ID   Q8EG41_SHEON            Unreviewed;       549 AA.
AC   Q8EG41;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   24-JAN-2024, entry version 113.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:AAN54823.2};
DE            EC=4.1.1.15 {ECO:0000313|EMBL:AAN54823.2};
GN   OrderedLocusNames=SO_1769 {ECO:0000313|EMBL:AAN54823.2};
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN54823.2, ECO:0000313|Proteomes:UP000008186};
RN   [1] {ECO:0000313|EMBL:AAN54823.2, ECO:0000313|Proteomes:UP000008186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1 {ECO:0000313|EMBL:AAN54823.2,
RC   ECO:0000313|Proteomes:UP000008186};
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA   Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA   Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA   Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN54823.2; -; Genomic_DNA.
DR   RefSeq; NP_717379.2; NC_004347.2.
DR   RefSeq; WP_011071894.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EG41; -.
DR   STRING; 211586.SO_1769; -.
DR   PaxDb; 211586-SO_1769; -.
DR   KEGG; son:SO_1769; -.
DR   PATRIC; fig|1028802.3.peg.1449; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   OrthoDB; 9803665at2; -.
DR   PhylomeDB; Q8EG41; -.
DR   BioCyc; SONE211586:G1GMP-1619-MONOMER; -.
DR   Proteomes; UP000008186; 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:0008117; F:sphinganine-1-phosphate aldolase activity; IBA:GO_Central.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0030149; P:sphingolipid catabolic process; IBA:GO_Central.
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; IPR022517; Asp_decarboxylase_pyridox.
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   NCBIfam; TIGR03799; NOD_PanD_pyr; 1.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
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:UP000008186}.
FT   MOD_RES         339
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   549 AA;  61040 MW;  ABF5826111B85418 CRC64;
     MTQKLPRQAT ASEESLMRIF TVPEDADSTL SIIEQKLSED LAGFLGDSIA ALEKPLSEIE
     TDFQTFEIPN QPRFVSDYTD EIMQNLVAHS VHTAAPSFIG HMTSALPYFV LPLSKMMVGL
     NQNLVKIETS KAFTPLERQV LGMMHHLIYA QHDDFYRNWM HSANHSLGAF CSGGTVANIT
     ALWIARNQLL KADGDFKGVT REGLIKALRH YDYDDLAILV SERGHYSLGK AVDLLGIGRD
     NIISIPTDAD NKVDVTQMRK IAVELAHKRI KVMAIVGVAG TTETGNIDPL KQLAALASEL
     NCHFHVDAAW GGASLLSNKY RHLLDGVELA DSVTIDAHKQ MYVPMGAGMV LFKNPEFAHA
     IAHHAEYILR RGSKDLGSQT LEGSRPGMAM LVHACLQIIG RDGYEILINN SLEKARYFAE
     QIDAHPDFEL VTAPELCLLT YRYVPASVQA AMQVAIEQGD KAKLERFNEQ LDGLTQFIQK
     HQREQGKSFV SRTRIQPARY FRQPTVVFRV VLANPLTSHE ILNQVLIEQG EIATLDKEFL
     PALLAMVAE
//