ID   A8H648_SHEPA            Unreviewed;       548 AA.
AC   A8H648;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABV88035.1};
GN   OrderedLocusNames=Spea_2715 {ECO:0000313|EMBL:ABV88035.1};
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579 {ECO:0000313|EMBL:ABV88035.1, ECO:0000313|Proteomes:UP000002608};
RN   [1] {ECO:0000313|EMBL:ABV88035.1, ECO:0000313|Proteomes:UP000002608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1 {ECO:0000313|Proteomes:UP000002608};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000851; ABV88035.1; -; Genomic_DNA.
DR   RefSeq; WP_012155941.1; NC_009901.1.
DR   AlphaFoldDB; A8H648; -.
DR   STRING; 398579.Spea_2715; -.
DR   KEGG; spl:Spea_2715; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000002608; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002608}.
FT   MOD_RES         336
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   548 AA;  60336 MW;  284B6E9DAEB45EE1 CRC64;
     MTARKATASE EALLRIFTVP EAPDSTLSVI EQNISQNLMG FLQESVVAVE KPLSEVELDF
     QQYHIPAAPQ FVSDYADNMM QTLVAHSVHT SAPSFIGHMT SALPYFVLPL SKMMVGLNQN
     LVKIETSKAF TPLERQVLGM MHHLIYNQDE TFYQSWMHSA NVSLGAFCSG GTVANITALW
     TARNQLLKAD GDFKGIAKQG LLKGLRHYGY DDLAILVSER GHYSLAKTAD LLGIGRENII
     QVPTSDDNKV DVVKMREIAE QLDKDNIKVM AIVGVAGTTE TGNIDPLNAL ADLAAELNCH
     FHVDAAWGGA SLLSNKYRHL LAGIERADSV TIDAHKQMYV PMGAGMVIFK DPTFANAIKH
     HAEYILRQGS KDLGSQTLEG SRPGMAMLVH ACLKVIGREG YEILINNSLE KARYFADLIT
     AEADFELVSK PELCLLTYRY VPQSVQIAMA KAREIGDTAT LAQFNGLLDG LTKFVQKTQR
     EQGTSFVSRT RINPESHQLM DLKAVVFRVV LANPLTSHDI LQQVLAEQAQ IAKSETHFLP
     QLLTLAQS
//