ID   STYA_PSEFL              Reviewed;         415 AA.
AC   O06834;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Styrene monooxygenase StyA;
DE            EC=1.14.14.11;
DE   AltName: Full=Styrene monooxygenase large component;
GN   Name=styA;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=ST;
RX   PubMed=9172343; DOI=10.1128/aem.63.6.2232-2239.1997;
RA   Beltrametti F., Marconi A.M., Bestetti G., Colombo C., Galli E., Ruzzi M.,
RA   Zennaro E.;
RT   "Sequencing and functional analysis of styrene catabolism genes from
RT   Pseudomonas fluorescens ST.";
RL   Appl. Environ. Microbiol. 63:2232-2239(1997).
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, StyB reductase
CC       utilizes NADH to reduce FAD, which is then transferred to the
CC       oxygenase; the electron transfer is proposed to occur via a diffusing
CC       flavin. {ECO:0000269|PubMed:9172343}.
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:9172343};
CC   -!- PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:9172343}.
CC   -!- SUBUNIT: Homodimer. A direct interaction with the monooxygenase
CC       reductase component StyB seems not to be necessary for the enzymatic
CC       activity (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the StyA family. {ECO:0000305}.
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DR   EMBL; Z92524; CAB06823.1; -; Genomic_DNA.
DR   AlphaFoldDB; O06834; -.
DR   SMR; O06834; -.
DR   BioCyc; MetaCyc:MON-16946; -.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR   GO; GO:0042207; P:styrene catabolic process; IDA:UniProtKB.
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   FAD; Flavoprotein; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..415
FT                   /note="Styrene monooxygenase StyA"
FT                   /id="PRO_0000430448"
SQ   SEQUENCE   415 AA;  46411 MW;  20464E3EFECE640F CRC64;
     MKKRIGIVGA GTAGLHLGLF LRQHDVDVTV YTDRKPDEYS GLRLLNTVAH HAVTVQREVA
     LDVNEWPSEE FGYFGHYYYV GGSQPMRFYG DLKAPSRAVD YRLYQPMLMR ALEARGGKSC
     YDDVSTEDLE GLSEQYDLLV VCTGKNALGK VFEKQSENSP FEKPQRALCV GLFKGIKEAP
     IRAVTMSFSP GHGELIEIPT LSFNGMSTAL VLENHIGSDL EVLAHTKYDD DPRAFLDLML
     EKLRKHHPSV AERIDPAEFD LANSSLDILQ GGVVPAFRDG HATLSNGKTI IGLGDVQATV
     DPVLGQGANM ASHAAWILGE EILAHSVYDL RFSEHLERRR QDRVLCATRW TNFILSALSA
     LPPEFLAFLQ ILSQSREMAD EFTDNFNYPE RQWDRFSSPE RIGQWCNQYA PTIAA