PVCB_PSEAE
ID PVCB_PSEAE Reviewed; 291 AA.
AC Q9I1L4; A0A0M3KL23;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Tyrosine isonitrile desaturase {ECO:0000305};
DE EC=1.14.20.9 {ECO:0000269|PubMed:25866990};
DE AltName: Full=PaPvcB {ECO:0000303|PubMed:25866990};
DE AltName: Full=Paerucumarin biosynthesis protein PvcB {ECO:0000305};
GN Name=pvcB {ECO:0000303|PubMed:18689486};
GN OrderedLocusNames=PA2255 {ECO:0000312|EMBL:AAG05643.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION.
RX PubMed=18689486; DOI=10.1128/jb.00801-08;
RA Clarke-Pearson M.F., Brady S.F.;
RT "Paerucumarin, a new metabolite produced by the pvc gene cluster from
RT Pseudomonas aeruginosa.";
RL J. Bacteriol. 190:6927-6930(2008).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=MPAO1;
RX PubMed=32941967; DOI=10.1016/j.micpath.2020.104491;
RA Iftikhar A., Asif A., Manzoor A., Azeem M., Sarwar G., Rashid N.,
RA Qaisar U.;
RT "Mutation in pvcABCD operon of Pseudomonas aeruginosa modulates MexEF-OprN
RT efflux system and hence resistance to chloramphenicol and ciprofloxacin.";
RL Microb. Pathog. 149:104491-104491(2020).
RN [4] {ECO:0007744|PDB:3EAT}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, SUBUNIT, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=18824174; DOI=10.1016/j.jmb.2008.09.027;
RA Drake E.J., Gulick A.M.;
RT "Three-dimensional structures of Pseudomonas aeruginosa PvcA and PvcB, two
RT proteins involved in the synthesis of 2-isocyano-6,7-dihydroxycoumarin.";
RL J. Mol. Biol. 384:193-205(2008).
RN [5] {ECO:0007744|PDB:4YLM}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=PAK;
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 paerucumarin, a cyclized
CC isocyano derivative of tyrosine (PubMed:18689486, PubMed:18824174).
CC Catalyzes the 2-oxoglutarate-dependent oxidation of tyrosine isonitrile
CC (PubMed:25866990). {ECO:0000269|PubMed:18689486,
CC ECO:0000269|PubMed:18824174, 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56689;
CC Evidence={ECO:0000269|PubMed:25866990, ECO:0000305|PubMed:18824174};
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=93 uM for tyrosine isonitrile {ECO:0000269|PubMed:25866990};
CC KM=23 uM for 2-oxoglutarate {ECO:0000269|PubMed:25866990};
CC Note=kcat is 2.3 sec(-1). {ECO:0000269|PubMed:25866990};
CC -!- SUBUNIT: Homotrimer in solution. {ECO:0000269|PubMed:18824174}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene maintains the ability of
CC the strain to produce the pyoverdine siderophore (PubMed:18824174).
CC Deletion mutant is more sensitive to chloramphenicol and ciprofloxacin
CC in comparison with its parent strain. This sensitivity is probably due
CC to transcriptional repression of mexT and mexEF-oprN genes. Exogenous
CC addition of paerucumarin resumes the expression of mexT and mexEF-oprN
CC genes as well as resistance against chloramphenicol and ciprofloxacin
CC (PubMed:32941967). {ECO:0000269|PubMed:18824174,
CC ECO:0000269|PubMed:32941967}.
CC -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG05643.1; -; Genomic_DNA.
DR PIR; A83364; A83364.
DR RefSeq; NP_250945.1; NC_002516.2.
DR RefSeq; WP_003115812.1; NZ_QZGE01000014.1.
DR PDB; 3EAT; X-ray; 2.50 A; X=1-291.
DR PDB; 4YLM; X-ray; 2.05 A; X=1-291.
DR PDBsum; 3EAT; -.
DR PDBsum; 4YLM; -.
DR AlphaFoldDB; Q9I1L4; -.
DR SMR; Q9I1L4; -.
DR STRING; 287.DR97_6295; -.
DR PaxDb; Q9I1L4; -.
DR EnsemblBacteria; AAG05643; AAG05643; PA2255.
DR GeneID; 878457; -.
DR KEGG; pae:PA2255; -.
DR PATRIC; fig|208964.12.peg.2357; -.
DR PseudoCAP; PA2255; -.
DR HOGENOM; CLU_077936_0_0_6; -.
DR InParanoid; Q9I1L4; -.
DR OMA; HIFANNY; -.
DR PhylomeDB; Q9I1L4; -.
DR BioCyc; MetaCyc:MON-20394; -.
DR BioCyc; PAER208964:G1FZ6-2294-MON; -.
DR BRENDA; 1.14.20.10; 5087.
DR BRENDA; 1.14.20.9; 5087.
DR EvolutionaryTrace; Q9I1L4; -.
DR Proteomes; UP000002438; 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 3D-structure; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..291
FT /note="Tyrosine isonitrile desaturase"
FT /id="PRO_0000453970"
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"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:4YLM"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:4YLM"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:4YLM"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:4YLM"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:3EAT"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4YLM"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 116..129
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:4YLM"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:4YLM"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:4YLM"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:4YLM"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:4YLM"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:4YLM"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:4YLM"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 270..284
FT /evidence="ECO:0007829|PDB:4YLM"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:4YLM"
SQ SEQUENCE 291 AA; 33137 MW; 1D2E02B01850BDB7 CRC64;
MNAYLSDQPV RLSPLRDEQG NQPRFGLLLE PGRPGMHVGE LPAQWLKGLA RSHHLLLLRG
FAAFADAESL TRYCHDFGEV MLWPFGAVLE LVEQEGAEDH IFANNYVPLH WDGMYLETVP
EFQVFHCVDA PGDSDGGRTT FSSTPAALQL ADSSELELWR RASGRYQRSA AHYSSRSAAP
IVERHPRREF PILRFCEPPV EGDASFINPS EFHYDGIAPE QRGELLASLR RCLYHPQAHY
AHRWRSDDLV IADNLTLLHG REAFAHRAPR HLRRVHIHAE PALRNPHLQR D
