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Database: UniProt/TrEMBL
Entry: E7AEB8_HAEIF
LinkDB: E7AEB8_HAEIF
Original site: E7AEB8_HAEIF 
ID   E7AEB8_HAEIF            Unreviewed;       415 AA.
AC   E7AEB8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   26-NOV-2014, entry version 22.
DE   RecName: Full=Diaminopimelate decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120};
DE            Short=DAP decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120};
DE            Short=DAPDC {ECO:0000256|HAMAP-Rule:MF_02120};
DE            EC=4.1.1.20 {ECO:0000256|HAMAP-Rule:MF_02120};
GN   Name=lysA {ECO:0000256|HAMAP-Rule:MF_02120};
GN   ORFNames=HICON_06700 {ECO:0000313|EMBL:CBY86133.1};
OS   Haemophilus influenzae F3047.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=935897 {ECO:0000313|EMBL:CBY86133.1, ECO:0000313|Proteomes:UP000006797};
RN   [1] {ECO:0000313|EMBL:CBY86133.1, ECO:0000313|Proteomes:UP000006797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F3047 {ECO:0000313|EMBL:CBY86133.1};
RX   PubMed=22377449; DOI=10.3201/eid1803.110728;
RA   Strouts F.R., Power P., Croucher N.J., Corton N., van Tonder A.,
RA   Quail M.A., Langford P.R., Hudson M.J., Parkhill J., Kroll J.S.,
RA   Bentley S.D.;
RT   "Lineage-specific Virulence Determinants of Haemophilus influenzae
RT   Biogroup aegyptius.";
RL   Emerg. Infect. Dis. 18:449-457(2012).
CC   -!- FUNCTION: Specifically catalyzes the decarboxylation of meso-
CC       diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-
CC       Rule:MF_02120}.
CC   -!- CATALYTIC ACTIVITY: Meso-2,6-diaminoheptanedioate = L-lysine +
CC       CO(2). {ECO:0000256|HAMAP-Rule:MF_02120,
CC       ECO:0000256|RuleBase:RU003738}.
CC   -!- COFACTOR:
CC       Note=Pyridoxal phosphate. {ECO:0000256|HAMAP-Rule:MF_02120,
CC       ECO:0000256|RuleBase:RU003738, ECO:0000256|SAAS:SAAS00069857};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02120}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. LysA subfamily. {ECO:0000256|HAMAP-Rule:MF_02120}.
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DR   EMBL; FQ670204; CBY86133.1; -; Genomic_DNA.
DR   RefSeq; YP_004137818.1; NC_014922.1.
DR   ProteinModelPortal; E7AEB8; -.
DR   EnsemblBacteria; CBY86133; CBY86133; HICON_06700.
DR   GeneID; 10111073; -.
DR   KEGG; hil:HICON_06700; -.
DR   PATRIC; 45234356; VBIHaeInf177079_0420.
DR   HOGENOM; HOG000045070; -.
DR   KO; K01586; -.
DR   BioCyc; HINF935897:GJ9O-395-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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02120};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006797};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|RuleBase:RU003738};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|RuleBase:RU003738};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|RuleBase:RU003738};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|SAAS:SAAS00069977}.
FT   REGION      274    277       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
FT   BINDING     239    239       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
FT   BINDING     277    277       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     313    313       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     317    317       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     345    345       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     372    372       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02120}.
FT   BINDING     372    372       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   MOD_RES      60     60       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
SQ   SEQUENCE   415 AA;  46018 MW;  42A6A6FACF9ED280 CRC64;
     MNFFQYKHNK LYAEDIPIQQ LAEQFGTPLY VYSRATLERH WHAFDSAFGK RPHLICFAVK
     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 NSRARTAEVL VDGDQSYLIR RRETLQELWA LESTI
//
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