ID   VGB_MYCVP               Reviewed;         290 AA.
AC   A1T6B0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-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=Mvan_1889;
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000511; ABM12710.1; -; Genomic_DNA.
DR   RefSeq; WP_011779128.1; NC_008726.1.
DR   AlphaFoldDB; A1T6B0; -.
DR   SMR; A1T6B0; -.
DR   STRING; 350058.Mvan_1889; -.
DR   EnsemblBacteria; ABM12710; ABM12710; Mvan_1889.
DR   KEGG; mva:Mvan_1889; -.
DR   eggNOG; COG4257; Bacteria.
DR   HOGENOM; CLU_054751_1_0_11; -.
DR   OMA; ALWFTEW; -.
DR   OrthoDB; 966287at2; -.
DR   Proteomes; UP000009159; 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..290
FT                   /note="Virginiamycin B lyase"
FT                   /id="PRO_0000313775"
FT   ACT_SITE        267
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT   BINDING         265
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
SQ   SEQUENCE   290 AA;  30073 MW;  280740B42F89E639 CRC64;
     MIPRVTSTAQ TDLTEGADPY GICAADDGAL WVTLVHSGAV VRLSADGGRR DYPIGAQARP
     SVVTVGRDGT AWFTRTGDDR ITALDRTGAM TTFELASGSG PFGICVGADG AVWFTESTGD
     RLGRIDPDAT VSYVALPEGC FPAFVAAGAD GAVWATLNHA DAVVRILPSA DPEVIDIPTP
     GAAPVGITWG GDAVWFVEIA TGRIGRIGDD RLVTEFALPD PACRPHAITA GPDGCWFTEW
     ATDRVGHIGR DGTVEEYDLP SSVSEPHGIT VAPDGAVWVA AESGSVVRLG