ID   Q2LV45_SYNAS            Unreviewed;       572 AA.
AC   Q2LV45;
DT   21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   21-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:ABC77952.1};
DE            EC=4.1.1.15 {ECO:0000313|EMBL:ABC77952.1};
GN   ORFNames=SYN_00664 {ECO:0000313|EMBL:ABC77952.1};
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC77952.1, ECO:0000313|Proteomes:UP000001933};
RN   [1] {ECO:0000313|EMBL:ABC77952.1, ECO:0000313|Proteomes:UP000001933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB {ECO:0000313|EMBL:ABC77952.1,
RC   ECO:0000313|Proteomes:UP000001933};
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CP000252; ABC77952.1; -; Genomic_DNA.
DR   RefSeq; WP_011417973.1; NC_007759.1.
DR   AlphaFoldDB; Q2LV45; -.
DR   STRING; 56780.SYN_00664; -.
DR   KEGG; sat:SYN_00664; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_7; -.
DR   InParanoid; Q2LV45; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000001933; 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:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010977; Aromatic_deC.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
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:UP000001933}.
FT   MOD_RES         353
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   572 AA;  65332 MW;  FB48932CD50872E0 CRC64;
     MNSLRTDNIP PPRKIETTLE YMHKLFIMPN SSDRFIEFGD LLLDMIHDFF QQKGGIHSEI
     PLKKLAKIFN NIDIPQNQML IRDVLQEIKG NIINHSVKVA NPYYIGHMTS AIPYFMILLE
     MIAVSLNQNQ VKIESAKAST FVEREFLCWM HRLVYQNPSQ FYKKNIQNHR FALGNITSDG
     TVANMTALAL AVAKAFPPDG KRFEGIRNEG LPRSLEYYGY RQALVLVSRR GHYSICKIGS
     ILGIGSKGVV FSPVHPYTNK ADIDKLWQTI EKIRKEDKRV GKPSRFLALV GIAGTTETGN
     IDNLDAMAGV ARELNAHYHV DAAWGGGALL MENGRELFTG IDKADSVSLD AHKLLFSPNA
     MGICLFKNID DSLKLYHTSN YIIRKGSVDL GRFTLEGPRP FACLKPWAAM KIIGRRGYEL
     IFLHACGLQD IFITLIKNDP QFELLNTPEL FIINYRFVPK ELREMLDRLM LDPRANAEKI
     TQINNVVNEI NVELHKKIRV RDTSFVSRTR LESTRYSPRK IVVLRAITIN PNTEPHMLEQ
     ILVEHRLLGE QIWQDRNLLR KTLHICNKLI DV
//