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Database: UniProt/TrEMBL
Entry: A0A0C5VCE3_PROFF
LinkDB: A0A0C5VCE3_PROFF
Original site: A0A0C5VCE3_PROFF 
ID   A0A0C5VCE3_PROFF        Unreviewed;       470 AA.
AC   A0A0C5VCE3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   25-OCT-2017, entry version 17.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=RM25_2222 {ECO:0000313|EMBL:AJQ91926.1};
OS   Propionibacterium freudenreichii subsp. freudenreichii.
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Propionibacterium.
OX   NCBI_TaxID=66712 {ECO:0000313|EMBL:AJQ91926.1, ECO:0000313|Proteomes:UP000032238};
RN   [1] {ECO:0000313|EMBL:AJQ91926.1, ECO:0000313|Proteomes:UP000032238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6207 / DSM 20271 / LMG 16412 / NBRC 12424 / NCIMB 5959 /
RC   NCTC 10470 / NRRL B-3523 {ECO:0000313|Proteomes:UP000032238};
RA   Koskinen P., Deptula P., Smolander O.-P., Kammonen J., Savijoki K.,
RA   Paulin L., Piironen V., Auvinen P., Varmanen P.;
RT   "Complete genome sequence of Propionibacterium freudenreichii DSM
RT   20271T.";
RL   Submitted (DEC-2014) 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; CP010341; AJQ91926.1; -; Genomic_DNA.
DR   EnsemblBacteria; AJQ91926; AJQ91926; RM25_2222.
DR   KEGG; pfre:RM25_2222; -.
DR   PATRIC; fig|66712.6.peg.2272; -.
DR   KO; K01580; -.
DR   Proteomes; UP000032238; 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:UP000032238};
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     283    283       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   470 AA;  52977 MW;  155688CE14FA649E CRC64;
     MNDPTRHPTY SIDRSQLGAV EINPVFARPA EATEFSKFRL PASESLPETA YQVVHDEAML
     DGNARLNLAT FVGTWMDGYA NRLYAESADK NMIDKDEYPK TAEIETRCWT MLADLWHAPD
     PDNTIGTSTI GSSEACMLGG LALKRRWQHA RKAAGKPTDH PNMVMSSAVQ VCWEKFCNYW
     DIEPRYVPIS EDHKVLDGTN LADYVDENTI GVVAIMGVTY TGMYEPVKQI AAALDEIQER
     TGLDVKIHVD AASGGMIAPF IQPDLEWDFR VERVASINTS GHKYGLVYPG LGWVVWRSVD
     DLPEDLIFKV SYLGGDMPTF ALNFSRPGAQ VLLQYYMFLR LGMDGFRRVQ TNSHDVAKFL
     SSQIGAMDDF ELWNDGSDIP VFAWRLKDRP NRKWDLYDLS ERLRTRGWLV PAYPMPADLT
     DVTVQRIVVR NGLSHDLADA FLESMRAEVA YLDALPAPMP SQHKQSGFHH
//
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