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Database: UniProt/TrEMBL
Entry: A0A0A0NI60_9ACTN
LinkDB: A0A0A0NI60_9ACTN
Original site: A0A0A0NI60_9ACTN 
ID   A0A0A0NI60_9ACTN        Unreviewed;       423 AA.
AC   A0A0A0NI60;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   25-OCT-2017, entry version 18.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=M271_27055 {ECO:0000313|EMBL:AGP56881.1};
OS   Streptomyces rapamycinicus NRRL 5491.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1343740 {ECO:0000313|EMBL:AGP56881.1, ECO:0000313|Proteomes:UP000030183};
RN   [1] {ECO:0000313|EMBL:AGP56881.1, ECO:0000313|Proteomes:UP000030183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 5491 {ECO:0000313|EMBL:AGP56881.1};
RX   PubMed=23929477;
RA   Baranasic D., Gacesa R., Starcevic A., Zucko J., Blazic M., Horvat M.,
RA   Gjuracic K., Fujs S., Hranueli D., Kosec G., Cullum J., Petkovic H.;
RT   "Draft Genome Sequence of Streptomyces rapamycinicus Strain NRRL 5491,
RT   the Producer of the Immunosuppressant Rapamycin.";
RL   Genome Announc. 1:0-0(2013).
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; CP006567; AGP56881.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGP56881; AGP56881; M271_27055.
DR   KEGG; src:M271_27055; -.
DR   PATRIC; fig|1343740.8.peg.3341; -.
DR   KO; K01580; -.
DR   BioCyc; SRAP1343740:G13G7-5366-MONOMER; -.
DR   Proteomes; UP000030183; 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:UP000030183};
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     239    239       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   423 AA;  47276 MW;  0A40BA414D8637AC CRC64;
     MAPTTAYQFV HDELMLDGNA RQNLATFVTT WMEPQAGRLM SDCFAKNMID KDEYPRTAEL
     ERRCVTMLGH LWHAPDPDAV VGCSTTGSSE ACMLAGMAFK RRWAKRNPVS YPATARPNLV
     MGTNVQVCWE KFCDFWEVEA RQVPMEGDRY HLDPRAAAEL CDENTIGVVA VLGSTFDGSY
     EPVAEVCRAL DDLQERTGLD IPVHVDGASG AMVAPFLDPD LVWDFQLPRV ASINTSGHKY
     GLVYPGVGWA LWRTADALPE ELVFRVDYLG GNMPTFSLNF SRPGSQVAAQ YYTFVRLGRE
     GYRAVQQQTR DVARSLAERI EAFGDFTMLS RGDQLPVFAF TTAEGIRGFD VYDVSRRLRE
     RGWLVPAYTF PPNREDLSVL RVVCRNGFSE DLADLFLGDL GSLLPELRSQ SAPMGKVVKA
     FHH
//
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