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Database: UniProt
Entry: B0SPX6_LEPBP
LinkDB: B0SPX6_LEPBP
Original site: B0SPX6_LEPBP 
ID   B0SPX6_LEPBP            Unreviewed;       422 AA.
AC   B0SPX6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   13-SEP-2023, entry version 96.
DE   SubName: Full=Diaminopimelate decarboxylase (DAP decarboxylase) {ECO:0000313|EMBL:ABZ97542.1};
DE            EC=4.1.1.20 {ECO:0000313|EMBL:ABZ97542.1};
GN   Name=lysA {ECO:0000313|EMBL:ABZ97542.1};
GN   OrderedLocusNames=LEPBI_I1434 {ECO:0000313|EMBL:ABZ97542.1};
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ97542.1, ECO:0000313|Proteomes:UP000001847};
RN   [1] {ECO:0000313|EMBL:ABZ97542.1, ECO:0000313|Proteomes:UP000001847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris
RC   {ECO:0000313|Proteomes:UP000001847};
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600183-50};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       {ECO:0000256|RuleBase:RU003737}.
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DR   EMBL; CP000786; ABZ97542.1; -; Genomic_DNA.
DR   RefSeq; WP_012388421.1; NC_010602.1.
DR   AlphaFoldDB; B0SPX6; -.
DR   STRING; 456481.LEPBI_I1434; -.
DR   KEGG; lbi:LEPBI_I1434; -.
DR   HOGENOM; CLU_026444_0_2_12; -.
DR   OMA; YCRSMAS; -.
DR   OrthoDB; 9802241at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS07035-MONOMER; -.
DR   Proteomes; UP000001847; Chromosome I.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR   CDD; cd06828; PLPDE_III_DapDC; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR002986; DAP_deCOOHase_LysA.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR43727; DIAMINOPIMELATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43727:SF2; DIAMINOPIMELATE DECARBOXYLASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR   PRINTS; PR01181; DAPDCRBXLASE.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:ABZ97542.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT   DOMAIN          44..272
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          273..373
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        339
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         57
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   422 AA;  46784 MW;  5D9174E13F3F7D35 CRC64;
     MTSIEKLKFL KEDQVRTLAK EFGTPLFVYS EKEIEQKCDD TLAFPNAFGL QVRYAMKANP
     NSNILQIMKK KGILIDASSE HEVVRALHFG FSPESIMLTS QEFPKAFVEL IGKGVKFNAC
     SLRQLELFGQ HFPGKSVSIR FNPGLGSGHT KKTDVGGVTS SFGIWHEKLE EVKAIVNKYN
     LVVEKVHTHI GSGSDPEVWK AVAKYTLEYA ESFPSVTVVS LGGGYKVGRM EDEKSTNLQT
     IGAPVKIQFE EFAKKHGRKL ILEIEPGTYL IALCGALLTT VDDKVDTGKH GFQFLKLDTG
     MDSNTRPSLY GARHPLITVK KDGGIPSSHK EYVVVGHCCE SGDVFTQKEG GEPITRLMGE
     AEIGDYVVME AIGAYCSSMS TKNYNSFPET AEVLLRKNGE TKLIRKKEPV MEIFRNEILV
     VE
//
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