ID A0A0M8TR50_9ACTN Unreviewed; 435 AA.
AC A0A0M8TR50;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:KOU70067.1};
GN ORFNames=ADK57_12195 {ECO:0000313|EMBL:KOU70067.1};
OS Streptomyces sp. MMG1533.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU70067.1, ECO:0000313|Proteomes:UP000037741};
RN [1] {ECO:0000313|Proteomes:UP000037741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600183-50};
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000256|RuleBase:RU003737}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOU70067.1}.
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DR EMBL; LGDG01000100; KOU70067.1; -; Genomic_DNA.
DR RefSeq; WP_053749429.1; NZ_LGDG01000100.1.
DR AlphaFoldDB; A0A0M8TR50; -.
DR STRING; 1415546.ADK57_12195; -.
DR PATRIC; fig|1415546.3.peg.2659; -.
DR OrthoDB; 9802241at2; -.
DR Proteomes; UP000037741; Unassembled WGS sequence.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
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; 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 PANTHER; PTHR43727; DIAMINOPIMELATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43727:SF3; DIAMINOPIMELATE DECARBOXYLASE; 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.
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|ARBA:ARBA00023154};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000037741}.
FT DOMAIN 43..290
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 294..386
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 359
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 65
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 435 AA; 46123 MW; A25F29BF5F22EA89 CRC64;
MTNVNASAAE RRERILRAAV VQGLVEPDDA VLAAFVDLDG VAASVAALHA AFPDTVSVLH
TFAAKANCLV PVLEELRTLG MGCEVASAGE LAQALAAGFA PEQIVFDSPA KTRSELTQAL
ELGVAVNADN FQELARIDEI LASRPSASRI GVRLNPQVGG GEIAEMSTAT ATSKFGIPLE
DDGSRGRLLE AYRARPWLTW VHAHVGSQGC PLELIAEGIA QAVAFADEVN LKLGRRQVTG
IDIGGGLPVN FLDDETTPAF EEYVKCLQAH VPALFSGEYR IVTEFGRSLL AKNGFTAACV
EYTKTSGGRP IAITHAGAQV ATRTVFMPSS WPLRLTAHCP DGSLKTGEPV SQDIAGPCCF
AGDLLARARP LPMLAPGDIV SLLDTGAYYS STPFHYNSLP DPAVHGVRID PQGNIEFLPL
RPAETIRHVL ARTGW
//
