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Database: UniProt/TrEMBL
Entry: A0A1B2I7Z4_9BACT
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Original site: A0A1B2I7Z4_9BACT 
ID   A0A1B2I7Z4_9BACT        Unreviewed;       463 AA.
AC   A0A1B2I7Z4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   20-JUN-2018, entry version 14.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=BED41_13890 {ECO:0000313|EMBL:ANZ46092.1};
OS   Cloacibacillus porcorum.
OC   Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae;
OC   Cloacibacillus.
OX   NCBI_TaxID=1197717 {ECO:0000313|EMBL:ANZ46092.1, ECO:0000313|Proteomes:UP000093044};
RN   [1] {ECO:0000313|EMBL:ANZ46092.1, ECO:0000313|Proteomes:UP000093044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL-84 {ECO:0000313|EMBL:ANZ46092.1,
RC   ECO:0000313|Proteomes:UP000093044};
RA   Looft T., Bayles D.O., Alt D.P.;
RT   "Complete genome of Cloacibacillus porcorum.";
RL   Submitted (AUG-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; CP016757; ANZ46092.1; -; Genomic_DNA.
DR   RefSeq; WP_066747595.1; NZ_CP016757.1.
DR   EnsemblBacteria; ANZ46092; ANZ46092; BED41_13890.
DR   KEGG; cpor:BED41_13890; -.
DR   KO; K01580; -.
DR   Proteomes; UP000093044; 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   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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:UP000093044};
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     273    273       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   463 AA;  52290 MW;  312A1F239394720B CRC64;
     MSLYQKEYEH RAIDPTFGSA AMSSLLPKDA FPEAEMNPQD AYQAIHNELV LDGNASQNLA
     TFCQTWLDDE THKLMDECID KNMIDKDEYP QTAELEARCV RMLGNLWNSP EEANTIGTST
     TGSSEAAMLG GLAALWRWRK KRKAQGKPTD KPNIVTGAVQ ICWDKFARYW DIEQRQIPMK
     PGKYCMTPEE VVKYVDENTI CVVPTLGLTF TLQYEPVKQI AAALDKLQQE TGLDIPIHVD
     GASGGFIAPF IHRDLVWDFR IERVKSINAS GHKFGLSPLG VGWVMWREVS DLPEELIFYV
     NYLGGNMPTF ALNFSRPAGQ IVSQYYNFIR LGKEGYTKIQ QECAETGQYL ANEIMKFGIF
     EMVYDGEGGV PGCTWKFRDD VKPGFSLYDL ADKLRSRGWQ VPAYSLPADA QNIVVQRILV
     RKGFNIDMAS LLVEDMKRAL EYFKAHPVAK PLTEAETGNF KHS
//
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