BESC_STREN
ID BESC_STREN Reviewed; 257 AA.
AC F8JJ25; G8XHD6;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=4-chloro-allylglycine synthase {ECO:0000305|PubMed:30867596};
DE EC=1.14.99.- {ECO:0000269|PubMed:30867596};
DE AltName: Full=L-2-amino-4-chloropent-4-enoate synthase {ECO:0000305|PubMed:30867596};
GN Name=besC {ECO:0000303|PubMed:30867596};
GN OrderedLocusNames=SCATT_p06890 {ECO:0000312|EMBL:AEW98882.1};
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, AND DISRUPTION PHENOTYPE.
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 an oxidative
CC C-C bond cleavage in 4-chloro-L-lysine to form 4-chloro-allyl-L-glycine
CC (also named L-2-amino-4-chloropent-4-enoate), with release of
CC formaldehyde and ammonia. Is also able to react with L-lysine directly
CC to produce allylglycine in vitro. {ECO:0000269|PubMed:30867596}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-chloro-L-lysine + AH2 + O2 = A + formaldehyde + H2O + L-2-
CC amino-4-chloropent-4-enoate + NH4(+); Xref=Rhea:RHEA:59888,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:17499, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57555, ChEBI:CHEBI:143276;
CC Evidence={ECO:0000269|PubMed:30867596};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59889;
CC Evidence={ECO:0000269|PubMed:30867596};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:30867596};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:O84616};
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}.
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DR EMBL; CP003229; AEW98882.1; -; Genomic_DNA.
DR RefSeq; WP_014151496.1; NC_017585.1.
DR PDB; 7TWA; X-ray; 1.70 A; A/B/C/D=1-257.
DR PDBsum; 7TWA; -.
DR AlphaFoldDB; F8JJ25; -.
DR SMR; F8JJ25; -.
DR EnsemblBacteria; AEW98882; AEW98882; SCATT_p06890.
DR KEGG; scy:SCATT_p06890; -.
DR PATRIC; fig|1003195.11.peg.1005; -.
DR HOGENOM; CLU_1081474_0_0_11; -.
DR OrthoDB; 1763737at2; -.
DR Proteomes; UP000007842; Plasmid pSCATT.
DR GO; GO:0062146; F:4-chloro-allylglycine synthase activity; 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 GO; GO:0062142; P:L-beta-ethynylserine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0062143; P:L-propargylglycine biosynthetic process; IMP:UniProtKB.
DR Gene3D; 1.20.910.10; -; 1.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR039068; PqqC-like.
DR PANTHER; PTHR40279; PTHR40279; 1.
DR SUPFAM; SSF48613; SSF48613; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Antibiotic biosynthesis; Iron;
KW Metal-binding; Oxidoreductase; Plasmid; Reference proteome.
FT CHAIN 1..257
FT /note="4-chloro-allylglycine synthase"
FT /id="PRO_0000447349"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O84616"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O84616"
FT BINDING 119
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O84616"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O84616"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O84616"
FT BINDING 207
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O84616"
FT BINDING 210
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O84616"
SQ SEQUENCE 257 AA; 29443 MW; 17D4E3036D3C035E CRC64;
MTDLNTPEST SKPVWEHFDH VEPGIRRRIA VADPEIKEYL DGMLARIASH RGVEHPFLNA
YRTTALDPEQ ERHLFSECYY FFRYLPFYIT GMAVKTRDEM ILREIILNVA DEVGSDPTHS
TLFADFLARI GIDKEHLDGY QPLEVTRQLN DGIRHLYTET SINKALGALY ADETMSSIMV
SKINDGLRNQ GYDDDLRHFW QLHIDVEVGH SNSVFNAIAP YVGSKAARAE FEEGVFEFLG
LVERYWDGVR ELVGIGK
