ID   A0A1X0WEQ4_9GAMM        Unreviewed;       423 AA.
AC   A0A1X0WEQ4;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   08-MAY-2019, entry version 11.
DE   RecName: Full=Diaminopimelate decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};
DE            Short=DAP decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120};
DE            Short=DAPDC {ECO:0000256|HAMAP-Rule:MF_02120};
DE            EC=4.1.1.20 {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};
GN   Name=lysA {ECO:0000256|HAMAP-Rule:MF_02120};
GN   ORFNames=BS640_11765 {ECO:0000313|EMBL:ORJ25288.1};
OS   Rouxiella badensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Rouxiella.
OX   NCBI_TaxID=1646377 {ECO:0000313|EMBL:ORJ25288.1, ECO:0000313|Proteomes:UP000192536};
RN   [1] {ECO:0000313|EMBL:ORJ25288.1, ECO:0000313|Proteomes:UP000192536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100043 {ECO:0000313|EMBL:ORJ25288.1,
RC   ECO:0000313|Proteomes:UP000192536};
RX   PubMed=28100296; DOI=10.1099/ijsem.0.001794;
RA   Le Fleche-Mateos A., Kugler J.H., Hansen S.H., Syldatk C.,
RA   Hausmann R., Lomprez F., Vandenbogaert M., Manuguerra J.C.,
RA   Grimont P.A.;
RT   "Rouxiella badensis sp. nov. and Rouxiella silvae sp. nov. isolated
RT   from peat bog soil in Germany and emendation of the genus
RT   description.";
RL   Int. J. Syst. Evol. Microbiol. 67:1255-1259(2017).
CC   -!- FUNCTION: Specifically catalyzes the decarboxylation of meso-
CC       diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-
CC       Rule:MF_02120}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine;
CC         Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02120,
CC         ECO:0000256|RuleBase:RU003738};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02120,
CC         ECO:0000256|RuleBase:RU003738, ECO:0000256|SAAS:SAAS00373528};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02120}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. LysA subfamily. {ECO:0000256|HAMAP-Rule:MF_02120}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ORJ25288.1}.
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DR   EMBL; MRWE01000017; ORJ25288.1; -; Genomic_DNA.
DR   UniPathway; UPA00034; UER00027.
DR   Proteomes; UP000192536; Unassembled WGS sequence.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   CDD; cd06828; PLPDE_III_DapDC; 1.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_02120; LysA; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR002986; DAP_deCOOHase_LysA.
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   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; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR01048; lysA; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02120};
KW   Complete proteome {ECO:0000313|Proteomes:UP000192536};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|RuleBase:RU003738};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|RuleBase:RU003738};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|RuleBase:RU003738};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|SAAS:SAAS00272807}.
FT   DOMAIN       32    379       Orn_DAP_Arg_deC. {ECO:0000259|Pfam:
FT                                PF00278}.
FT   DOMAIN       47    278       Orn_Arg_deC_N. {ECO:0000259|Pfam:
FT                                PF02784}.
FT   REGION      271    274       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
FT   BINDING     230    230       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
FT   BINDING     274    274       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     310    310       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     314    314       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     346    346       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     381    381       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02120}.
FT   BINDING     381    381       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   MOD_RES      54     54       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
SQ   SEQUENCE   423 AA;  46415 MW;  240195A6E370A6C2 CRC64;
     MPFALNNNEN ALNSANLLSA VKAFGSPVWV YDAQVIEQRI SQLRLFDVIR FAQKASSNIH
     ILRLMREQGV KVDSVSLGEI ERALVAGFKP GYQPGEHSEI VFTADVLDPA TLARVTELSI
     PVNAGSIDML EQIGQQKPGH PVWLRVNPGF GHGHSQKTNT GGENSKHGIW FGDLPLALEK
     IRAYQLKLVG IHMHIGSGVD YQHLEQVCDT MVRQVIELGH DIEAISAGGG LSIPYQFGGE
     SIDTDHYYGL WNRAREQIAA HLGHPVSLEI EPGRFLVAES GVLVAQIRAV KSMGSRHYVL
     VDAGFSDLMR PSMYGSYHHI SVLPADGRDL SEQPQRESVI AGPLCESGDV FTQQAGGGVE
     TRVLPEADIN DYLVFHDTGA YGASMSSNYN SRPLIAEVLF ENGVPRLIRR RQTIEELLAL
     ENI
//