ID A0A4Q7W9A1_9ACTN Unreviewed; 296 AA. AC A0A4Q7W9A1; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 02-JUN-2021, entry version 6. DE RecName: Full=Virginiamycin B lyase {ECO:0000256|HAMAP-Rule:MF_01282, ECO:0000256|PIRNR:PIRNR026412}; DE EC=4.2.99.- {ECO:0000256|HAMAP-Rule:MF_01282, ECO:0000256|PIRNR:PIRNR026412}; DE AltName: Full=Streptogramin B lyase {ECO:0000256|HAMAP-Rule:MF_01282, ECO:0000256|PIRNR:PIRNR026412}; GN Name=vgb {ECO:0000256|HAMAP-Rule:MF_01282}; GN ORFNames=EV371_2187 {ECO:0000313|EMBL:RZU05773.1}; OS Plantactinospora sp. CNZ321. OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Plantactinospora; unclassified Plantactinospora. OX NCBI_TaxID=2512141 {ECO:0000313|EMBL:RZU05773.1, ECO:0000313|Proteomes:UP000294176}; RN [1] {ECO:0000313|EMBL:RZU05773.1, ECO:0000313|Proteomes:UP000294176} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNZ321 {ECO:0000313|EMBL:RZU05773.1, RC ECO:0000313|Proteomes:UP000294176}; RA Jensen P.; RT "Genome sequnecing to address fundamental questions about secondary RT metabolites and their potential function as extracellular electron shuttles RT (EESs)."; RL Submitted (FEB-2019) 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:0000256|HAMAP-Rule:MF_01282, CC ECO:0000256|PIRNR:PIRNR026412}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01282, CC ECO:0000256|PIRNR:PIRNR026412}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01282, CC ECO:0000256|PIRNR:PIRNR026412}. CC -!- SIMILARITY: Belongs to the Vgb family. {ECO:0000256|HAMAP- CC Rule:MF_01282, ECO:0000256|PIRNR:PIRNR026412}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RZU05773.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; SHKQ01000001; RZU05773.1; -; Genomic_DNA. DR Proteomes; UP000294176; Unassembled WGS sequence. DR GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0017001; P:antibiotic catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule. 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 {ECO:0000256|HAMAP-Rule:MF_01282, KW ECO:0000256|PIRNR:PIRNR026412}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01282, ECO:0000256|PIRNR:PIRNR026412}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01282, ECO:0000256|PIRNR:PIRNR026412}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01282, KW ECO:0000256|PIRNR:PIRNR026412}. FT ACT_SITE 272 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01282" FT METAL 270 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01282" FT METAL 287 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01282" FT BINDING 230 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01282" SQ SEQUENCE 296 AA; 30782 MW; 2A5E5FE1D6EDA18C CRC64; MTSARHPSVR EFPVADSTAG PYGVTIGPDS ATWVTLVHGG EILRMTATGE IRRYPLGEST GPSVITAGPD GALWFTRRDH RIGRVSLSGE VTSYPIPSPN GGPYGITTGP DGALWFTELN ADRIGRIGTD GAIEEHPLPE TGGSPAMITA GADGALWFTL HQANAVGRIA LDGAVTLHPL PTADAGPVGI TGGADGAVWF VEIAAGQLGR ITPDGEITEI PLPDRAARPH AIAAAPDGSY WFTEWGANRV GRLGPDGTIR EYDLPTPGSE PHGIAVDPDG VVWVALEIGA VARLSW //