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PVCA_PSEAE
ID   PVCA_PSEAE              Reviewed;         328 AA.
AC   Q9I1L5;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=L-tyrosine isonitrile synthase {ECO:0000305};
DE            EC=4.1.99.24 {ECO:0000305|PubMed:18824174};
DE   AltName: Full=Paerucumarin biosynthesis protein PvcA {ECO:0000305};
GN   Name=pvcA {ECO:0000303|PubMed:18689486};
GN   OrderedLocusNames=PA2254 {ECO:0000312|EMBL:AAG05642.1};
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, AND DISRUPTION PHENOTYPE.
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] {ECO:0007744|PDB:3E59}
RP   X-RAY CRYSTALLOGRAPHY (2.10 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).
CC   -!- FUNCTION: Involved in the biosynthesis of paerucumarin, a cyclized
CC       isocyano derivative of tyrosine (PubMed:18689486, PubMed:18824174).
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:18689486, ECO:0000269|PubMed:18824174,
CC       ECO:0000305|PubMed:18824174}.
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:18824174};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45733;
CC         Evidence={ECO:0000305|PubMed:18824174};
CC   -!- SUBUNIT: Monomer 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:18689486,
CC       PubMed:18824174). Disruption mutant cannot produce paerucumarin
CC       (PubMed:18689486). {ECO:0000269|PubMed:18689486,
CC       ECO:0000269|PubMed:18824174}.
CC   -!- SIMILARITY: Belongs to the isocyanide synthase family. {ECO:0000305}.
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DR   EMBL; AE004091; AAG05642.1; -; Genomic_DNA.
DR   PIR; H83363; H83363.
DR   RefSeq; NP_250944.1; NC_002516.2.
DR   RefSeq; WP_003113733.1; NZ_QZGE01000014.1.
DR   PDB; 3E59; X-ray; 2.10 A; A/B/C/D=1-328.
DR   PDBsum; 3E59; -.
DR   AlphaFoldDB; Q9I1L5; -.
DR   SMR; Q9I1L5; -.
DR   STRING; 287.DR97_6296; -.
DR   PaxDb; Q9I1L5; -.
DR   PRIDE; Q9I1L5; -.
DR   DNASU; 878099; -.
DR   EnsemblBacteria; AAG05642; AAG05642; PA2254.
DR   GeneID; 878099; -.
DR   KEGG; pae:PA2254; -.
DR   PATRIC; fig|208964.12.peg.2356; -.
DR   PseudoCAP; PA2254; -.
DR   HOGENOM; CLU_038280_0_0_6; -.
DR   InParanoid; Q9I1L5; -.
DR   OMA; TRDDWLT; -.
DR   BioCyc; MetaCyc:MON-20393; -.
DR   BioCyc; PAER208964:G1FZ6-2293-MON; -.
DR   BRENDA; 4.1.99.24; 5087.
DR   EvolutionaryTrace; Q9I1L5; -.
DR   Proteomes; UP000002438; 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   1: Evidence at protein level;
KW   3D-structure; Lyase; Reference proteome.
FT   CHAIN           1..328
FT                   /note="L-tyrosine isonitrile synthase"
FT                   /id="PRO_0000453966"
FT   HELIX           9..18
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   HELIX           25..28
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   HELIX           33..53
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   HELIX           82..101
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   HELIX           114..117
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   HELIX           125..142
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   STRAND          145..149
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   HELIX           152..154
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   HELIX           156..161
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   HELIX           165..176
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   HELIX           180..187
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   HELIX           191..208
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   HELIX           217..245
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   STRAND          246..255
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   STRAND          261..266
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   HELIX           278..280
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   STRAND          281..293
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   HELIX           295..300
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   STRAND          304..308
FT                   /evidence="ECO:0007829|PDB:3E59"
FT   STRAND          311..317
FT                   /evidence="ECO:0007829|PDB:3E59"
SQ   SEQUENCE   328 AA;  37134 MW;  DE646CA9BEF43B29 CRC64;
     MYAIAEDTLP ARVLKELLLY RRRYPEHRQS ASEADEIRRI EQVQLPRIAA FIEAGEPIEF
     VLPAFPAKSP NPGKVLDSRP DMAERLSLSF LNHLCQRIQL FYAPGAKITV CSDGRVFGDL
     VRIGDAHISA YQDALRLMIE EIGATHIGVF NLEDVRAFEA QRDNHEQLRQ LLIGGYAEPL
     ESIRETLLAS EEGLLLYRAI TRFLYEDGLT PDYQGSKTAL QRDAKERAYG VIQRSWAWGA
     LLADQFPRAI RLSIHPQPAD SLKFGIHMMP TRDDWLTPWH GVAVNTEDRF VLMKRSEVLE
     LGGELVQING QPSHYRLPAR AARRAAVA
 
 
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