PVCB_XENNA
ID PVCB_XENNA Reviewed; 296 AA.
AC D3V9Q5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Tyrosine isonitrile desaturase/decarboxylase {ECO:0000305};
DE EC=1.14.20.10 {ECO:0000269|PubMed:25866990};
DE AltName: Full=Rhabduscin biosynthesis protein PvcB {ECO:0000305};
DE AltName: Full=XnPvcB {ECO:0000303|PubMed:25866990};
GN Name=pvcB {ECO:0000303|PubMed:25866990};
GN Synonyms=isnB {ECO:0000303|PubMed:22711807};
GN OrderedLocusNames=XNC1_1222 {ECO:0000312|EMBL:CBJ89293.1};
OS Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / CCUG 14189 / LMG
OS 1036 / NCIMB 9965 / AN6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=406817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19061 / DSM 3370 / CCUG 14189 / LMG 1036 / NCIMB 9965 / AN6;
RX PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA Goodrich-Blair H.;
RT "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT convergent lifestyles from divergent genomes.";
RL PLoS ONE 6:E27909-E27909(2011).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 19061 / DSM 3370 / CCUG 14189 / LMG 1036 / NCIMB 9965 / AN6;
RX PubMed=22711807; DOI=10.1073/pnas.1201160109;
RA Crawford J.M., Portmann C., Zhang X., Roeffaers M.B., Clardy J.;
RT "Small molecule perimeter defense in entomopathogenic bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:10821-10826(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=25866990; DOI=10.1021/acs.biochem.5b00255;
RA Zhu J., Lippa G.M., Gulick A.M., Tipton P.A.;
RT "Examining reaction specificity in PvcB, a source of diversity in
RT isonitrile-containing natural products.";
RL Biochemistry 54:2659-2669(2015).
CC -!- FUNCTION: Involved in the biosynthesis of rhabduscin, a tyrosine
CC derivative which is a potent inhibitor of phenoloxidase, a key
CC component of the insect's innate immune system (PubMed:22711807).
CC Catalyzes the 2-oxoglutarate-dependent oxidative decarboxylation of
CC tyrosine isonitrile (PubMed:25866990). {ECO:0000269|PubMed:22711807,
CC ECO:0000269|PubMed:25866990}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-3-(4-hydroxyphenyl)-2-isocyanopropanoate + 2-oxoglutarate
CC + H(+) + O2 = 4-[(E)-2-isocyanoethenyl]phenol + 2 CO2 + H2O +
CC succinate; Xref=Rhea:RHEA:56692, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:140647,
CC ChEBI:CHEBI:140650; EC=1.14.20.10;
CC Evidence={ECO:0000269|PubMed:25866990};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56693;
CC Evidence={ECO:0000269|PubMed:25866990, ECO:0000305|PubMed:22711807};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:25866990};
CC Note=Binds 1 Fe(2+) per subunit. {ECO:0000250|UniProtKB:Q9XB59};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for tyrosine isonitrile {ECO:0000269|PubMed:25866990};
CC KM=5.7 uM for 2-oxoglutarate {ECO:0000269|PubMed:25866990};
CC Note=kcat is 5.1 sec(-1). {ECO:0000269|PubMed:25866990};
CC -!- DISRUPTION PHENOTYPE: Deletion of pvcA and pvcB abolishes rhabduscin
CC biosynthesis and decreases virulence of the strain.
CC {ECO:0000269|PubMed:22711807}.
CC -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR EMBL; FN667742; CBJ89293.1; -; Genomic_DNA.
DR RefSeq; WP_010845413.1; NC_014228.1.
DR STRING; 406817.XNC1_1222; -.
DR EnsemblBacteria; CBJ89293; CBJ89293; XNC1_1222.
DR KEGG; xne:XNC1_1222; -.
DR eggNOG; COG2175; Bacteria.
DR HOGENOM; CLU_077936_0_0_6; -.
DR OMA; YFYAHQW; -.
DR BioCyc; MetaCyc:MON-20399; -.
DR BRENDA; 1.14.20.10; 7603.
DR Proteomes; UP000008075; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 1.
PE 1: Evidence at protein level;
KW Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..296
FT /note="Tyrosine isonitrile desaturase/decarboxylase"
FT /id="PRO_0000453971"
FT BINDING 102
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9XB59"
FT BINDING 104
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9XB59"
FT BINDING 251
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9XB59"
SQ SEQUENCE 296 AA; 34275 MW; B11534817A981B3D CRC64;
MNTYEIDCHV ELVKPFGLLI TPNYPEQDIN SLPVDALRKL AQDHLLVILR GFQSGFTDKE
KLTEYTRHWG ELMTWPFGVV LDVMEQSIPS DHVLDSSYIP LHWDGMYREA IPEFQIFHCV
SAPEAAQGGR TTFVNTEQLI LDASEDEFNT WKNTTITYRT KKVTHYGGEV VSPLVCLHPK
GNKWVIRYNE PMHQEDKYAD HHSVTIQGLL SEEQKAFEET LYNRLYDPRY FYAHQWQSGD
MVISDNFSLL HGREAFISRS PRHLQRVHVH GMPVCENNSF RTISDSNSID STVKEV