ID U5WT60_MYCKA Unreviewed; 460 AA.
AC U5WT60;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 55.
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=MKAN_20150 {ECO:0000313|EMBL:AGZ52354.1};
OS Mycobacterium kansasii ATCC 12478.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=557599 {ECO:0000313|EMBL:AGZ52354.1, ECO:0000313|Proteomes:UP000017786};
RN [1] {ECO:0000313|EMBL:AGZ52354.1, ECO:0000313|Proteomes:UP000017786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12478 {ECO:0000313|EMBL:AGZ52354.1,
RC ECO:0000313|Proteomes:UP000017786};
RG McGill University Mycobacterium genome consortium;
RA Veyrier F.J., Behr M.A.;
RT "Genome sequence of Mycobacterium kansasii.";
RL Submitted (OCT-2013) 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; CP006835; AGZ52354.1; -; Genomic_DNA.
DR RefSeq; WP_023371123.1; NC_022663.1.
DR AlphaFoldDB; U5WT60; -.
DR GeneID; 29701905; -.
DR KEGG; mkn:MKAN_20150; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_019582_2_1_11; -.
DR OrthoDB; 3401800at2; -.
DR Proteomes; UP000017786; 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}.
FT MOD_RES 277
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 460 AA; 50823 MW; 25F7B2319BAABAA9 CRC64;
MSRSHPSVPA HSIAPAYTGR MFTAPIPALR LPEESMDPEA AYQFIHDELM LDGSSRLNLA
TFVTTWMDPE AGQLMAETFD KNMIDKDEYP ATAAIESRCV SMVADLFHAE GLRDDDPGSA
TGVSTIGSSE AVMLGGLAMK WRWRARTKDW KGRTPNLVMG SNVQVVWEKF CRYFDVEPRY
LPMEKGRYVI TPEQVIDAVD EDTIGVVAIL GTTYTGELEP VAEICAALDG LAARGGVDVP
VHVDAASGGF VVPFLHPDLQ WDFRLPRVVS INVSGHKYGL TYPGVGFVVW RGPEYLPEEL
VFRVNYLGGD MPTFTLNFSR PGNQVVGQYY NFLRLGREGY TKVMQALSQT ARWLGEQLEG
AEHCELISDG SAIPVVAFRL AGDRGYTEFD LSHELRTCGW QVPAYTMPDN ATDISVLRIV
VREGLSADLA RALHDDISTA VRTLDKVKPG GHYDAQHFAH
//
