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Database: UniProt
Entry: A0A0W7X7R9_9ACTN
LinkDB: A0A0W7X7R9_9ACTN
Original site: A0A0W7X7R9_9ACTN 
ID   A0A0W7X7R9_9ACTN        Unreviewed;       416 AA.
AC   A0A0W7X7R9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Diaminopimelate decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AT728_06225 {ECO:0000313|EMBL:KUF18658.1};
OS   Streptomyces silvensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1765722 {ECO:0000313|EMBL:KUF18658.1, ECO:0000313|Proteomes:UP000054804};
RN   [1] {ECO:0000313|EMBL:KUF18658.1, ECO:0000313|Proteomes:UP000054804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53525 {ECO:0000313|EMBL:KUF18658.1,
RC   ECO:0000313|Proteomes:UP000054804};
RA   Johnston C.W., Li Y., Magarvey N.A.;
RT   "Draft genome sequence of Streptomyces silvensis ATCC 53525, a producer of
RT   novel hormone antagonists.";
RL   Submitted (DEC-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:KUF18658.1}.
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DR   EMBL; LOCL01000029; KUF18658.1; -; Genomic_DNA.
DR   RefSeq; WP_058846815.1; NZ_LOCL01000029.1.
DR   AlphaFoldDB; A0A0W7X7R9; -.
DR   STRING; 1765722.AT728_06225; -.
DR   OrthoDB; 9802241at2; -.
DR   Proteomes; UP000054804; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR002433; Orn_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
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; PR01179; ODADCRBXLASE.
DR   PRINTS; PR01182; ORNDCRBXLASE.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054804}.
FT   DOMAIN          26..275
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          276..376
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        349
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         48
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   416 AA;  43688 MW;  33B399E93FD7E0B6 CRC64;
     MTENAFLLNL AARYGTPLYA YDLPAVRRAA AALRSDLPAG SRILYSVKAN PHPLLIETLR
     TEGCEAEVSS VGELAVAIAA GHAPERVLYS GPGKSPSDLR TALASGVRTF SVESVTDRQR
     LDALAQDADV RCDYLVRLNG PAGSVHGSLR MSGSASAFGA DVADMEALRA LLTVRSRTRP
     IGLHTFFATN IGNEDSLIAE FQQAVRTVSE VCRETEFVPH MIDLGGGFPA PQAAPGGVTR
     HPRLASAVEG ALDAHLVTRR TSGVEIAFES GRYLVGAAGT LITEVLDVKR SRGRTFAVLD
     TGVNALGGMS GLGRLMAPQA RPYRLAPAPT RDVPSGDEPC PVTLVGPLCT PLDVLNRSVD
     LGEVRVGDLL AVPNVGAYGL TASLVGFLSH PLPTEIVHDG GTVVAARRLA LAEVHL
//
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