ID   BESB_STREN              Reviewed;         500 AA.
AC   G8XHD7;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 2.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=L-2-amino-4-chloropent-4-enoate dechlorinase/desaturase {ECO:0000305|PubMed:30867596};
DE            EC=4.5.1.- {ECO:0000269|PubMed:30867596};
DE   AltName: Full=4-chloro-allyl-L-glycine acetylenase {ECO:0000305|PubMed:30867596};
DE   AltName: Full=L-propargylglycine synthase {ECO:0000305|PubMed:30867596};
GN   Name=besB {ECO:0000303|PubMed:30867596};
GN   OrderedLocusNames=SCATT_p06900 {ECO:0000312|EMBL:AEW98883.1};
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   REACTION MECHANISM.
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 gamma-
CC       elimination of chloride from 4-chloro-allyl-L-glycine (also named L-2-
CC       amino-4-chloropent-4-enoate), followed by an isomerization, to form the
CC       terminal-alkyne product L-propargylglycine.
CC       {ECO:0000269|PubMed:30867596}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-2-amino-4-chloropent-4-enoate = chloride + H(+) + L-
CC         propargylglycine; Xref=Rhea:RHEA:59892, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:57555, ChEBI:CHEBI:143285;
CC         Evidence={ECO:0000269|PubMed:30867596};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59893;
CC         Evidence={ECO:0000269|PubMed:30867596};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
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. They accumulate the intermediate 4-chloro-allyl-L-glycine.
CC       {ECO:0000269|PubMed:30867596}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AEW98883.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP003229; AEW98883.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_042507713.1; NC_017585.1.
DR   AlphaFoldDB; G8XHD7; -.
DR   SMR; G8XHD7; -.
DR   EnsemblBacteria; AEW98883; AEW98883; SCATT_p06900.
DR   KEGG; scy:SCATT_p06900; -.
DR   PATRIC; fig|1003195.29.peg.6485; -.
DR   HOGENOM; CLU_011302_2_0_11; -.
DR   Proteomes; UP000007842; Plasmid pSCATT.
DR   GO; GO:0062144; F:L-propargylglycine synthase activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; NAS: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.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Antibiotic biosynthesis; Lyase; Plasmid;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..500
FT                   /note="L-2-amino-4-chloropent-4-enoate
FT                   dechlorinase/desaturase"
FT                   /id="PRO_0000447352"
FT   MOD_RES         311
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P06721"
SQ   SEQUENCE   500 AA;  52917 MW;  552FCE28AD93F5E5 CRC64;
     MSAGSPAEPR PVPGSVHSVS VSIPDVRSVI GFESGDPATL RRIAWGYPRF RTHPYVARVA
     ALVAGAVGGR AQDLVLTRSV RAAEAAAAYA GLAPGAVFEA SGVRGVRVAE DDPALAAVRG
     HVQHTGAHLT SREAEDVLLE AGLIEARQAE EAVSEEPAEA VRSALATAYG AGDPADVSLH
     NSGMNAVAAA VAAVTDLQRP AGRRRWIQLG WIFFDTMSLL DKRLFGTDHV TVPDPFDLAA
     LSRVVAAHPG QLAGIIAELP SNPSLRCPDV PALREIADRA GCALVLDATI ATPHNVDVLG
     YADVVCESLT KYATGSADVL MGAAVVGSAS PWAAQLREGL RRFGDVPYHR DAARVAARIR
     DYGDRMKRVN AGAVALAGFL ERQSAVRAVS WPYDAASQAN YRKVERLSDA PGGLLMVDLR
     VPLERVYDRL AVAKGPSFGA EFTMASPQIF IAHFDLLSTP EGRAELRSRG LHRDMLRISV
     GVEDPELIAE VFRDAFDGAG