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DMPK_PSEUF
ID   DMPK_PSEUF              Reviewed;          92 AA.
AC   P19729;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Phenol 2-monooxygenase, auxiliary component DmpK {ECO:0000305};
DE   AltName: Full=Phenol 2-monooxygenase P0 component;
DE   AltName: Full=Phenol hydroxylase P0 protein;
GN   Name=dmpK {ECO:0000303|PubMed:2254258}; Synonyms=pheA1;
OS   Pseudomonas sp. (strain CF600).
OG   Plasmid pVI150.
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=79676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=CF600;
RX   PubMed=2254258; DOI=10.1128/jb.172.12.6826-6833.1990;
RA   Nordlund I., Powlowski J., Shingler V.;
RT   "Complete nucleotide sequence and polypeptide analysis of multicomponent
RT   phenol hydroxylase from Pseudomonas sp. strain CF600.";
RL   J. Bacteriol. 172:6826-6833(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BH;
RA   Takeo M., Maeda Y., Okada H., Miyama K., Mori K., Ike M., Fujita M.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RC   STRAIN=CF600;
RX   PubMed=2254259; DOI=10.1128/jb.172.12.6834-6840.1990;
RA   Powlowski J., Shingler V.;
RT   "In vitro analysis of polypeptide requirements of multicomponent phenol
RT   hydroxylase from Pseudomonas sp. strain CF600.";
RL   J. Bacteriol. 172:6834-6840(1990).
RN   [4]
RP   FUNCTION, SUBUNIT, INTERACTION WITH DMPL AND DMPN, AND MASS SPECTROMETRY.
RC   STRAIN=CF600;
RX   PubMed=8995386; DOI=10.1074/jbc.272.2.945;
RA   Powlowski J., Sealy J., Shingler V., Cadieux E.;
RT   "On the role of DmpK, an auxiliary protein associated with multicomponent
RT   phenol hydroxylase from Pseudomonas sp. strain CF600.";
RL   J. Biol. Chem. 272:945-951(1997).
CC   -!- FUNCTION: DmpK is an auxiliary protein associated with the
CC       multicomponent phenol hydroxylase DmpLMNOP and it may be involved in
CC       the post-translational incorporation of iron into the oxygenase
CC       component of the phenol hydroxylase (PubMed:8995386). Required for
CC       growth on phenol but not for in vitro phenol hydroxylase activity
CC       (PubMed:2254258, PubMed:2254259). {ECO:0000269|PubMed:2254258,
CC       ECO:0000269|PubMed:2254259, ECO:0000269|PubMed:8995386}.
CC   -!- PATHWAY: Aromatic compound metabolism; phenol degradation.
CC       {ECO:0000269|PubMed:2254258}.
CC   -!- SUBUNIT: Homotrimer or homotetramer (PubMed:8995386). Interacts with
CC       the phenol hydroxylase components DmpL (P1 component) and DmpN (P3
CC       component) (PubMed:8995386). {ECO:0000269|PubMed:8995386}.
CC   -!- MASS SPECTROMETRY: Mass=10451; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8995386};
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene cannot grow on phenol.
CC       {ECO:0000269|PubMed:2254258}.
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DR   EMBL; M60276; AAA25939.1; -; Genomic_DNA.
DR   EMBL; D28864; BAA06014.1; -; Genomic_DNA.
DR   AlphaFoldDB; P19729; -.
DR   BioCyc; MetaCyc:MON-12794; -.
DR   BRENDA; 1.14.13.244; 16277.
DR   UniPathway; UPA00728; -.
DR   GO; GO:0018662; F:phenol 2-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019336; P:phenol-containing compound catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR010353; DmpK.
DR   Pfam; PF06099; Phenol_hyd_sub; 1.
DR   PIRSF; PIRSF000039; Phenol_monooxy_K; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Plasmid.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8995386"
FT   CHAIN           2..92
FT                   /note="Phenol 2-monooxygenase, auxiliary component DmpK"
FT                   /id="PRO_0000079940"
SQ   SEQUENCE   92 AA;  10586 MW;  9893DFD3CAACB71E CRC64;
     MTVTNTPTPT FDQLTRYIRV RSEPEAKFVE FDFAIGHPEL FVELVLPQDA FVKFCQHNRV
     VAMDEAMAKA VDDDMVKWRF GDVGRRLPKD PG
 
 
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