ID K8EEF3_CARML Unreviewed; 467 AA.
AC K8EEF3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, 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; Bacillota; 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., Afzal M.I.,
RA Rahman A., Kergourlay G., Champomier-Verges M.C., Zagorec M., Dalgaard P.,
RA Leisner J.J., Prevost H., Revol-Junelles A.M., Borges F.;
RT "Complete Chromosome Sequence of Carnobacterium maltaromaticum LMA 28.";
RL Genome Announc. 1:0-0(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00000018,
CC ECO:0000256|RuleBase:RU361171};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; HE999757; CCO10173.1; -; Genomic_DNA.
DR RefSeq; WP_015075600.1; NC_019425.2.
DR AlphaFoldDB; K8EEF3; -.
DR STRING; 1234679.BN424_690; -.
DR KEGG; cml:BN424_690; -.
DR PATRIC; fig|1234679.3.peg.663; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_019582_2_1_9; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000000212; Chromosome.
DR GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
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 CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.160; -; 1.
DR Gene3D; 4.10.280.50; -; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43321:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000000212}.
FT MOD_RES 278
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="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
//