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Database: UniProt/TrEMBL
Entry: A5UDZ8_HAEIE
LinkDB: A5UDZ8_HAEIE
Original site: A5UDZ8_HAEIE 
ID   A5UDZ8_HAEIE            Unreviewed;       450 AA.
AC   A5UDZ8;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   19-FEB-2014, entry version 45.
DE   RecName: Full=Diaminopimelate decarboxylase;
DE            Short=DAP decarboxylase;
DE            Short=DAPDC;
DE            EC=4.1.1.20;
GN   Name=lysA; OrderedLocusNames=CGSHiEE_08490;
OS   Haemophilus influenzae (strain PittEE).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374930;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittEE;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R.,
RA   Post J.C., Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12
RT   clinical nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
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; CP000671; ABQ98999.1; -; Genomic_DNA.
DR   RefSeq; YP_001291382.1; NC_009566.1.
DR   ProteinModelPortal; A5UDZ8; -.
DR   STRING; 374930.CGSHiEE_08490; -.
DR   EnsemblBacteria; ABQ98999; ABQ98999; CGSHiEE_08490.
DR   GeneID; 5225887; -.
DR   KEGG; hip:CGSHiEE_08490; -.
DR   PATRIC; 20279566; VBIHaeInf81350_1713.
DR   eggNOG; COG0019; -.
DR   HOGENOM; HOG000045070; -.
DR   KO; K01586; -.
DR   OMA; NKFGIPI; -.
DR   OrthoDB; EOG6Z9B18; -.
DR   ProtClustDB; CLSK870477; -.
DR   BioCyc; HINF374930:GJDD-1563-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   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; SSF50621; 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      274    277       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING     239    239       Pyridoxal phosphate; via amide nitrogen
FT                                (By similarity).
FT   BINDING     277    277       Substrate (By similarity).
FT   BINDING     313    313       Substrate (By similarity).
FT   BINDING     317    317       Substrate (By similarity).
FT   BINDING     345    345       Substrate (By similarity).
FT   BINDING     372    372       Pyridoxal phosphate (By similarity).
FT   BINDING     372    372       Substrate (By similarity).
FT   MOD_RES      60     60       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   450 AA;  50044 MW;  A9B15BA412E286C0 CRC64;
     MNFFQYKNNK LYAEDIPVQQ LAEQFGTPLY VYSRATLERH WHAFDSAFGK HPHLICFAVK
     SCSNIGVLNI MAKLGSGFDI VSQGELERVL AAGGDASKVV FSGVAKSREE IMRALEVGIR
     CFNVESVSEL KHINQIAGEM GKIAPISLRV NPDVDAHTHP YISTGLKENK FGVSVNEARE
     VYKLASTLPN IKITGMDCHI GSQLTELQPF LDATDRLIVL MEQLKEDGIT LKHLDLGGGL
     GVTYTDETPP HPSDYANALL EKLKNYPELE IILEPGRAIS ANAGILVAKV QYLKSNESRN
     FAITDTGMND MIRPALYEAY MNIVEIDRTL EREKAIYDVV GPVCETSDFL GKQRELSIAE
     GDYIAQCSAG AYGASMSSNY NSRARTAEVF SRWRSILFDS SPRNLTGTLG IRIDHLIFLI
     LKKSGKKLSI FLPHFFYFYP SINLPQIVSF
//
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