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Database: UniProt/TrEMBL
Entry: A4SRW8_AERS4
LinkDB: A4SRW8_AERS4
Original site: A4SRW8_AERS4 
ID   A4SRW8_AERS4            Unreviewed;       416 AA.
AC   A4SRW8;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   26-NOV-2014, entry version 56.
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   ECO:0000313|EMBL:ABO91640.1};
GN   OrderedLocusNames=ASA_3679 {ECO:0000313|EMBL:ABO91640.1};
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245 {ECO:0000313|EMBL:ABO91640.1, ECO:0000313|Proteomes:UP000000225};
RN   [1] {ECO:0000313|Proteomes:UP000000225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449 {ECO:0000313|Proteomes:UP000000225};
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A.,
RA   Kimball J., Munholland J., Murphy C., Sarty D., Williams J.,
RA   Nash J.H., Johnson S.C., Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights
RT   into the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(2008).
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; CP000644; ABO91640.1; -; Genomic_DNA.
DR   RefSeq; YP_001143388.1; NC_009348.1.
DR   ProteinModelPortal; A4SRW8; -.
DR   STRING; 382245.ASA_3679; -.
DR   EnsemblBacteria; ABO91640; ABO91640; ASA_3679.
DR   GeneID; 4996032; -.
DR   KEGG; asa:ASA_3679; -.
DR   PATRIC; 20793794; VBIAerSal2987_3652.
DR   eggNOG; COG0019; -.
DR   HOGENOM; HOG000045070; -.
DR   KO; K01586; -.
DR   OMA; HCFNVES; -.
DR   OrthoDB; EOG6Z9B18; -.
DR   BioCyc; ASAL382245:GJJN-3666-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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02120};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000225};
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     240    240       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      61     61       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
SQ   SEQUENCE   416 AA;  45299 MW;  08E79755567AABB5 CRC64;
     MDHFNYDADG QLQAEQTSLQ HLAEQYGTPL YVYSRATLER HWHAFDQAAG DIPHLICYAV
     KANSNLALLN LLARLGSGFD IVSGGELSRV LAAGGDPAKV VFSGVAKSEA EMRLALDKEI
     LCFNLESEAE LERLNRVAGS MGKKARVSVR VNPDIDAGTH PYISTGLKQN KFGIPIEQAP
     AIYRKAAAMA NIEIKGVDCH IGSQLTELNP FMEAADKLLR LIDTLAAEGI HIHHLDVGGG
     LGVNYGAEQP PHPTEYAEAL KQKLAGRDLT LLFEPGRAIV ANAGVLLTRV EYLKPGETRN
     FALIDAGMND LLRPSLYGAW MNIIEVDSRT AHEKALYDVV GPVCETGDFL GKERTLAIAE
     GSLLAVRSAG AYGFTMSSNY NTRPRAAEVL VDGTQSFLIR EREQLADLWR GEHLLP
//
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