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Database: UniProt
Entry: A0A2A3HI41_9ACTN
LinkDB: A0A2A3HI41_9ACTN
Original site: A0A2A3HI41_9ACTN 
ID   A0A2A3HI41_9ACTN        Unreviewed;       456 AA.
AC   A0A2A3HI41;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:PBC67382.1};
GN   ORFNames=BX265_7975 {ECO:0000313|EMBL:PBC67382.1};
OS   Streptomyces sp. TLI_235.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938860 {ECO:0000313|EMBL:PBC67382.1, ECO:0000313|Proteomes:UP000218662};
RN   [1] {ECO:0000313|EMBL:PBC67382.1, ECO:0000313|Proteomes:UP000218662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TLI_235 {ECO:0000313|EMBL:PBC67382.1,
RC   ECO:0000313|Proteomes:UP000218662};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2017) 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:PBC67382.1}.
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DR   EMBL; NSGV01000004; PBC67382.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3HI41; -.
DR   Proteomes; UP000218662; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022657; De-COase2_CS.
DR   InterPro; IPR022644; De-COase2_N.
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; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218662}.
FT   DOMAIN          46..296
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          297..391
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        364
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         70
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   456 AA;  48088 MW;  F1337F0649EAE725 CRC64;
     MESTHEHEGL RRIDAHRRDR VVRAAAAAGL VGERHVAAGF LDVDGVRRTV ADLHAAFGPD
     VPVLHTFAVK AAALVPVLRL VADAGMGCEV ASPGELALAR AAGIPAHRIV LDSPAKTDAE
     LAEALGLGVA VNADNLQELE RTAALLAVHR SASVLGLRVN PQVGAGTIGA MSTASEHSKF
     GVPLRDPGAR ERVLDAFDRY PWLTRLHVHV GSQGCWPDLI AAGVRATWEL AEEVNRRAGR
     RQVTSVDLGG GLPVNFDDDE VRPTHAEYAA HLRAAVPGLF GGDYSLVTEF GRSVVAKHGF
     TAARVEYTKE VGGRRIALTH AGAHLATRTV FMPDAWPLRV GVHHPDGTPR RGPEEVQDVA
     GPCCFAGDLV ARGRALPRIE PGDLVVLHDT GGYYTSAPWA YNSIARPAVH GFTTAGGQVR
     FATVRTEQTL AEIAAEAGGA HADTLTSLAR GGPGGR
//
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