ID   B8CRI9_SHEPW            Unreviewed;       548 AA.
AC   B8CRI9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ACJ29997.1};
DE            EC=4.1.1.15 {ECO:0000313|EMBL:ACJ29997.1};
GN   OrderedLocusNames=swp_3293 {ECO:0000313|EMBL:ACJ29997.1};
OS   Shewanella piezotolerans (strain WP3 / JCM 13877).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225849 {ECO:0000313|EMBL:ACJ29997.1, ECO:0000313|Proteomes:UP000000753};
RN   [1] {ECO:0000313|EMBL:ACJ29997.1, ECO:0000313|Proteomes:UP000000753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP3 / JCM 13877 {ECO:0000313|Proteomes:UP000000753};
RX   PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA   Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA   Bartlett D.H., Yu J., Hu S., Xiao X.;
RT   "Environmental adaptation: genomic analysis of the piezotolerant and
RT   psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT   WP3.";
RL   PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ29997.1; -; Genomic_DNA.
DR   RefSeq; WP_020913347.1; NC_011566.1.
DR   AlphaFoldDB; B8CRI9; -.
DR   STRING; 225849.swp_3293; -.
DR   KEGG; swp:swp_3293; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000000753; 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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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}.
FT   MOD_RES         336
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   548 AA;  60694 MW;  3D4D1B3D6FC498BD CRC64;
     MTPRRATASE EALLRIFTVP EAPDSTLSVI EQNISQNLMG FLQESVVAVE KPLTEIELDF
     QQHQIPAAPQ FVSDYADDMM QTLVAHSVHT SAPSFIGHMT SALPYFVLPL SKMMVGLNQN
     LVKIETSKAF TPLERQVLGM MHHLIYAEND DFYQNWMHSA NVSLGAFCSG GTVANITALW
     TARNQLLKAD GNYRGVAAQG VMKGLRHYGY DDLAILVSER GHYSLGKTAD LLGIGRENII
     QVPTAEDNKV DVSKMRKLAN QLAADKIKVM AIVGVAGTTE TGNIDPLNEL ADLASELNCH
     FHVDAAWGGA SLLSEKYRHL LAGIERADSV TIDAHKQMYV PMGAGMVIFK DPTFANAIKH
     HAEYILRKGS KDLGSQTLEG SRPGMAMLVH ACLKVIGRDG YEILINNSLE KARYFADLIN
     QHQDFELVSK PELCLLTYRY VPQKVQIAMA NARANNDVDK LSEFNSLLDG LTKFVQKRQR
     EQGTSFVSRT RINPEKAHLM DIKAVVFRVV LANPLTTPEI LQQVLAEQKV IASQEQRFLP
     NLLALAER
//