ID   I6YG46_MYCTU            Unreviewed;       460 AA.
AC   I6YG46;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 78.
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:CCP46254.1};
GN   OrderedLocusNames=Rv3432c {ECO:0000313|EMBL:CCP46254.1};
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332 {ECO:0000313|EMBL:CCP46254.1, ECO:0000313|Proteomes:UP000001584};
RN   [1] {ECO:0000313|EMBL:CCP46254.1, ECO:0000313|Proteomes:UP000001584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv {ECO:0000313|Proteomes:UP000001584};
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E.III., Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L., Oliver K., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton J.,
RA   Squares R., Squares S., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2] {ECO:0007829|PubMed:21969609}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21969609; DOI=10.1074/mcp.M111.011445;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP46254.1; -; Genomic_DNA.
DR   RefSeq; NP_217949.1; NC_000962.3.
DR   RefSeq; WP_003418277.1; NZ_NVQJ01000027.1.
DR   AlphaFoldDB; I6YG46; -.
DR   SMR; I6YG46; -.
DR   STRING; 83332.Rv3432c; -.
DR   PaxDb; 83332-Rv3432c; -.
DR   DNASU; 887580; -.
DR   GeneID; 887580; -.
DR   KEGG; mtu:Rv3432c; -.
DR   PATRIC; fig|83332.111.peg.3826; -.
DR   TubercuList; Rv3432c; -.
DR   eggNOG; COG0076; Bacteria.
DR   InParanoid; I6YG46; -.
DR   OrthoDB; 3401800at2; -.
DR   PhylomeDB; I6YG46; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
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   1: Evidence at protein level;
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:UP000001584}.
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   460 AA;  50780 MW;  B5DA3156D4C7CB4F CRC64;
     MSRSHPSVPA HSIAPAYTGR MFTAPVPALR MPDESMDPEA AYRFIHDELM LDGSSRLNLA
     TFVTTWMDPE AEKLMAETFD KNMIDKDEYP ATAAIEARCV SMVADLFHAE GLRDHDPTSA
     TGVSTIGSSE AVMLGGLALK WRWRQRVGSW KGRMPNLVMG SNVQVVWEKF CRYFDVEPRY
     LPMERGRYVI TPEQVLAAVD ENTIGVVAIL GTTYTGELEP IAEICAALDK LAAGGGVDVP
     VHVDAASGGF VVPFLHPDLV WDFRLPRVVS INVSGHKYGL TYPGVGFVVW RGPEHLPEDL
     VFRVNYLGGD MPTFTLNFSR PGNQVVGQYY NFLRLGRDGY TKVMQALSHT ARWLGDQLRE
     VDHCEVISDG SAIPVVSFRL AGDRGYTEFD VSHELRTFGW QVPAYTMPDN ATDVAVLRIV
     VREGLSADLA RALHDDAVTA LAALDKVKPG GHFDAQHFAH
//