ID H1S7B5_9BURK Unreviewed; 301 AA.
AC H1S7B5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Virginiamycin B lyase {ECO:0000256|PIRNR:PIRNR026412};
DE EC=4.2.99.- {ECO:0000256|PIRNR:PIRNR026412};
DE AltName: Full=Streptogramin B lyase {ECO:0000256|PIRNR:PIRNR026412};
GN ORFNames=OR16_19101 {ECO:0000313|EMBL:EHP41640.1};
OS Cupriavidus basilensis OR16.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP41640.1, ECO:0000313|Proteomes:UP000005808};
RN [1] {ECO:0000313|EMBL:EHP41640.1, ECO:0000313|Proteomes:UP000005808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR16 {ECO:0000313|EMBL:EHP41640.1,
RC ECO:0000313|Proteomes:UP000005808};
RX PubMed=22461549; DOI=10.1128/JB.06752-11;
RA Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA Nagy I., Horvath B., Nagy I., Kukolya J.;
RT "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL J. Bacteriol. 194:2109-2110(2012).
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|PIRNR:PIRNR026412}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRNR:PIRNR026412};
CC -!- SUBUNIT: Monomer. {ECO:0000256|PIRNR:PIRNR026412}.
CC -!- SIMILARITY: Belongs to the Vgb family. {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:EHP41640.1}.
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DR EMBL; AHJE01000045; EHP41640.1; -; Genomic_DNA.
DR AlphaFoldDB; H1S7B5; -.
DR PATRIC; fig|1127483.3.peg.3831; -.
DR Proteomes; UP000005808; Unassembled WGS sequence.
DR GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR011217; Streptogrm_lyase.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR40274; VIRGINIAMYCIN B LYASE; 1.
DR PANTHER; PTHR40274:SF3; VIRGINIAMYCIN B LYASE; 1.
DR PIRSF; PIRSF026412; Streptogrm_lyase; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|PIRNR:PIRNR026412}; Hydrolase {ECO:0000313|EMBL:EHP41640.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR026412};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR026412};
KW Membrane {ECO:0000313|EMBL:EHP41640.1};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR026412};
KW Transmembrane {ECO:0000313|EMBL:EHP41640.1}.
SQ SEQUENCE 301 AA; 32623 MW; E8F63E8AAAF24FBD CRC64;
MRIQSYAVPA GAHPHDVAPA QDGSVWYTAQ PLGALGRLDP ATGKTTHIPL GRDAAPHGVI
VGPDGAAWIT DGGQNAIVRV DPATRALKRF PLPAGHPNAN LNTAVFDAQG HLWFTGQNGV
YGELDPIGRI RIFDAPNGAG PYGITITPGG DVYYASLAGN YIARIDKATG AAHVIVPPTP
YAGPRRIWSD SKGTLWVSEW TAGKLGAYDP ATERWREWRL PGDGPHAYAV YVDERDKVWL
SDWGANAVLR FDPQTGRFER FTSSRPHANV RQMLGRPGEV WTAESGTDQL VVYRFKEGAR
E
//
