ID   VGB_NOCFA               Reviewed;         279 AA.
AC   Q5YWV1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=NFA_24930;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD57340.1; -; Genomic_DNA.
DR   RefSeq; WP_011209025.1; NC_006361.1.
DR   AlphaFoldDB; Q5YWV1; -.
DR   SMR; Q5YWV1; -.
DR   STRING; 247156.NFA_24930; -.
DR   EnsemblBacteria; BAD57340; BAD57340; NFA_24930.
DR   GeneID; 61133241; -.
DR   KEGG; nfa:NFA_24930; -.
DR   eggNOG; COG4257; Bacteria.
DR   HOGENOM; CLU_054751_1_0_11; -.
DR   OMA; ALWFTEW; -.
DR   BioCyc; NFAR247156:NFA_RS12490-MON; -.
DR   Proteomes; UP000006820; 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; -; 2.
DR   HAMAP; MF_01282; VirginiamycinB_lyase; 1.
DR   InterPro; IPR011217; Streptogrm_lyase.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Lyase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..279
FT                   /note="Virginiamycin B lyase"
FT                   /id="PRO_0000313776"
FT   ACT_SITE        255
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT   BINDING         253
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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"
SQ   SEQUENCE   279 AA;  28848 MW;  CB0BDB77D1062A61 CRC64;
     MPEILEVVDV DGGPYGVTVD ETGTLWFTLA ARGAVGRLVD GTVETVALEP ADGSPTVIMA
     EGDGAWFTEF RGNRIGRVEA NGALSFLTAE SPYGLCRAGD GGLWYTELSA GGVVHRAPDG
     TTTRHAVEGM PSMIAEAADG TVFVTLNQGN AVARITPDGQ VRTTALPTAG AGPVGLATAA
     DGAWFVELLA GQLGHVDRDG TVTEHPLPDR DARPHAVVVA PDGTVWFTEW AAARLGRRTA
     DGEITELALP GAEPHGLAVA PDGTLWVAME SGALVHVRP