ID   A9KWF3_SHEB9            Unreviewed;       549 AA.
AC   A9KWF3;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABX48776.1};
GN   OrderedLocusNames=Sbal195_1603 {ECO:0000313|EMBL:ABX48776.1};
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599 {ECO:0000313|EMBL:ABX48776.1, ECO:0000313|Proteomes:UP000000770};
RN   [1] {ECO:0000313|EMBL:ABX48776.1, ECO:0000313|Proteomes:UP000000770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195 {ECO:0000313|EMBL:ABX48776.1,
RC   ECO:0000313|Proteomes:UP000000770};
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-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; CP000891; ABX48776.1; -; Genomic_DNA.
DR   RefSeq; WP_006085345.1; NC_009997.1.
DR   AlphaFoldDB; A9KWF3; -.
DR   GeneID; 11771838; -.
DR   KEGG; sbn:Sbal195_1603; -.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   Proteomes; UP000000770; 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}.
FT   MOD_RES         339
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   549 AA;  60644 MW;  BC8A753AAABCB4CE CRC64;
     MTQKLPRQAT ASEESLLRIF TAPEDAGSTL SIIEQKLSED LAGFLGDSIA ALEKPLSEIE
     TDFQAFEIPT QPRFVSDYTD EIMQNLVAHS VHTAAPSFIG HMTSALPYFV LPLSKMMVGL
     NQNLVKIETS KAFTPLERQV LGMMHHLIYD QDTDFYQSWM HSANHSLGAF CSGGTVANIT
     ALWIARNQLL KADGEFKGVS REGLLKALRH YGYDDLAILV SERGHYSLGK AVDLLGIGRD
     NIISIPTGID NKVDVAKMRQ AALELASKNI KVLAIVGVAG TTETGNVDPL TELAALAKEL
     NCHFHVDAAW GGASLLSNKY RHLLTGIELA DSVTIDAHKQ MYVPMGAGMV LFKDPEFAHA
     IAHHAEYILR RGSKDLGSQT LEGSRPGMAM LVHACLQIIG RDGYEILINN SLEKARYFAE
     QIKAHKDFEL VTEPELCLLT YRYVPACVQA AIQLACEQAD TIRVARFNEL LDGLTQFIQK
     HQREQGKSFV SRTRIQPARY FRQATVVFRV VLANPLTSHD ILNQVLVEQS EIAALDNEFL
     PVLMAMVAD
//