ID   STYA_PSESP              Reviewed;         415 AA.
AC   O50214;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Styrene monooxygenase StyA;
DE            EC=1.14.14.11;
DE   AltName: Full=Styrene monooxygenase large component;
GN   Name=styA; Synonyms=stdA;
OS   Pseudomonas sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VLB120;
RX   PubMed=9603811; DOI=10.1128/aem.64.6.2032-2043.1998;
RA   Panke S., Witholt B., Schmid A., Wubbolts M.G.;
RT   "Towards a biocatalyst for (S)-styrene oxide production: characterization
RT   of the styrene degradation pathway of Pseudomonas sp. strain VLB120.";
RL   Appl. Environ. Microbiol. 64:2032-2043(1998).
RN   [2]
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, AND FUNCTION.
RX   PubMed=15292130; DOI=10.1128/jb.186.16.5292-5302.2004;
RA   Otto K., Hofstetter K., Rothlisberger M., Witholt B., Schmid A.;
RT   "Biochemical characterization of StyAB from Pseudomonas sp. strain VLB120
RT   as a two-component flavin-diffusible monooxygenase.";
RL   J. Bacteriol. 186:5292-5302(2004).
CC   -!- FUNCTION: Styrene monooxygenase which catalyzes the first step in the
CC       aerobic styrene degradation pathway by enantioselective epoxidation of
CC       the vinyl side chain. In a two-component system, a reductase utilizes
CC       NADH to reduce FAD, which is then transferred to the oxygenase; the
CC       electron transfer is proposed to occur via a diffusing flavin.
CC       {ECO:0000269|PubMed:15292130}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FADH2 + O2 + styrene = (2S)-2-phenyloxirane + FAD + H(+) +
CC         H2O; Xref=Rhea:RHEA:31727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:27452, ChEBI:CHEBI:51014,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.14.14.11;
CC         Evidence={ECO:0000269|PubMed:15292130};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.45 mM for styrene (in the presence of styB, FAD and NADH)
CC         {ECO:0000269|PubMed:15292130};
CC         Vmax=2.1 umol/min/mg enzyme {ECO:0000269|PubMed:15292130};
CC   -!- PATHWAY: Aromatic compound metabolism.
CC   -!- SUBUNIT: Homodimer. A direct interaction with the monooxygenase
CC       reductase component StyB seems not to be necessary for the enzymatic
CC       activity. {ECO:0000269|PubMed:15292130}.
CC   -!- SIMILARITY: Belongs to the StyA family. {ECO:0000305}.
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DR   EMBL; AF031161; AAC23718.1; -; Genomic_DNA.
DR   AlphaFoldDB; O50214; -.
DR   SMR; O50214; -.
DR   SABIO-RK; O50214; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR041654; StyA_sbd.
DR   Pfam; PF17885; Smoa_sbd; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; Monooxygenase;
KW   Oxidoreductase.
FT   CHAIN           1..415
FT                   /note="Styrene monooxygenase StyA"
FT                   /id="PRO_0000418832"
SQ   SEQUENCE   415 AA;  46346 MW;  EC1E5BE4722655A1 CRC64;
     MKKRIGIVGA GTAGLHLGLF LRQHDVDVTV YTDRKPDEYS GLRLLNTVAH NAVTVQREVA
     LDVNEWPSEE FGYFGHYYYV GGPQPMRFYG DLKAPSRAVD YRLYQPMLMR ALEARGGKFC
     YDAVSAEDLE GLSEQYDLLV VCTGKYALGK VFEKQSENSP FEKPQRALCV GLFKGIKEAP
     IRAVTMSFSP GHGELIEIPT LSFNGMSTAL VLENHIGSDL EVLAHTKYDD DPRAFLDLML
     EKLGKHHPSV AERIDPAEFD LANSSLDILQ GGVVPAFRDG HATLNNGKTI IGLGDIQATV
     DPVLGQGANM ASYAAWILGE EILAHSVYDL RFSEHLERRR QDRVLCATRW TNFTLSALSA
     LPPEFLAFLQ ILSQSREMAD EFTDNFNYPE RQWDRFSSPE RIGQWCSQFA PTIAA