ID   BESA_STREN              Reviewed;         482 AA.
AC   G8XHD8;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=L-propargylglycine--L-glutamate ligase {ECO:0000305|PubMed:30867596};
DE            EC=6.3.2.- {ECO:0000269|PubMed:30867596};
GN   Name=besA {ECO:0000303|PubMed:30867596};
GN   OrderedLocusNames=SCATT_p06910 {ECO:0000312|EMBL:AEW98884.1};
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, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, 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-beta-ethynylserine, that are produced as
CC       antibiotics by S.cattleya. Catalyzes the ATP-dependent ligation of L-
CC       propargylglycine to L-glutamate to form the dipeptide L-gamma-glutamyl-
CC       L-propargylglycine. Is selective for L-propargylglycine over norvaline,
CC       allylglycine and the standard proteinogenic amino acids, except L-
CC       cysteine which can be used as a substrate to a lesser extent.
CC       {ECO:0000269|PubMed:30867596}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + L-propargylglycine = ADP + H(+) + L-gamma-
CC         glutamyl-L-propargylglycine + phosphate; Xref=Rhea:RHEA:59896,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:143285, ChEBI:CHEBI:143286,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:30867596};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59897;
CC         Evidence={ECO:0000269|PubMed:30867596};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.49 mM for L-propargylglycine {ECO:0000269|PubMed:30867596};
CC         KM=4.9 mM for L-cysteine {ECO:0000269|PubMed:30867596};
CC         Note=kcat is 2.0 sec(-1) for the glutamylation of L-propargylglycine.
CC         kcat is 1.53 sec(-1) for the glutamylation of L-cysteine.;
CC   -!- PATHWAY: Amino-acid metabolism. {ECO:0000269|PubMed:30867596}.
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:30867596}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene produce lowered levels of
CC       both L-propargylglycine and 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; AEW98884.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8XHD8; -.
DR   SMR; G8XHD8; -.
DR   EnsemblBacteria; AEW98884; AEW98884; SCATT_p06910.
DR   KEGG; scy:SCATT_p06910; -.
DR   PATRIC; fig|1003195.29.peg.6486; -.
DR   HOGENOM; CLU_008013_0_0_11; -.
DR   OMA; PGIPFSH; -.
DR   Proteomes; UP000007842; Plasmid pSCATT.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0062145; F:L-propargylglycine--L-glutamate ligase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0062142; P:L-beta-ethynylserine biosynthetic process; IMP:UniProtKB.
DR   InterPro; IPR003806; ATP-grasp_PylC-type.
DR   InterPro; IPR041356; PGM1_C.
DR   InterPro; IPR040754; PreAtp-grasp.
DR   Pfam; PF02655; ATP-grasp_3; 1.
DR   Pfam; PF18105; PGM1_C; 1.
DR   Pfam; PF18604; PreAtp-grasp; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Antibiotic biosynthesis; ATP-binding; Ligase;
KW   Nucleotide-binding; Plasmid; Reference proteome.
FT   CHAIN           1..482
FT                   /note="L-propargylglycine--L-glutamate ligase"
FT                   /id="PRO_0000447348"
SQ   SEQUENCE   482 AA;  52271 MW;  0531FA32853F0E84 CRC64;
     MYGAGVVTRM NEAERFHMTD PGSTKILIYA FNYADRMLEE VPYLRYSAER SLCFLGDLRD
     PGTRLVVITS EAVDPATLDY HLRDVFRFDE PALADVRRRL TLLTPASRAA RPLDSLVLED
     EALVETLRRA VAERPAGTIV DFSASPATDE LGRRTGATPE EGDHAFVARW GSKSGGKEIC
     LRAGVAVPGG TSEVLRSEAE VVEAIHRLSC GTAAARRAMV KLDAITWAAS IGNVLIDRDK
     LRHTGDLVGS AEVIRLPAEE FRRELAEQGA IVEEFLEEIT DSPSGLGHIE RDGTVRVVAC
     HDQVLSGGQY WGCRFPADER WRPEITDAVR RTGEVLSGLG HRGAFGVDFV VAGERGLLAV
     EINLRKVGPS HVVRYAEALV GARVGADGML RGADGRPVYY THGRLLEPET LGKLNPRTAV
     ERLRAEGLLY RHDTGEGVAL HVLGALNACG FVELTALARS PEAADGYSRA AQALLTGPYP
     SA