ID   VGB_MYCSK               Reviewed;         280 AA.
AC   A1UJW6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Mkms_3932;
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=189918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS;
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   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
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; CP000518; ABL93124.1; -; Genomic_DNA.
DR   RefSeq; WP_011561238.1; NC_008705.1.
DR   AlphaFoldDB; A1UJW6; -.
DR   SMR; A1UJW6; -.
DR   STRING; 189918.Mkms_3932; -.
DR   EnsemblBacteria; ABL93124; ABL93124; Mkms_3932.
DR   KEGG; mkm:Mkms_3932; -.
DR   HOGENOM; CLU_054751_1_0_11; -.
DR   OMA; ALWFTEW; -.
DR   OrthoDB; 966287at2; -.
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; IPR011044; Quino_amine_DH_bsu.
DR   InterPro; IPR011217; Streptogrm_lyase.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   SUPFAM; SSF50969; SSF50969; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..280
FT                   /note="Virginiamycin B lyase"
FT                   /id="PRO_0000313773"
FT   ACT_SITE        256
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         254
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT   BINDING         271
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
SQ   SEQUENCE   280 AA;  28958 MW;  4617B58B27999A3C CRC64;
     MSLIREIAGG PYALAAGPDG AMWVTLVHDG AIARVGADGA VDRFPVADGS RPSLISAGPD
     GALWFTRNGD DRIGRLTTAG ELTEFPLSEG SAPFGICAGA DGALWFTEMG SGGIGRITVD
     GQTSGWASVG GTPSMITRGP DDAVWFTLNQ GNAIGRLHPR DGVTMRELPT RGAGPVGITA
     THDDAIWFTE ILADKLGRIP LDGALQEIDL PGKPHAVVAD PSGGVWVSLW GADRLARVSA
     DGDIETFDLP PGSEPHGLAF GPDGGLWVAL ESGFVLRMPD