ID   H6LH03_ACEWD            Unreviewed;       470 AA.
AC   H6LH03;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=gad {ECO:0000313|EMBL:AFA47141.1};
GN   OrderedLocusNames=Awo_c03370 {ECO:0000313|EMBL:AFA47141.1};
OS   Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS   / WB1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Acetobacterium.
OX   NCBI_TaxID=931626 {ECO:0000313|EMBL:AFA47141.1, ECO:0000313|Proteomes:UP000007177};
RN   [1] {ECO:0000313|Proteomes:UP000007177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC   {ECO:0000313|Proteomes:UP000007177};
RA   Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA   Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT   "Complete genome sequence of Acetobacterium woodii.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFA47141.1, ECO:0000313|Proteomes:UP000007177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC   {ECO:0000313|Proteomes:UP000007177};
RX   PubMed=22479398; DOI=10.1371/journal.pone.0033439;
RA   Poehlein A., Schmidt S., Kaster A.K., Goenrich M., Vollmers J., Thurmer A.,
RA   Bertsch J., Schuchmann K., Voigt B., Hecker M., Daniel R., Thauer R.K.,
RA   Gottschalk G., Muller V.;
RT   "An ancient pathway combining carbon dioxide fixation with the generation
RT   and utilization of a sodium ion gradient for ATP synthesis.";
RL   PLoS ONE 7:E33439-E33439(2012).
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; CP002987; AFA47141.1; -; Genomic_DNA.
DR   RefSeq; WP_014354744.1; NC_016894.1.
DR   AlphaFoldDB; H6LH03; -.
DR   STRING; 931626.Awo_c03370; -.
DR   KEGG; awo:Awo_c03370; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_9; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000007177; 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:UP000007177}.
FT   MOD_RES         279
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   470 AA;  53079 MW;  8D2069FB923D4B38 CRC64;
     MLHSRPNKDQ LESVYETPVF SNDPLNSTLP KYQLNEESID PELAYLLIKD DLLDEGSARL
     NLATFCQTYM EPAAVRIMSE TLEKNAIDKS EYPQTTDLEN RCVNIIADLW NAPEDSAYIG
     TSTVGSSEAC MLGGLAMKFA WREKAKQAGI DILGRKPNLV ISSGFQVCWE KFCVYWDIEM
     RCVPLDPDHM SLNMDTVMDY VDNDTIGIVA IMGITYTGKY DDVKKLDELV EVYNQTAVIP
     VSIHVDGASG GLFAPFIFPD LEWDFRLKNV ISINTSGHKY GLVYPGIGWI VWKDKCYLPS
     ELIFSVSYLG GDLPTMAINF SRSSSQIIGQ YFNFLSYGYR GYQKIHERTR SVAKYIAAEL
     EQTQLFDIYN DGDNIPIVCW KLKANLDKPW SLYDLADRLR TTGWQVPAYP LPDNLSDLII
     QRVVVRQDLS LQLAISFIND IKASIDALDH AHIIIYGHSD ENKGAMGFTH
//