ID   DCSA_STRLA              Reviewed;         265 AA.
AC   D2Z024;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Putative N(omega)-hydroxy-L-arginine synthase DcsA;
GN   Name=dcsA;
OS   Streptomyces lavendulae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11924;
RX   PubMed=20086163; DOI=10.1128/aac.01226-09;
RA   Kumagai T., Koyama Y., Oda K., Noda M., Matoba Y., Sugiyama M.;
RT   "Molecular cloning and heterologous expression of a biosynthetic gene
RT   cluster for the antitubercular agent D-cycloserine produced by Streptomyces
RT   lavendulae.";
RL   Antimicrob. Agents Chemother. 54:1132-1139(2010).
RN   [2]
RP   FUNCTION, COFACTOR, AND DISRUPTION PHENOTYPE.
RX   PubMed=22547619; DOI=10.1128/aac.00614-12;
RA   Kumagai T., Takagi K., Koyama Y., Matoba Y., Oda K., Noda M., Sugiyama M.;
RT   "Heme protein and hydroxyarginase necessary for biosynthesis of D-
RT   cycloserine.";
RL   Antimicrob. Agents Chemother. 56:3682-3689(2012).
CC   -!- FUNCTION: Involved in the biosynthesis of the antibiotic D-cycloserine
CC       (DCS), a cyclic structural analog of D-alanine, used as an
CC       antitubercular agent. Could catalyze the production of N(omega)-
CC       hydroxy-L-arginine (NHA) from L-arginine.
CC       {ECO:0000269|PubMed:22547619}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000269|PubMed:22547619};
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not produce
CC       cycloserine (DCS). {ECO:0000269|PubMed:22547619}.
CC   -!- SIMILARITY: Belongs to the DcsA family. {ECO:0000305}.
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DR   EMBL; AB516431; BAI70375.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2Z024; -.
DR   PRIDE; D2Z024; -.
DR   KEGG; ag:BAI70375; -.
DR   BioCyc; MetaCyc:MON-18020; -.
DR   GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
DR   InterPro; IPR014988; Uncharacterised_YqcI/YcgG.
DR   PANTHER; PTHR40045; PTHR40045; 1.
DR   Pfam; PF08892; YqcI_YcgG; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Heme; Iron; Metal-binding.
FT   CHAIN           1..265
FT                   /note="Putative N(omega)-hydroxy-L-arginine synthase DcsA"
FT                   /id="PRO_0000424060"
SQ   SEQUENCE   265 AA;  29723 MW;  CF9583A50D6DC92F CRC64;
     MNCYPAGHLL GKGHVQLNES GENAELISQE QIGDDLNGWH RDAFEDIASR LTDPGFPCVF
     SRNAFRKKLV KFVFVEGSGK EDIRHLGAGL KDYVELSRDW DGALDTAYPL VVVFSADAVT
     ADSVEQYHAF GWWVLQELHA IDPTPWPEGV DKGPQSEAWS MCFHGMPLFI NMSSPAHQVR
     RSRNLGRHFA LVINPRERFD VFAGDTPSGR KVRSNIRGRI ARYDGTPHAQ QLGSYGTGAL
     EWMQYGLVEE NRERADVCPF TFRGA