ID   BESE_STREN              Reviewed;         268 AA.
AC   F8JJ27; G8XHD4;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=L-gamma-glutamyl-L-propargylglycine hydroxylase {ECO:0000305|PubMed:30867596};
DE            EC=1.14.11.- {ECO:0000269|PubMed:30867596};
GN   Name=besE {ECO:0000303|PubMed:30867596};
GN   OrderedLocusNames=SCATT_p06870 {ECO:0000312|EMBL:AEW98880.1};
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, SUBSTRATE SPECIFICITY, PATHWAY, AND
RP   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-beta-ethynylserine, that are produced as
CC       antibiotics by S.cattleya. Catalyzes the hydroxylation of the dipeptide
CC       L-gamma-glutamyl-L-propargylglycine, leading to L-gamma-glutamyl-L-
CC       beta-ethynylserine. Cannot use L-propargylglycine as substrate.
CC       {ECO:0000269|PubMed:30867596}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-gamma-glutamyl-L-propargylglycine + O2 =
CC         CO2 + L-gamma-glutamyl-(3R)-L-beta-ethynylserine + succinate;
CC         Xref=Rhea:RHEA:59900, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:143286,
CC         ChEBI:CHEBI:143287; Evidence={ECO:0000269|PubMed:30867596};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59901;
CC         Evidence={ECO:0000269|PubMed:30867596};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000305|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 still produce L-
CC       propargylglycine but not L-beta-ethynylserine, that are terminal
CC       alkyne-containing amino acids produced by wild-type S.cattleya.
CC       {ECO:0000269|PubMed:30867596}.
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DR   EMBL; CP003229; AEW98880.1; -; Genomic_DNA.
DR   RefSeq; WP_014151498.1; NC_017585.1.
DR   AlphaFoldDB; F8JJ27; -.
DR   SMR; F8JJ27; -.
DR   EnsemblBacteria; AEW98880; AEW98880; SCATT_p06870.
DR   KEGG; scy:SCATT_p06870; -.
DR   PATRIC; fig|1003195.11.peg.1007; -.
DR   HOGENOM; CLU_072365_1_0_11; -.
DR   OMA; HHDIFAK; -.
DR   OrthoDB; 1861154at2; -.
DR   Proteomes; UP000007842; Plasmid pSCATT.
DR   GO; GO:0062148; F:L-gamma-glutamyl-L-propargylglycine hydroxylase 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.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Antibiotic biosynthesis; Dioxygenase; Iron;
KW   Oxidoreductase; Plasmid; Reference proteome.
FT   CHAIN           1..268
FT                   /note="L-gamma-glutamyl-L-propargylglycine hydroxylase"
FT                   /id="PRO_0000447351"
SQ   SEQUENCE   268 AA;  29424 MW;  248F79B957C576E4 CRC64;
     MSGTTHHHAT FPAVEAAAFT RRHLDDLAAG LLGTVRVPGF FGRPALDTML TSLHRVPVVS
     FDLDRMHHPM ARFGTALNDY RTPELALDAD RYWHDADTAR RQWAGIGMTP DPLELALDAL
     GRAWGVRPAP ATIGGRPAFV GMLREVNDGT FIHYDDINRE YRGGLFDQKI VAQLAFNAWL
     AAPREGGTTT VWRHRWEPAD ENRRHGYGFQ PTAVADDPYV TVAPAAGDAL LFNANNYHVV
     HPGAPGQRRI ALACFLGVTA GGELVVWS