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Database: UniProt/TrEMBL
Entry: B1VSF2_STRGG
LinkDB: B1VSF2_STRGG
Original site: B1VSF2_STRGG 
ID   B1VSF2_STRGG            Unreviewed;       475 AA.
AC   B1VSF2;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   25-OCT-2017, entry version 57.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=SGR_4077 {ECO:0000313|EMBL:BAG20906.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG20906.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG20906.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG20906.1; -; Genomic_DNA.
DR   RefSeq; WP_003968251.1; NC_010572.1.
DR   ProteinModelPortal; B1VSF2; -.
DR   STRING; 455632.SGR_4077; -.
DR   EnsemblBacteria; BAG20906; BAG20906; SGR_4077.
DR   GeneID; 6211654; -.
DR   KEGG; sgr:SGR_4077; -.
DR   PATRIC; fig|455632.4.peg.4152; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   Proteomes; UP000001685; 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:UP000001685};
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:UP000001685}.
FT   MOD_RES     288    288       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   475 AA;  52996 MW;  3BF11BB2565BEE35 CRC64;
     MPLHRGAHPE QDEPSEERRR LALNPFFGEA DPTAAMNTAP PRHRLPDGPL PPLTAYRLVH
     DELMLDGNSR LNLATFVTTW MEPQAGVLMG ECRDKNMIDK DEYPRTAELE RRCVAMLADL
     WNAPDPRAAV GCSTTGSSEA CMLAGLALKR RWAKRNADRY PATARPNLVM GVNVQVCWEK
     FCDFWEVEAR LVPMEGERFH LDPAAAAELC DENTIGVVGI LGSTFDGSYE PIAELCAALD
     AFQKRTGLDV PVHVDGASGA MVAPFLDPDL VWDFRLPRVA SINTSGHKYG LVYPGVGWAL
     WRTADALPEE LVFRVNYLGG DMPTFALNFS RPGAQVVAQY YTFLRLGHEG YRAVQQASRD
     VACALARAIE ELGDFRLLTR GDELPVFAFT TNDDVHAYDV FDVSRRLRER GWLVPAYTFP
     ANRQDLSVLR VVCRNGFSSD LAELLIEDLK LLLPELRSQK HPLSHDRAVP TAFHH
//
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