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Database: UniProt
Entry: A0A0B5FAX7_STRA4
LinkDB: A0A0B5FAX7_STRA4
Original site: A0A0B5FAX7_STRA4 
ID   A0A0B5FAX7_STRA4        Unreviewed;       420 AA.
AC   A0A0B5FAX7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Diaminopimelate decarboxylase {ECO:0000313|EMBL:AJE87622.1};
GN   ORFNames=SLNWT_7246 {ECO:0000313|EMBL:AJE87622.1};
OS   Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 /
OS   NBRC 107858).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1081613 {ECO:0000313|EMBL:AJE87622.1, ECO:0000313|Proteomes:UP000031523};
RN   [1] {ECO:0000313|EMBL:AJE87622.1, ECO:0000313|Proteomes:UP000031523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858
RC   {ECO:0000313|Proteomes:UP000031523};
RA   Lu C.;
RT   "Enhanced salinomycin production by adjusting the supply of polyketide
RT   extender units in Streptomyce albus DSM 41398.";
RL   Submitted (JAN-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}.
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DR   EMBL; CP010519; AJE87622.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B5FAX7; -.
DR   KEGG; sals:SLNWT_7246; -.
DR   Proteomes; UP000031523; Chromosome.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR   CDD; cd06843; PLPDE_III_PvsE_like; 1.
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; 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   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:UP000031523}.
FT   DOMAIN          30..279
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          280..378
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        351
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         52
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   420 AA;  44002 MW;  C96E7C5FE7106644 CRC64;
     MTLPTPEVRA RVLALSGEEL PAYLYDLAAL RAHLGGIRAA LPEGVELYYA AKANPEVEIL
     GALGPYVDGF EVSSGGESAH VAGAVPGAAL AFGGPGKTPA EIAGALRSGV RRFHAESVHE
     LHLLESLAAT VVPGSRLRVL IRVNLRVEGE ALAGNALAMG GGPTPFGMDP AQADHALALL
     TGGSCPHLEF RGVHAHLASG LAADAQLALA RRVVEWSLAL GRRHRLPVAE VNVGGGMAVD
     YARPGERFDW AAYGAGLARL SAEHEGLRLR IEPGRALTAY CGWYASEVLD VKHSHGEEFA
     VLRGGTHHLR TPATKGHDQP CTVLPSPAPW PHSWPRPAAR GERVTLAGQL CTPKDVLARG
     VPAAGLRAGD RVVFAIAGAY AWNISHHDFL MHPRPGFHFL GREEPGRTAG ADTTGADGAG
//
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