ID Q486N2_COLP3 Unreviewed; 420 AA.
AC Q486N2;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 01-MAY-2013, entry version 55.
DE RecName: Full=Diaminopimelate decarboxylase;
DE Short=DAP decarboxylase;
DE Short=DAPDC;
DE EC=4.1.1.20;
GN Name=lysA; OrderedLocusNames=CPS_1240;
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H / ATCC BAA-681;
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic
RT analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ25851.1; -; Genomic_DNA.
DR RefSeq; YP_267983.1; NC_003910.7.
DR ProteinModelPortal; Q486N2; -.
DR STRING; 167879.CPS_1240; -.
DR STRING; Q486N2; -.
DR PRIDE; Q486N2; -.
DR EnsemblBacteria; AAZ25851; AAZ25851; CPS_1240.
DR GeneID; 3520097; -.
DR KEGG; cps:CPS_1240; -.
DR PATRIC; 21465721; VBIColPsy94388_1112.
DR eggNOG; COG0019; -.
DR HOGENOM; HOG000045070; -.
DR KO; K01586; -.
DR OMA; DSGMNDL; -.
DR BioCyc; CPSY167879:GI48-1321-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 374 374 Pyridoxal phosphate (By similarity).
FT BINDING 374 374 Substrate (By similarity).
FT MOD_RES 63 63 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 420 AA; 45533 MW; 0F975CF9E9265963 CRC64;
MTPVSYFPHK NNEMFVENIA LSDIAQHVQT PFYCYSSTAI ETSFQAYKNA FSSQDALICY
AVKANSNQAV LATLAKLGSG ADVVSMGEIR RAITAGIPAD KIVYSGVAKT EEEIHYALSL
GIFQFNVESE PELELISKVA TSLNKTAAIA FRINPDVCAQ THAKISTGKA ENKFGVPISK
ARIAYKRAAS LPGIKVQGVD VHIGSQLTSL APFEEAYQRI AELVNELRAD GHEISVVDVG
GGLGITYLDE IIPSKQSYAD LVKAQLGHLN CKIIIEPGRS LLGNAGILVS SVVFIKNGEE
RQFLILDAGM NDLIRPSMYE AYHQIIAVNK GANELKTYDV VGPVCETGDT FAKARQVHKS
DAGDLIAIMS SGAYGSVMSS SYNTRMLAPE VMVKGNEFAI VKKRPSYEEI IKQDIIPSWL
//
