVNTYLE DNAKSLLSAN ANKNLADNDE YPALLDLSKR
     CVSILAHLWG VQKGEKAVGS PTVGSSEAIH LGGLAMKRSW QQRRREQGKD ASRPNIIMGA
     NAQVALEKFA RYFDVEARIL PVSAKSKYRL DPELVRENVD ENTIGVFVIL GSTYTGHYEP
     VEEVAQVLDE YQKNTGIDIP IHVDAASGGF VAPFTFAGAG GAKWNFEIPR VHSINTSGHK
     YGLVTAGLGW IIWRDEAYLP QDLIFKLHYL GGTEESFTLN FSRPGAQVVV QYYNFIHLGF
     DGYREAMENC LANARMLSKS LEETGWYTCV SDIHRPVQGK REPKGGETSA SYVAGLPVVS
     FRLTDDFRRQ FPHIQQETIS LLLRARQWII PNYALPPNVN STEILRVVVR VNMSLDMLDR
     LITDIVQVTE MLMERDEVDL SVLKEQRERR EEVQEKDKEH RRQKHRRDKV EGVEKKRMEE
     GIHRGPVPTE FIHPNQIFFK ETTTSIYQER RRPRGELVAL GEVLPRQEGE TLGQWISRLE
     MVRDMTLDWA EQYEMSKLAS RLGSRSASPE NLDYFYSKQS PQVHLPTLWK LCGAIPREFP
     QDEDKIEEVA ARSTDEHYLA RFTTIFRNAL SKSQVRISSL APGSPPGQLT QGSDIEPTTN
     QRPRAPALKK ATDSLIIHRN RKLFKRALKF LDRFPDDEEA QEEYITLWLE DTHLRSKDTS
     QVTLHAALIS SKIDSSNDEG NDMDESSFLD FDLDGWIEKC FGAL
//
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