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
//