DCSB_STRLA
ID DCSB_STRLA Reviewed; 273 AA.
AC D2Z025;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=N(omega)-hydroxy-L-arginine amidinohydrolase;
DE EC=3.5.3.25;
DE AltName: Full=hydroxyarginase;
GN Name=dcsB;
OS Streptomyces lavendulae.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1914;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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, CATALYTIC ACTIVITY, 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. Catalyzes the hydrolysis of N(omega)-hydroxy-L-
CC arginine (NHA) to yield hydroxyurea (HU) and L-ornithine.
CC {ECO:0000269|PubMed:20086163, ECO:0000269|PubMed:22547619}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega)-hydroxy-L-arginine = hydroxyurea + L-ornithine;
CC Xref=Rhea:RHEA:36791, ChEBI:CHEBI:15377, ChEBI:CHEBI:44423,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:60107; EC=3.5.3.25;
CC Evidence={ECO:0000269|PubMed:22547619};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not produce
CC cycloserine (DCS). {ECO:0000269|PubMed:22547619}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; AB516431; BAI70376.1; -; Genomic_DNA.
DR PDB; 6LUG; X-ray; 1.90 A; A/B=1-273.
DR PDB; 6LUH; X-ray; 1.50 A; A/B=1-273.
DR PDBsum; 6LUG; -.
DR PDBsum; 6LUH; -.
DR AlphaFoldDB; D2Z025; -.
DR SMR; D2Z025; -.
DR KEGG; ag:BAI70376; -.
DR BioCyc; MetaCyc:MON-18017; -.
DR BRENDA; 3.5.3.25; 133.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR43782; PTHR43782; 1.
DR Pfam; PF00491; Arginase; 1.
DR SUPFAM; SSF52768; SSF52768; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Hydrolase; Manganese; Metal-binding.
FT CHAIN 1..273
FT /note="N(omega)-hydroxy-L-arginine amidinohydrolase"
FT /id="PRO_0000424061"
FT BINDING 109
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 109
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 111
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 113
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 198
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 198
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6LUH"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 18..33
FT /evidence="ECO:0007829|PDB:6LUH"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 59..74
FT /evidence="ECO:0007829|PDB:6LUH"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:6LUH"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:6LUH"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:6LUH"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:6LUH"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:6LUH"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:6LUH"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:6LUH"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:6LUH"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:6LUH"
FT HELIX 249..270
FT /evidence="ECO:0007829|PDB:6LUH"
SQ SEQUENCE 273 AA; 28919 MW; 6ACF98FBD56C3C6D CRC64;
MIDLIVSQGR VADRAAWMIE GAARTARALE ERYGLKGHYV GEPAPHADDD WSVALPQARE
TLVAVREAAT ESIKGDNLTV LVNNTCSVSL ATLPVVAREH PDAVVLYIDG HGDFNTPETT
DTGYLGGMVL SGACGLWDSG HGAGLRPEQA VLVGSRDIDE GERELIRKAG VRVIPPGEAT
AQAVLDAVKD APVWIHIDWD VLEPGSIPAD YTVPDGMLPA QIRAVFEAIP AERLIGVELA
ELNAPADSER AEQAVAVILD MVAPAFDAAA ARP
