ID   PVCB_ERWAC              Reviewed;         292 AA.
AC   D4I2N1;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Tyrosine isonitrile desaturase {ECO:0000305};
DE            EC=1.14.20.9 {ECO:0000269|PubMed:25866990};
DE   AltName: Full=EaPvcB {ECO:0000303|PubMed:25866990};
GN   Name=pvcB {ECO:0000303|PubMed:25866990};
GN   OrderedLocusNames=EAMY_1787 {ECO:0000312|EMBL:CBA20737.1};
OS   Erwinia amylovora (strain CFBP1430).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=665029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFBP1430;
RX   PubMed=20192826; DOI=10.1094/mpmi-23-4-0384;
RA   Smits T.H., Rezzonico F., Kamber T., Blom J., Goesmann A., Frey J.E.,
RA   Duffy B.;
RT   "Complete genome sequence of the fire blight pathogen Erwinia amylovora
RT   CFBP 1430 and comparison to other Erwinia spp.";
RL   Mol. Plant Microbe Interact. 23:384-393(2010).
RN   [2]
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: Catalyzes the 2-oxoglutarate-dependent oxidation of tyrosine
CC       isonitrile. {ECO:0000269|PubMed:25866990}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-3-(4-hydroxyphenyl)-2-isocyanopropanoate + 2-oxoglutarate
CC         + O2 = (2E)-3-(4-hydroxyphenyl)-2-isocyanoprop-2-enoate + CO2 + H2O +
CC         succinate; Xref=Rhea:RHEA:56688, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:140647, ChEBI:CHEBI:140648;
CC         EC=1.14.20.9; Evidence={ECO:0000269|PubMed:25866990};
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=16 uM for tyrosine isonitrile {ECO:0000269|PubMed:25866990};
CC         KM=4.8 uM for 2-oxoglutarate {ECO:0000269|PubMed:25866990};
CC         Note=kcat is 0.22 sec(-1). {ECO:0000269|PubMed:25866990};
CC   -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR   EMBL; FN434113; CBA20737.1; -; Genomic_DNA.
DR   RefSeq; WP_004157574.1; NC_013961.1.
DR   STRING; 665029.EAMY_1787; -.
DR   EnsemblBacteria; CBA20737; CBA20737; EAMY_1787.
DR   GeneID; 8914734; -.
DR   KEGG; eam:EAMY_1787; -.
DR   PATRIC; fig|665029.3.peg.1722; -.
DR   eggNOG; COG2175; Bacteria.
DR   HOGENOM; CLU_077936_0_0_6; -.
DR   OMA; HIFANNY; -.
DR   OrthoDB; 1742732at2; -.
DR   BRENDA; 1.14.20.9; 2136.
DR   Proteomes; UP000001841; Chromosome.
DR   GO; GO:0008336; F:gamma-butyrobetaine dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; 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.
FT   CHAIN           1..292
FT                   /note="Tyrosine isonitrile desaturase"
FT                   /id="PRO_0000453969"
FT   BINDING         110
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XB59"
FT   BINDING         112
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XB59"
FT   BINDING         259
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XB59"
SQ   SEQUENCE   292 AA;  33087 MW;  ABD32BFECD736A51 CRC64;
     MNPADLPDTL DVAPLTGETG EPCSFGILIK PCRAGRHIGE LSVTWLRALV YSHQLVVLRG
     FDHFASSDSL TRYCATFGEI MMWPYGAVLE LVEHANPDDH IFANSYVPLH WDGMYLDTVP
     EFQLFQCVHA AGDMQGGRTT FSSTNAALRI ATPAVRELWA RAHGRYQRSV ELYSNTVEAP
     IIGIHPLREF PVIRFCEPPD ENDATFLNPS SYSFGGINKD EEEMLLVSLM KTLRDPRVYY
     AHQWQTGDFV LSDNLSLLHG REQYTHHSGR HLRRVHIHGR PQIANHHLVR SE