ID   STYC_PSEFL              Reviewed;         169 AA.
AC   O06836;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Styrene-oxide isomerase;
DE            EC=5.3.99.7;
GN   Name=styC;
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).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA   Shearer A.G., Altman T., Rhee C.D.;
RT   "Finding sequences for over 270 orphan enzymes.";
RL   PLoS ONE 9:E97250-E97250(2014).
CC   -!- FUNCTION: Epoxystyrene isomerase that catalyzes the second step in the
CC       aerobic styrene degradation pathway by converting epoxystyrene to
CC       phenylacetaldehyde. {ECO:0000269|PubMed:9172343}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=styrene oxide = 2-phenylacetaldehyde; Xref=Rhea:RHEA:21604,
CC         ChEBI:CHEBI:16424, ChEBI:CHEBI:17907; EC=5.3.99.7;
CC         Evidence={ECO:0000269|PubMed:9172343};
CC   -!- PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:9172343}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; Z92524; CAB06825.1; -; Genomic_DNA.
DR   AlphaFoldDB; O06836; -.
DR   BioCyc; MetaCyc:MON-16948; -.
DR   BRENDA; 5.3.99.7; 5121.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0018846; F:styrene-oxide isomerase activity; IDA:UniProtKB.
DR   GO; GO:0042207; P:styrene catabolic process; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Isomerase; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..169
FT                   /note="Styrene-oxide isomerase"
FT                   /id="PRO_0000430449"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   169 AA;  18101 MW;  737C036EAF776CE9 CRC64;
     MLHAFERKMA GHGILMIFCT LLFGVGLWMH LVGGFEIIPG YILEFHVPGS PEGWARAHSG
     PALNGMMVIA VAFVLPSLGF ADKKPHLLGN IIILDGWANV GFYFFSNFSP NRGLTFGPNH
     FGPGDIFSFL ALAPAYLFGV LAMGALAVIG YQALKSVGSR KAVPHATAE