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Database: UniProt/TrEMBL
Entry: A0A143C3Q4_9ACTN
LinkDB: A0A143C3Q4_9ACTN
Original site: A0A143C3Q4_9ACTN 
ID   A0A143C3Q4_9ACTN        Unreviewed;       468 AA.
AC   A0A143C3Q4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   25-OCT-2017, entry version 12.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=A4E84_22630 {ECO:0000313|EMBL:AMW12044.1};
OS   Streptomyces sp. S10(2016).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1783515 {ECO:0000313|EMBL:AMW12044.1, ECO:0000313|Proteomes:UP000076096};
RN   [1] {ECO:0000313|EMBL:AMW12044.1, ECO:0000313|Proteomes:UP000076096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S10 {ECO:0000313|EMBL:AMW12044.1,
RC   ECO:0000313|Proteomes:UP000076096};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K.,
RA   Barbian K., Babar A., Rosenke K.;
RL   Submitted (APR-2016) 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; CP015098; AMW12044.1; -; Genomic_DNA.
DR   RefSeq; WP_062928336.1; NZ_CP015098.1.
DR   EnsemblBacteria; AMW12044; AMW12044; A4E84_22630.
DR   KEGG; stsi:A4E84_22630; -.
DR   KO; K01580; -.
DR   Proteomes; UP000076096; 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:UP000076096};
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     281    281       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   468 AA;  51803 MW;  C44BEFA7F23398AE CRC64;
     MPLHEGPHRA AGRRMSVNPF YGPANPLGDM AEAPPTHRLP DQPMAPSTAH QLVRDELMLD
     GNARLNLATF VTTWMEPEAG VLMAECRDKN MIDKDEYPRT AELERRCVAM LADLWNAPDP
     ATAVGCSTTG SSEACMLAGM ALKRRWAKRN ADRYPGARPN LVMGVNVQVC WEKFCNFWEV
     EARLVPMEGE RFHLDPQAAA ELCDENTIGV VGILGSTFDG SYEPVADLCA ALDALRERTG
     LDIPVHVDGA SGAMVAPFLD EDLVWDFRLP RVASINTSGH KYGLVYPGVG WALWRDAEAL
     PEELVFRVNY LGGDMPTFAL NFSRPGAQVV AQYYTFLRLG RDGYRAVQQA ARDVATGLAG
     RVEALGDFRL LTRGDELPVF AFTTAPDVTA YDVFDVSRRL RENGWLVPAY TFPPNREDLS
     VLRVVCRNGF SADLAELLAQ DLERLLPDLR RQPRPLTEDK GAATSFHH
//
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