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Database: UniProt/TrEMBL
Entry: N0CSY9_9ACTN
LinkDB: N0CSY9_9ACTN
Original site: N0CSY9_9ACTN 
ID   N0CSY9_9ACTN            Unreviewed;       475 AA.
AC   N0CSY9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   25-OCT-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=SFUL_3078 {ECO:0000313|EMBL:AGK78014.1};
OS   Streptomyces fulvissimus DSM 40593.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1303692 {ECO:0000313|EMBL:AGK78014.1, ECO:0000313|Proteomes:UP000013304};
RN   [1] {ECO:0000313|EMBL:AGK78014.1, ECO:0000313|Proteomes:UP000013304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40593 {ECO:0000313|EMBL:AGK78014.1,
RC   ECO:0000313|Proteomes:UP000013304};
RA   Myronovskyi M., Tokovenko B., Manderscheid N., Petzke L.,
RA   Luzhetskyy A.;
RT   "Complete genome sequence of Streptomyces fulvissimus.";
RL   Submitted (APR-2013) 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; CP005080; AGK78014.1; -; Genomic_DNA.
DR   RefSeq; WP_015609372.1; NC_021177.1.
DR   EnsemblBacteria; AGK78014; AGK78014; SFUL_3078.
DR   KEGG; sfi:SFUL_3078; -.
DR   PATRIC; fig|1303692.3.peg.3098; -.
DR   KO; K01580; -.
DR   OrthoDB; POG091H06F5; -.
DR   Proteomes; UP000013304; 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:UP000013304};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:AGK78014.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     288    288       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   475 AA;  52983 MW;  C7F40F8C171FDE68 CRC64;
     MPLHRGAHPQ RDEHSDERRR LALNPFFGEA DPTAAMNTAP PRHRLPDGPL PPLTAYRLVH
     DELMLDGNSR LNLATFVTTW MEPQAGVLMG ECQDKNMIDK DEYPRTAELE RRCVAMLADL
     WNAPDPAAAV GCSTTGSSEA CMLAGLALKR RWAKRNADRY PATARPNLVM GVNVQVCWDK
     FCNFWEVEAR QVPMDGERFH LDPQAAAELC DENTIGVVGI LGSTFDGSYE PIADLCAALD
     ALQERTGLDI PVHVDGASGA MVAPFLDPDL EWDFRLPRVS SINTSGHKYG LVYPGVGWAL
     WRTADELPEE LVFRVNYLGG DMPTFALNFS RPGAQVVAQY YTFLRLGHDG YRAVQQASRD
     VACSLARAVE ELGDFRLLTR GDELPVFAFT TKPEVHAYDV FDVSRRLREH GWLVPAYTFP
     AHREDLSVLR VVCRNGFSSD LAALLIEDLK LLLPELRAQK HPLSHDRATV TAFHH
//
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