ID   PVCA_XENNA              Reviewed;         335 AA.
AC   D3V9Q4;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=L-tyrosine isonitrile synthase {ECO:0000305};
DE            EC=4.1.99.24 {ECO:0000305|PubMed:22711807, ECO:0000305|PubMed:28212039};
DE   AltName: Full=Rhabduscin biosynthesis protein PvcA {ECO:0000305};
GN   Name=pvcA {ECO:0000303|PubMed:28212039};
GN   Synonyms=isnA {ECO:0000303|PubMed:22711807};
GN   OrderedLocusNames=XNC1_1221 {ECO:0000312|EMBL:CBJ89292.1};
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.
RX   PubMed=28212039; DOI=10.1021/acs.orglett.7b00258;
RA   Chang W.C., Sanyal D., Huang J.L., Ittiamornkul K., Zhu Q., Liu X.;
RT   "In vitro stepwise reconstitution of amino acid derived vinyl isocyanide
RT   biosynthesis: detection of an elusive intermediate.";
RL   Org. Lett. 19:1208-1211(2017).
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       Responsible for the synthesis of the isonitrile group on tyrosine using
CC       the C2 of ribulose 5-phosphate as the source of the carbon atom
CC       (Probable). {ECO:0000269|PubMed:22711807, ECO:0000305|PubMed:28212039}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 5-phosphate + L-tyrosine = (2S)-3-(4-
CC         hydroxyphenyl)-2-isocyanopropanoate + formaldehyde + H(+) + H2O +
CC         hydroxyacetone + phosphate; Xref=Rhea:RHEA:45732, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16842, ChEBI:CHEBI:27957,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58121, ChEBI:CHEBI:58315,
CC         ChEBI:CHEBI:140647; EC=4.1.99.24;
CC         Evidence={ECO:0000305|PubMed:22711807, ECO:0000305|PubMed:28212039};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45733;
CC         Evidence={ECO:0000305|PubMed:22711807, ECO:0000305|PubMed:28212039};
CC   -!- DISRUPTION PHENOTYPE: Deletion of isnA and isnB abolishes rhabduscin
CC       biosynthesis and decreases virulence of the strain.
CC       {ECO:0000269|PubMed:22711807}.
CC   -!- SIMILARITY: Belongs to the isocyanide synthase family. {ECO:0000305}.
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DR   EMBL; FN667742; CBJ89292.1; -; Genomic_DNA.
DR   RefSeq; WP_010845414.1; NC_014228.1.
DR   STRING; 406817.XNC1_1221; -.
DR   EnsemblBacteria; CBJ89292; CBJ89292; XNC1_1221.
DR   KEGG; xne:XNC1_1221; -.
DR   eggNOG; COG3207; Bacteria.
DR   HOGENOM; CLU_038280_0_0_6; -.
DR   OMA; TRDDWLT; -.
DR   BioCyc; MetaCyc:MON-20417; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR007817; Isocyanide_synthase_DIT1.
DR   InterPro; IPR017133; PvcA.
DR   PANTHER; PTHR37285; PTHR37285; 1.
DR   Pfam; PF05141; DIT1_PvcA; 1.
DR   PIRSF; PIRSF037196; Pyoverdine_chromoph_PvcA; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..335
FT                   /note="L-tyrosine isonitrile synthase"
FT                   /id="PRO_0000453967"
SQ   SEQUENCE   335 AA;  38442 MW;  68A68B4831C8C16C CRC64;
     MEYFDIEEVS SKILHELLQY RRRFPESEHT IQYEENKVSE VQLPRIRAFV EQGKPIECIL
     PAFPTKSPNP RKVLGKMPDM AEKLSLMFLN SLCQRIQLYY PPGAKIIICS DGHVFSDLIH
     VDDNTITDYQ VEIEKLLHES GATHLSVFNL GNVESLTQYT DDYDQLRELL VKNYASSTEE
     IKAILKENEE GLLLYRAITR FLYEDSLLPE YTGSKNALQK DARQRSVGVI QRSWAWGNLL
     AEQFPQAIRL SIHPQSVESL KLGIHMMPTR DDWLTPWHGV AANINGQFVL MKSDEVKNLQ
     GKLIHIRGVP SHYVIETESE RNQEIEPIAE AVHAG