ID A0A1R4HTJ4_9MICO Unreviewed; 432 AA.
AC A0A1R4HTJ4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Diaminopimelate decarboxylase {ECO:0000256|RuleBase:RU003738};
DE EC=4.1.1.20 {ECO:0000256|RuleBase:RU003738};
GN ORFNames=FM113_10165 {ECO:0000313|EMBL:SJN10806.1};
OS Leucobacter sp. 7(1).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1255613 {ECO:0000313|EMBL:SJN10806.1, ECO:0000313|Proteomes:UP000195513};
RN [1] {ECO:0000313|EMBL:SJN10806.1, ECO:0000313|Proteomes:UP000195513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7(1) {ECO:0000313|Proteomes:UP000195513};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU003738};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600183-50, 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|RuleBase:RU003738}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000256|RuleBase:RU003737}.
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DR EMBL; FUID01000052; SJN10806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4HTJ4; -.
DR OrthoDB; 9802241at2; -.
DR UniPathway; UPA00034; UER00027.
DR Proteomes; UP000195513; Unassembled WGS sequence.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR CDD; cd06828; PLPDE_III_DapDC; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 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; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR01048; lysA; 1.
DR PANTHER; PTHR43727; DIAMINOPIMELATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43727:SF2; DIAMINOPIMELATE DECARBOXYLASE 1, CHLOROPLASTIC-RELATED; 1.
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; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154,
KW ECO:0000256|RuleBase:RU003738};
KW Decarboxylase {ECO:0000256|RuleBase:RU003738};
KW Lyase {ECO:0000256|RuleBase:RU003738, ECO:0000313|EMBL:SJN10806.1};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154,
KW ECO:0000256|RuleBase:RU003738};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000195513}.
FT DOMAIN 54..291
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 292..380
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 353
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 78
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 432 AA; 45527 MW; 33417169E5CCEFFB CRC64;
MAGSGFHDPR FERIFPPNAA VRADGVLEVG GCSVPALAEE FGTPLYVIDE QGLRDRMRAY
REGLAARWPN SQVAFASKSF PVLAAYAVAA AEGLAIDVAG AGELLLALES GAPAELIHLH
GNAKSHEELV LAVEAGIGAI VLDGEADVER LDALLTRPQD VLIRIIPGVD PNVPKAISTG
GVASKFGLPI PQAKALIAKL EAHPFINVVG LHLHIGSQVL EVEPFERAVE AVRELGEFPV
YNIGGGLGVD YNVTHHAPSL DEYLDAITAA ATRVLPAGSR LIIEPGRSLV ARTGMTAYRV
NNVKHTGATF VAVDGGLADQ MNVALMNMEF TPIVADRANA TPDTTAQLVG RQCESGDLLV
DRAELAAPAT GDTIVLAATG AYGYTLSNNY NGALKPAVVF CREGESRLAV RRQTYAEFLG
HHVGPSEEAW AS
//
