BESD_STREN
ID BESD_STREN Reviewed; 242 AA.
AC G8XHD5;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=L-lysine 4-chlorinase {ECO:0000305|PubMed:30867596};
DE EC=1.14.20.- {ECO:0000269|PubMed:30867596};
DE AltName: Full=Halogenase BesD {ECO:0000303|PubMed:30867596};
GN Name=besD {ECO:0000303|PubMed:30867596};
GN OrderedLocusNames=SCATT_p06880 {ECO:0000312|EMBL:AEW98881.1};
OS Streptomyces cattleya (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC
OS 14057 / NRRL 8057).
OG Plasmid pSCATT.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1003195;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057;
RA Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLY-129.
RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057;
RX PubMed=30867596; DOI=10.1038/s41586-019-1020-y;
RA Marchand J.A., Neugebauer M.E., Ing M.C., Lin C.I., Pelton J.G.,
RA Chang M.C.Y.;
RT "Discovery of a pathway for terminal-alkyne amino acid biosynthesis.";
RL Nature 567:420-424(2019).
CC -!- FUNCTION: Involved in the biosynthesis of terminal alkyne-containing
CC amino acids such as L-propargylglycine (Pra) and L-beta-ethynylserine,
CC that are produced as antibiotics by S.cattleya. Catalyzes the
CC chlorination of L-lysine at the C4 position, leading to the production
CC of 4-chloro-L-lysine. {ECO:0000269|PubMed:30867596}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + chloride + H(+) + L-lysine + O2 = 4-chloro-L-
CC lysine + CO2 + H2O + succinate; Xref=Rhea:RHEA:59884,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:32551, ChEBI:CHEBI:143276;
CC Evidence={ECO:0000269|PubMed:30867596};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59885;
CC Evidence={ECO:0000269|PubMed:30867596};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:30867596};
CC -!- PATHWAY: Amino-acid metabolism. {ECO:0000269|PubMed:30867596}.
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:30867596}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene no longer produce
CC detectable amounts of L-propargylglycine and L-beta-ethynylserine, that
CC are terminal alkyne-containing amino acids produced by wild-type
CC S.cattleya. {ECO:0000269|PubMed:30867596}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate/Fe-dependent halogenase
CC family. {ECO:0000305|PubMed:30867596}.
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DR EMBL; CP003229; AEW98881.1; -; Genomic_DNA.
DR PDB; 6NIE; X-ray; 1.95 A; A/B/C/D=2-242.
DR PDBsum; 6NIE; -.
DR AlphaFoldDB; G8XHD5; -.
DR SMR; G8XHD5; -.
DR EnsemblBacteria; AEW98881; AEW98881; SCATT_p06880.
DR KEGG; scy:SCATT_p06880; -.
DR PATRIC; fig|1003195.29.peg.6483; -.
DR HOGENOM; CLU_097175_0_0_11; -.
DR Proteomes; UP000007842; Plasmid pSCATT.
DR GO; GO:0062147; F:L-lysine 4-chlorinase activity; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0062142; P:L-beta-ethynylserine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0062143; P:L-propargylglycine biosynthetic process; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Antibiotic biosynthesis; Iron;
KW Oxidoreductase; Plasmid; Reference proteome.
FT CHAIN 1..242
FT /note="L-lysine 4-chlorinase"
FT /id="PRO_0000447350"
FT MUTAGEN 129
FT /note="G->D: Loss of chlorination activity."
FT /evidence="ECO:0000269|PubMed:30867596"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:6NIE"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:6NIE"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:6NIE"
FT HELIX 31..48
FT /evidence="ECO:0007829|PDB:6NIE"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:6NIE"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6NIE"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:6NIE"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:6NIE"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:6NIE"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:6NIE"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:6NIE"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:6NIE"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:6NIE"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:6NIE"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:6NIE"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:6NIE"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:6NIE"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:6NIE"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:6NIE"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:6NIE"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6NIE"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:6NIE"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:6NIE"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:6NIE"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:6NIE"
SQ SEQUENCE 242 AA; 27858 MW; 6FC4A54FB75DAE70 CRC64;
MCAPLEKDDI RRLSQAFHRF GIVTVTELIE PHTRKLVRAE ADRLLDQYAE RRDLRLATTD
YTRRSMSVVP SETIAANSEL VTGLYAHREL LAPLEAIAGE RLHPCPKADE EFLITRQEQR
GDTHGWHWGD FSFALIWVLQ APPIDVGGLL QCVPHTTWDK ASPQINRYLV ENPIDTYHFE
SGDVYFLRTD TTLHRTIPLR EDTTRIILNM TWAGERDLSR KLAADDRWWD NAEVSAARAI
KD
