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Database: UniProt/TrEMBL
Entry: C9Z0V4_STRSW
LinkDB: C9Z0V4_STRSW
Original site: C9Z0V4_STRSW 
ID   C9Z0V4_STRSW            Unreviewed;       479 AA.
AC   C9Z0V4;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   25-OCT-2017, entry version 56.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=SCAB_39881 {ECO:0000313|EMBL:CBG71067.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG71067.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG71067.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG71067.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H.,
RA   Parry R.J., Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like
RT   biosynthetic cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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; FN554889; CBG71067.1; -; Genomic_DNA.
DR   RefSeq; WP_013001690.1; NC_013929.1.
DR   STRING; 680198.SCAB_39881; -.
DR   EnsemblBacteria; CBG71067; CBG71067; SCAB_39881.
DR   GeneID; 24307487; -.
DR   KEGG; scb:SCAB_39881; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; POG091H06F5; -.
DR   BioCyc; SSCA680198:GJ76-3834-MONOMER; -.
DR   Proteomes; UP000001444; 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:UP000001444};
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:UP000001444}.
FT   MOD_RES     292    292       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   479 AA;  53024 MW;  1D671A808F21953F CRC64;
     MPLHRWDSDD ARDGGNGRKD GHRLAVNPFY GQANPAGGMT EAPPKHRLPD APLPPSTAYQ
     LVHDELMLDG NSRLNLATFV TTWMEPEAGV LMGECRDKNM IDKDEYPRTA ELERRCVSML
     ADLWNAPDPA AAVGCSTTGS SEACMLAGMA LKRRWAKRNA DRYPSADARP NLVMGVNVQV
     CWEKFCNFWE VEARQVPMEG DRFHLDPAAA AALCDENTIG VVGVLGSTFD GSYEPIAELC
     AVLDDLQERT GLNVPVHVDG ASGAMVAPFL DEELVWDFRL PRVASINTSG HKYGLVYPGV
     GWALWRSAEE LPEELVFRVN YLGGDMPTFA LNFSRPGAQV VAQYYTFLRL GREGFRAVQQ
     STRDVATLLA QQVGGFGDFR LLTRGDELPV FAFTTNEDVT AYDVFDVARR MRERGWLVPA
     YTFPENREDL SVLRVVCRNG FTSDLAGLFM EDLGSLLPEL RRQRGPLTRD AGAATGFHH
//
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