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Database: UniProt
Entry: Q8P6B5_XANCP
LinkDB: Q8P6B5_XANCP
Original site: Q8P6B5_XANCP 
ID   Q8P6B5_XANCP            Unreviewed;       427 AA.
AC   Q8P6B5;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:AAM42326.1};
GN   Name=lysA {ECO:0000313|EMBL:AAM42326.1};
GN   OrderedLocusNames=XCC3055 {ECO:0000313|EMBL:AAM42326.1};
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM42326.1, ECO:0000313|Proteomes:UP000001010};
RN   [1] {ECO:0000313|EMBL:AAM42326.1, ECO:0000313|Proteomes:UP000001010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25
RC   {ECO:0000313|Proteomes:UP000001010};
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F.Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A.Jr., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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; AE008922; AAM42326.1; -; Genomic_DNA.
DR   RefSeq; NP_638402.1; NC_003902.1.
DR   RefSeq; WP_011038170.1; NC_003902.1.
DR   AlphaFoldDB; Q8P6B5; -.
DR   STRING; 190485.XCC3055; -.
DR   EnsemblBacteria; AAM42326; AAM42326; XCC3055.
DR   KEGG; xcc:XCC3055; -.
DR   PATRIC; fig|190485.4.peg.3263; -.
DR   eggNOG; COG0019; Bacteria.
DR   HOGENOM; CLU_026444_0_3_6; -.
DR   OrthoDB; 9802241at2; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IBA:GO_Central.
DR   CDD; cd06843; PLPDE_III_PvsE_like; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022657; De-COase2_CS.
DR   InterPro; IPR022644; De-COase2_N.
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; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001010}.
FT   DOMAIN          28..376
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   DOMAIN          36..284
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   REGION          407..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        349
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   427 AA;  45993 MW;  9261F31E2A2C9B0F CRC64;
     MSLQIDATAV RAAVAQLRAH SDAPLCAYVY DLAALDAHAA WMRAQLPPGC TLFYAAKANA
     EPQILQTLAP YVDGFEAASG GELAWLHQQQ PDAALLFGGP GKLESELAQA VRLPDCTVHV
     ESLGELQRLA AIARQIAQPD RRRIPVFLRM NIAVPGAQTT RLMMGGQPSP FGLDPDDLDA
     ALLQLRASPA LELRGFHFHL MSHQRDAAAQ LHLIAAYLRT VQHWRQRHGL GPLLVNAGGG
     FGVDYLTPEA SFDWAGFCAG LPAVLHAHGD GLQLRLEPGR YVSASCGWYL MEVLDIKRSH
     GAWFAIARGG THHFRTPAAQ GHDHPCVVVR GTHAPVLRDT PVTLVGQLCT PKDVLARNQR
     VAALAPGDCL AFPLAGAYAW NISHQQFLMH PPPQMVFLPV HAQATATTGT RMSARRSASA
     TVSGSSR
//
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