ID E1UK81_BACAS Unreviewed; 439 AA.
AC E1UK81;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 01-MAY-2013, entry version 20.
DE RecName: Full=Diaminopimelate decarboxylase;
DE Short=DAP decarboxylase;
DE Short=DAPDC;
DE EC=4.1.1.20;
GN Name=lysA1; Synonyms=lysA; OrderedLocusNames=BAMF_2233;
OS Bacillus amyloliquefaciens (strain ATCC 23350 / DSM 7 / BCRC 11601 /
OS NBRC 15535 / NRRL B-14393).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=692420;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM7;
RX DOI=10.1099/ijs.0.023267-0 ;
RA Borriss R., Chen X., Rueckert C., Blom J., Becker A., Baumgarth B.,
RA Fan B., Pukall R., Schumann P., Sproer C., Junge H., Vater J.,
RA Puhler A., Klenk H.P.;
RT "Relationship of Bacillus amyloliquefaciens clades associated with
RT strains DSM7T and FZB42: a proposal for Bacillus amyloliquefaciens
RT subsp. amyloliquefaciens subsp. nov. and Bacillus amyloliquefaciens
RT subsp. plantarum subsp. nov. based on their discriminating complete
RT genome sequences.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23350 / DSM 7 / BCRC 11601 / NBRC 15535 / NRRL B-14393;
RX PubMed=21262282; DOI=10.1016/j.jbiotec.2011.01.006;
RA Ruckert C., Blom J., Chen X., Reva O., Borriss R.;
RT "Genome sequence of B. amyloliquefaciens type strain DSM7(T) reveals
RT differences to plant-associated B. amyloliquefaciens FZB42.";
RL J. Biotechnol. 155:78-85(2011).
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; FN597644; CBI43359.1; -; Genomic_DNA.
DR RefSeq; YP_003920829.1; NC_014551.1.
DR ProteinModelPortal; E1UK81; -.
DR EnsemblBacteria; CBI43359; CBI43359; BAMF_2233.
DR GeneID; 9781297; -.
DR KEGG; bao:BAMF_2233; -.
DR PATRIC; 42473658; VBIBacAmy172706_2406.
DR HOGENOM; HOG000045071; -.
DR KO; K01586; -.
DR BioCyc; BAMY692420:GHU2-1139-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 290 293 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 248 248 Pyridoxal phosphate; via amide nitrogen
FT (By similarity).
FT BINDING 293 293 Substrate (By similarity).
FT BINDING 330 330 Substrate (By similarity).
FT BINDING 334 334 Substrate (By similarity).
FT BINDING 362 362 Substrate (By similarity).
FT BINDING 390 390 Pyridoxal phosphate (By similarity).
FT BINDING 390 390 Substrate (By similarity).
FT MOD_RES 66 66 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 439 AA; 48559 MW; 2844C263CCF2FD93 CRC64;
MFLHGTSRQN KLGHLEIGGV DALYLVEHYG TPLYVYDVAL IRERAKSFKQ AFIDADLKAQ
VAYASKAFSS VAMIQLAEQE GLSLDVVSGG ELFTAVSAGF PADRIHFHGN NKSREELQMA
LDHQIGCIVV DNFHEISLLA ELCRKSGRAM DVLLRITPGV EAHTHDYITT GQEDSKFGFD
LHNGQIEKAI EQVLQSDHIR LLGVHCHIGS QIFDTAGFVL AAEKIFAKLN EWRESFGFVS
EVLNLGGGFG IRYTEEDEPL HPAVYVEKII EAVKENAELY AFDIPEIWIE PGRSLVGDAG
TTLYTIGSQK EVPGTRKYAA VDGGMSDNIR PALYQAKYEA VSANRISEHH DTTVSIAGKC
CESGDMLIWD IDLPEVKEGD LLAVFCTGAY GYSMANNYNR IPRPAVVFVE DGEAHLVIKR
ETYEDIVKLD LPFKTGVKQ
//
