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Database: UniProt/TrEMBL
Entry: K8EEF3_CARML
LinkDB: K8EEF3_CARML
Original site: K8EEF3_CARML 
ID   K8EEF3_CARML            Unreviewed;       467 AA.
AC   K8EEF3;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   20-JUN-2018, entry version 37.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=gadB {ECO:0000313|EMBL:CCO10173.1};
GN   ORFNames=BN424_690 {ECO:0000313|EMBL:CCO10173.1};
OS   Carnobacterium maltaromaticum LMA28.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1234679 {ECO:0000313|EMBL:CCO10173.1, ECO:0000313|Proteomes:UP000000212};
RN   [1] {ECO:0000313|Proteomes:UP000000212}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMA28 {ECO:0000313|Proteomes:UP000000212};
RX   PubMed=23405327; DOI=10.1128/genomeA.00115-12;
RA   Cailliez-Grimal C., Chaillou S., Anba-Mondoloni J., Loux V.,
RA   Afzal M.I., Rahman A., Kergourlay G., Champomier-Verges M.C.,
RA   Zagorec M., Dalgaard P., Leisner J.J., Prevost H.,
RA   Revol-Junelles A.M., Borges F.;
RT   "Complete Chromosome Sequence of Carnobacterium maltaromaticum LMA
RT   28.";
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; HE999757; CCO10173.1; -; Genomic_DNA.
DR   RefSeq; WP_015075600.1; NC_019425.2.
DR   EnsemblBacteria; CCO10173; CCO10173; BN424_690.
DR   GeneID; 35881233; -.
DR   KEGG; cml:BN424_690; -.
DR   PATRIC; fig|1234679.3.peg.663; -.
DR   KO; K01580; -.
DR   OrthoDB; POG091H06F5; -.
DR   Proteomes; UP000000212; 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:UP000000212};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:CCO10173.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000212}.
FT   MOD_RES     278    278       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   467 AA;  53319 MW;  922195170A184C23 CRC64;
     MLYGKEDQTK KNDYLEPIFG TGAEEQEIPK YKLGKNPIEP RVAYRLVKDE FLDEGNARQN
     LATFCQTYME DEAALLMAET LEKNAIDKSE YPRTAELENR CVNILADLWN APKEKSYTGT
     STVGSSEACM LAGMAMKFRW RNQAKKLGLN IQAASPNLVI SSGYQVCWEK FCVYWDIEMR
     TVPMDEKHMS MDMDKVMDYV DEYTIGIVGI LGITYTGKYD DIKALDALVE TYNSQTDYKI
     SIHVDGASGA MFAPFIEPKL QWDFRLKNVA SINTSGHKYG LVYPGIGWVL WRDKAYLPEE
     LVFNVSYLGG EMPTMAINFS RSASQIIGQY YNFLRFGFEG YRAIHQRTKD VAMYLAAEVE
     KTGLFKMYND GVNLPIVCYA LKVETEVEWT LYDLADRLLM KGWQVPAYPL PADLEDVLVQ
     RYVVRADFGM NTAVDFMEDF NEALKELNQA HVLFHSKEEH GAQGFTH
//
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