ID A0A126V2N0_9RHOB Unreviewed; 464 AA.
AC A0A126V2N0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ORFNames=RC74_13750 {ECO:0000313|EMBL:AML52195.1};
OS Falsihalocynthiibacter arcticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Falsihalocynthiibacter.
OX NCBI_TaxID=1579316 {ECO:0000313|EMBL:AML52195.1, ECO:0000313|Proteomes:UP000070371};
RN [1] {ECO:0000313|EMBL:AML52195.1, ECO:0000313|Proteomes:UP000070371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 20958 {ECO:0000313|EMBL:AML52195.1};
RA Lee Y.M., Baek K., Lee H.K., Shin S.C.;
RT "Complete genome sequence of Halocynthiibacter arcticus PAMC 20958t from
RT arctic marine sediment.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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; CP014327; AML52195.1; -; Genomic_DNA.
DR RefSeq; WP_039000394.1; NZ_CP014327.1.
DR AlphaFoldDB; A0A126V2N0; -.
DR STRING; 1579316.RC74_13750; -.
DR KEGG; hat:RC74_13750; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000070371; 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 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:UP000070371}.
FT MOD_RES 273
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 464 AA; 51538 MW; 4DAC060BA956B74E CRC64;
MVDTTKTPAP SNHFDEIYGS DEMSVPLSES IFPGSESDPR NVYASIRDEL MLDGNSRQNL
ATFCQTWEEP EIHQLMDDCI DKNMVDKDEY PQTAEIEQRC VRMLADLWNA PSGAATGCST
TGSSEAAMLG GLAMKRRWEA RRKAEGKPID KPNLITGPVQ VCWHKFTRYW DVEHREIPME
NGRLLMTPEE VLSLCDENTI GVVPTLGVTF TGQYEPVEAV SAALDKYEAE TGLDIPIHVD
GASGGFLAPF CAPELMWDFR LPRVKSINAS GHKFGLAPLG VGWIVWRSAD DLPENLVFWV
NYLGGNMRDI GLNFSRPGGP ITCQYYNFQR LGREGYTKIH KACYATAQYL AAEIGALGPF
DIVYDGDMTS GIPALCWTLK PDVDLGFTLF DLADRLRIYG WQVPAYTLPA NCQTQAIQRI
LVRNGVSRDL ATLLMRDIRK ALAHLTKHPA ETPLGENAAG GFHH
//