ID   VGB_SACEN               Reviewed;         300 AA.
AC   A4FF33;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Virginiamycin B lyase {ECO:0000255|HAMAP-Rule:MF_01282};
DE            EC=4.2.99.- {ECO:0000255|HAMAP-Rule:MF_01282};
DE   AltName: Full=Streptogramin B lyase {ECO:0000255|HAMAP-Rule:MF_01282};
GN   Name=vgb {ECO:0000255|HAMAP-Rule:MF_01282}; OrderedLocusNames=SACE_3383;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
CC   -!- FUNCTION: Inactivates the type B streptogramin antibiotics by
CC       linearizing the lactone ring at the ester linkage, generating a free
CC       phenylglycine carboxylate and converting the threonyl moiety into 2-
CC       amino-butenoic acid. {ECO:0000255|HAMAP-Rule:MF_01282}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01282};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01282}.
CC   -!- SIMILARITY: Belongs to the Vgb family. {ECO:0000255|HAMAP-
CC       Rule:MF_01282}.
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DR   EMBL; AM420293; CAM02658.1; -; Genomic_DNA.
DR   RefSeq; WP_009949602.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; A4FF33; -.
DR   SMR; A4FF33; -.
DR   STRING; 405948.SACE_3383; -.
DR   EnsemblBacteria; CAM02658; CAM02658; SACE_3383.
DR   KEGG; sen:SACE_3383; -.
DR   eggNOG; COG4257; Bacteria.
DR   HOGENOM; CLU_054751_1_0_11; -.
DR   OMA; ALWFTEW; -.
DR   OrthoDB; 966287at2; -.
DR   Proteomes; UP000006728; Chromosome.
DR   GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0017001; P:antibiotic catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   HAMAP; MF_01282; VirginiamycinB_lyase; 1.
DR   InterPro; IPR011217; Streptogrm_lyase.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PIRSF; PIRSF026412; Streptogrm_lyase; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Lyase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..300
FT                   /note="Virginiamycin B lyase"
FT                   /id="PRO_0000313777"
FT   ACT_SITE        272
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT   BINDING         270
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT   BINDING         287
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
SQ   SEQUENCE   300 AA;  31317 MW;  4799989BBD3E6292 CRC64;
     MARERTVEIR EHEVPDPAGG PYGITAGPDG ALWFTLVHSG LIARLAPGGE ATTHRLDADS
     GPAIITAGAD GALWFTEHRA HRIGRLTTED GLTEFAPPTP QAGPYGLATG ADGALWFTEA
     SAGRIGRITA EGEIAEFGLP VPGAFPSMIA AGPDDAMWFT ANQANAIGRM SFDGTAVLHE
     LPTEAAAPVG LALGPDGALW FTEIGAGQIG RVTADGAISE FPLPDRTSRP HAIVARGDEL
     WFTEWGANRV GRIDLDGRID VHELPTPNSE PHGIAVGQDG ALWVALENGA LARVAPESHD