(data stored in SCRATCH zone)

SWISSPROT: Q500B7_PSEU2

ID   Q500B7_PSEU2            Unreviewed;       415 AA.
AC   Q500B7;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 96.
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   OrderedLocusNames=Psyr_0182 {ECO:0000313|EMBL:AAY35255.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35255.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35255.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35255.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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}.
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DR   EMBL; CP000075; AAY35255.1; -; Genomic_DNA.
DR   RefSeq; WP_003401767.1; NC_007005.1.
DR   RefSeq; YP_233293.1; NC_007005.1.
DR   STRING; 205918.Psyr_0182; -.
DR   EnsemblBacteria; AAY35255; AAY35255; Psyr_0182.
DR   GeneID; 3365658; -.
DR   KEGG; psb:Psyr_0182; -.
DR   PATRIC; fig|205918.7.peg.178; -.
DR   eggNOG; ENOG4105CU5; Bacteria.
DR   eggNOG; COG0019; LUCA.
DR   HOGENOM; HOG000045070; -.
DR   KO; K01586; -.
DR   OMA; VVGYICE; -.
DR   BioCyc; PSYR205918:G1G4J-183-MONOMER; -.
DR   UniPathway; UPA00034; UER00027.
DR   Proteomes; UP000000426; Chromosome.
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; IPR022653; De-COase2_pyr-phos_BS.
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; PS00878; ODR_DC_2_1; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q500B7.
DR   SWISS-2DPAGE; Q500B7.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02120};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|RuleBase:RU003738};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738,
KW   ECO:0000313|EMBL:AAY35255.1};
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       30    368       Orn_DAP_Arg_deC. {ECO:0000259|Pfam:
FT                                PF00278}.
FT   DOMAIN       35    280       Orn_Arg_deC_N. {ECO:0000259|Pfam:
FT                                PF02784}.
FT   REGION      273    276       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
FT   COILED      123    143       {ECO:0000256|SAM:Coils}.
FT   BINDING     239    239       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
FT   BINDING     276    276       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     312    312       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     316    316       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     343    343       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     370    370       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02120}.
FT   BINDING     370    370       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   MOD_RES      60     60       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
SQ   SEQUENCE   415 AA;  45211 MW;  C3F8E1BA319B31E6 CRC64;
     MDAFNYRDGE LFAEGVALSA IAERFGTPTY VYSRAHIEAQ YRAYADALSG MPHMVCFAVK
     ANSNLGVLNV LARLGAGFDI VSRGELERVL AAGGKAEKIV FSGVGKTRED MRRALEVGVH
     CFNVESTDEL ERLQEVAAEL NVRAPISLRV NPDVDAGTHP YISTGLKENK FGIAIAAAED
     VYIRASQLPN LEVIGVDCHI GSQLTTLEPF IDALDRLLAL VDRLGDCGIH LHHIDLGGGL
     GVRYRDEEPP LAADYIKAVR ERLAGRDLGL LFEPGRFIVA NAGALLTRVE YLKHTEHKDF
     AIVDAAMNDL IRPALYQAWM DVTAVRPRDS EPRAYDIVGP ICETGDFLAK GRELALAEGD
     LLAVHSAGAY GFVMSSNYNT RGRAAEVLVD GSQAFEVRRR ETVAELFAGE SLLPE
//

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