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Database: UniProt/TrEMBL
Entry: M9TTL1_9ACTN
LinkDB: M9TTL1_9ACTN
Original site: M9TTL1_9ACTN 
ID   M9TTL1_9ACTN            Unreviewed;       474 AA.
AC   M9TTL1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, 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=F750_3277 {ECO:0000313|EMBL:AGJ55746.1};
OS   Streptomyces sp. PAMC 26508.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1265601 {ECO:0000313|EMBL:AGJ55746.1, ECO:0000313|Proteomes:UP000012995};
RN   [1] {ECO:0000313|EMBL:AGJ55746.1, ECO:0000313|Proteomes:UP000012995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC26508 {ECO:0000313|EMBL:AGJ55746.1,
RC   ECO:0000313|Proteomes:UP000012995};
RA   Shin S.C., Park H.;
RT   "Genome sequence of Streptomyces sp. PAMC26508, isolated from
RT   Antarctic lichen Cladonia borealis.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003990; AGJ55746.1; -; Genomic_DNA.
DR   RefSeq; WP_015577711.1; NC_021055.1.
DR   EnsemblBacteria; AGJ55746; AGJ55746; F750_3277.
DR   KEGG; strp:F750_3277; -.
DR   PATRIC; fig|1265601.4.peg.3116; -.
DR   KO; K01580; -.
DR   OrthoDB; POG091H06F5; -.
DR   BioCyc; SSP1265601:G13G3-3275-MONOMER; -.
DR   Proteomes; UP000012995; Chromosome.
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:UP000012995};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:AGJ55746.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     287    287       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   474 AA;  52952 MW;  3D8B89B6FC5A4C1D CRC64;
     MALHQGRHGR PAPSEEHRRL ALNPFFGEAD PTAPMVAAPP THRLPEDPLP PSTAYRLVHD
     ELMLDGNSRL NLATFVTTWM EPQAGVLMSE CRDKNMIDKD EYPRTAELER RCVAMLADLW
     NAPDPASTVG CSTTGSSEAC MLAGMALKRR WSAKNADRYP ATARPNLVMG VNVQVCWEKF
     CTFWEVEPRQ VPMDGERFHL DPQAAAELCD ENTIGVVGIL GSTFDGSYEP IADLCAALDD
     LQERTGLDIP VHVDGASGAM IAPFLDPDLV WDFRLPRVSS INTSGHKYGL VYPGVGWALW
     RSPAELPEEL VFRVNYLGGD MPTFALNFSR PGAQVVAQYY TFLRLGREGY RAVQQASRDI
     ARRLAVQFEA LEDFRLLTRG DELPVFAVTT KPDVQAYDVF DVSRRLRERG WLVPAYTFPA
     NRQDLSVLRV VCRNGFSSDL AELLLDDLRG LLPELRSQPH PLHRDPGVQT AFHH
//
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