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Database: UniProt/TrEMBL
Entry: A0A1V0V7B2_9ACTN
LinkDB: A0A1V0V7B2_9ACTN
Original site: A0A1V0V7B2_9ACTN 
ID   A0A1V0V7B2_9ACTN        Unreviewed;       475 AA.
AC   A0A1V0V7B2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   22-NOV-2017, entry version 5.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=B7C62_14605 {ECO:0000313|EMBL:ARF73364.1};
OS   Kitasatospora albolonga.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Kitasatospora.
OX   NCBI_TaxID=68173 {ECO:0000313|EMBL:ARF73364.1, ECO:0000313|Proteomes:UP000192251};
RN   [1] {ECO:0000313|EMBL:ARF73364.1, ECO:0000313|Proteomes:UP000192251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 101047 {ECO:0000313|EMBL:ARF73364.1,
RC   ECO:0000313|Proteomes:UP000192251};
RA   Yin M., Jiang Y.;
RT   "The complete genome sequence of Streptomyces albolongus YIM 101047,
RT   the producer of novel bafilomycins and novel odoriferous
RT   sesquiterpenoids.";
RL   Submitted (APR-2017) 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; CP020563; ARF73364.1; -; Genomic_DNA.
DR   KEGG; kab:B7C62_14605; -.
DR   KO; K01580; -.
DR   Proteomes; UP000192251; 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:UP000192251};
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}.
FT   MOD_RES     288    288       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   475 AA;  53060 MW;  7C56F923AB966BEE CRC64;
     MPLHRGAHPQ RDEHSEERLR LALNPFYGEA DPTGAMNTAP PRHKLPDGPL PPLTAYRLVH
     DELMLDGNSR LNLATFVTTW MEPQAGVLMG ECQDKNMIDK DEYPRTAELE RRCVAMLADL
     WHAPDPATAV GCSTTGSSEA CMLAGLALKR RWAKRNADRY PATARPNLVM GVNVQVCWEK
     FCNFWEVEAR QVPMDGERFH LDPQAAAELC DENTIGVVGI LGSTFDGSYE PIADLCAALD
     ALQERTGLDI PVHVDGASGA MVAPFLDPDL TWDFRLPRVS SINTSGHKYG LVYPGVGWAL
     WRTSDELPEE LVFRVNYLGG DMPTFALNFS RPGAQVVAQY YTFLRLGRDG YRAVQQSARD
     VARGLSRSVE ELGDFRLLTR GDELPVFAFT TNPDVHAYDV FDVSRRLREH GWLVPAYTFP
     ANRQDLSVLR VVCRNGFSSD LAALLIEDLK LLLPELRAQK HPLSHDRAVR TAFHH
//
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