ID A0A7I6H9J8_ECOHS Unreviewed; 420 AA. AC A0A7I6H9J8; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 03-AUG-2022, entry version 6. DE RecName: Full=Diaminopimelate decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738}; 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, ECO:0000256|RuleBase:RU003738}; GN Name=lysA {ECO:0000256|HAMAP-Rule:MF_02120, GN ECO:0000313|EMBL:ABV07226.1}; GN ORFNames=EcHS_A2985 {ECO:0000313|EMBL:ABV07226.1}; OS Escherichia coli O9:H4 (strain HS). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=331112 {ECO:0000313|EMBL:ABV07226.1, ECO:0000313|Proteomes:UP000001123}; RN [1] {ECO:0000313|EMBL:ABV07226.1, ECO:0000313|Proteomes:UP000001123} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HS {ECO:0000313|EMBL:ABV07226.1, RC ECO:0000313|Proteomes:UP000001123}; RX PubMed=18676672; DOI=10.1128/JB.00619-08; RA Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F., RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., RA Henderson I.R., Sperandio V., Ravel J.; RT "The pangenome structure of Escherichia coli: comparative genomic analysis RT of E. coli commensal and pathogenic isolates."; RL J. Bacteriol. 190:6881-6893(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: CC Reaction=H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine; CC Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02120, CC ECO:0000256|RuleBase:RU003738}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738}; 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 family. CC LysA subfamily. {ECO:0000256|HAMAP-Rule:MF_02120}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000802; ABV07226.1; -; Genomic_DNA. DR RefSeq; WP_001120711.1; NC_009800.1. DR SMR; A0A7I6H9J8; -. DR KEGG; ecx:EcHS_A2985; -. DR OMA; HGNAKSP; -. DR UniPathway; UPA00034; UER00027. DR Proteomes; UP000001123; Chromosome. DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule. DR CDD; cd06828; PLPDE_III_DapDC; 1. 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 Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP- KW Rule:MF_02120}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_02120, 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}. FT DOMAIN 31..376 FT /note="Orn_DAP_Arg_deC" FT /evidence="ECO:0000259|Pfam:PF00278" FT DOMAIN 33..275 FT /note="Orn_Arg_deC_N" FT /evidence="ECO:0000259|Pfam:PF02784" FT REGION 268..271 FT /note="Pyridoxal phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02120" FT BINDING 227 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02120" FT BINDING 271 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02120" FT BINDING 307 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02120" FT BINDING 311 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02120" FT BINDING 343 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02120" FT BINDING 378 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02120" FT BINDING 378 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02120" FT MOD_RES 54 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02120" SQ SEQUENCE 420 AA; 46177 MW; 0A26ABCFAF8462B5 CRC64; MPHSLFSTDT DLTAENLLRL PAEFGCPVWV YDAQIIRRQI AALKQFDVVR FAQKACSNIH ILRLMREQGV KVDSVSLGEI ERALAAGYNP QTHPDDIVFT ADVIDQATLE RVSELQIPVN AGSVDMLDQL GQVSPGHRVW LRVNPGFGHG HSQKTNTGGE NSKHGIWYTD LPAALDVIQR HHLQLVGIHM HIGSGVDYAH LEQVCGAMVR QVIEFGQDLQ AISAGGGLSV PYQQGEEAVD TEHYYGLWNA AREQIARHLG HPVKLEIEPG RFLVAQSGVL ITQVRSVKQM GSRHFVLVDA GFNDLMRPAM YGSYHHISAL AADGRSLEHA PTVETVVAGP LCESGDVFTQ QEGGNVETRA LPEVKAGDYL VLHDTGAYGA SMSSNYNSRP LLPEVLFDNG QARLIRRRQT IEELLALELL //