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Database: UniProt/TrEMBL
Entry: Q82TE0_NITEU
LinkDB: Q82TE0_NITEU
Original site: Q82TE0_NITEU 
ID   Q82TE0_NITEU            Unreviewed;       417 AA.
AC   Q82TE0;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   09-JUL-2014, entry version 73.
DE   RecName: Full=Diaminopimelate decarboxylase;
DE            Short=DAP decarboxylase;
DE            Short=DAPDC;
DE            EC=4.1.1.20;
GN   Name=lysA; OrderedLocusNames=NE1957;
OS   Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / NBRC 14298;
RX   PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA   Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA   Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and
RT   obligate chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(2003).
CC   -!- FUNCTION: Specifically catalyzes the decarboxylation of meso-
CC       diaminopimelate (meso-DAP) to L-lysine (By similarity).
CC   -!- CATALYTIC ACTIVITY: Meso-2,6-diaminoheptanedioate = L-lysine +
CC       CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. LysA subfamily.
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DR   EMBL; AL954747; CAD85868.1; -; Genomic_DNA.
DR   RefSeq; NP_841975.1; NC_004757.1.
DR   ProteinModelPortal; Q82TE0; -.
DR   STRING; 228410.NE1957; -.
DR   EnsemblBacteria; CAD85868; CAD85868; NE1957.
DR   GeneID; 1082915; -.
DR   KEGG; neu:NE1957; -.
DR   PATRIC; 22715221; VBINitEur56163_2196.
DR   HOGENOM; HOG000045070; -.
DR   KO; K01586; -.
DR   OMA; YDAHHEI; -.
DR   OrthoDB; EOG6Z9B18; -.
DR   PhylomeDB; Q82TE0; -.
DR   BioCyc; NEUR228410:GJNO-1994-MONOMER; -.
DR   UniPathway; UPA00034; UER00027.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP.
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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Complete proteome; Decarboxylase; Lyase;
KW   Lysine biosynthesis; Pyridoxal phosphate.
FT   REGION      276    279       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING     242    242       Pyridoxal phosphate; via amide nitrogen
FT                                (By similarity){EA2}.
FT   BINDING     279    279       Substrate (By similarity){EA2}.
FT   BINDING     315    315       Substrate (By similarity){EA2}.
FT   BINDING     319    319       Substrate (By similarity){EA2}.
FT   BINDING     346    346       Substrate (By similarity){EA2}.
FT   BINDING     373    373       Pyridoxal phosphate (By similarity){EA2}.
FT   BINDING     373    373       Substrate (By similarity){EA2}.
FT   MOD_RES      63     63       N6-(pyridoxal phosphate)lysine (By
FT                                similarity){EA2}.
SQ   SEQUENCE   417 AA;  45495 MW;  632E9B56D4E6C5A6 CRC64;
     MSSFSSFEYR DSQLFVESVP LAEIAAKFGT PCYVYSSAAI RTTYQIFDHA FGQRDHLICY
     AVKANSNLAI LNLLARLGSG FDIVSGGELQ RVLKAGGDPQ KTVFSGVGKT PEEIRAALAA
     NILCFNVESE MELMVLNEIA GQMGKIAPVS LRVNPDVDAN THPYISTGMK ENKFGIPAAE
     AGRIYSLAHQ LPHIQVSGLD CHIGSQLTEI APFIEAADKM LDLLARLQTM GVTIKHLDLG
     GGLGIRYDRE SPPSIEAYIK ALCTIAENHP QQLLIEPGRS MVGNAGLLLT RVHYLKHTSH
     RNFAIVDAAM NDMLRPALYQ AYHSILPVTK RTGETKTYQI VGPVCETGDF LGHDRNLALT
     KNDLLAVMSA GAYGMSMSSN YNTRPRAAEV MVDGSTVHLI RARETVEDLY ALEKLPI
//
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