ID Q82TE0_NITEU Unreviewed; 417 AA.
AC Q82TE0;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 01-MAY-2013, entry version 66.
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 HSSP; P31848; 1HKV.
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; AQVFDIV; -.
DR ProtClustDB; CLSK586036; -.
DR BioCyc; NEUR228410:GJNO-1994-MONOMER; -.
DR UniPathway; UPA00034; UER00027.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:HAMAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:HAMAP.
DR Gene3D; 2.40.37.10; -; 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 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; Racem_decarbox_C; 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;
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).
FT BINDING 279 279 Substrate (By similarity).
FT BINDING 315 315 Substrate (By similarity).
FT BINDING 319 319 Substrate (By similarity).
FT BINDING 346 346 Substrate (By similarity).
FT BINDING 373 373 Pyridoxal phosphate (By similarity).
FT BINDING 373 373 Substrate (By similarity).
FT MOD_RES 63 63 N6-(pyridoxal phosphate)lysine (By
FT similarity).
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
//
