ID   XAMOE_XANP2             Reviewed;         341 AA.
AC   Q9ZET3;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Alkene monooxygenase system, oxygenase component subunit beta {ECO:0000303|PubMed:10103255};
DE            EC=1.14.13.69 {ECO:0000269|PubMed:1444418, ECO:0000269|PubMed:9312093};
GN   Name=xamoE {ECO:0000303|PubMed:10103255, ECO:0000312|EMBL:CAA09915.1};
GN   Synonyms=aamE {ECO:0000303|PubMed:10103255};
GN   OrderedLocusNames=Xaut_4861 {ECO:0000312|EMBL:ABS70072.1};
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OG   Plasmid pXAUT01 {ECO:0000312|EMBL:ABS70072.1,
OG   ECO:0000312|Proteomes:UP000002417}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC BAA-1158 / Py2 {ECO:0000312|EMBL:CAA09915.1};
RX   PubMed=10103255; DOI=10.1128/aem.65.4.1589-1595.1999;
RA   Zhou N.Y., Jenkins A., Chan Kwo Chion C.K., Leak D.J.;
RT   "The alkene monooxygenase from Xanthobacter strain Py2 is closely related
RT   to aromatic monooxygenases and catalyzes aromatic monohydroxylation of
RT   benzene, toluene, and phenol.";
RL   Appl. Environ. Microbiol. 65:1589-1595(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2 {ECO:0000312|Proteomes:UP000002417};
RC   PLASMID=pXAUT01 {ECO:0000312|EMBL:ABS70072.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT   "Complete sequence of plasmid pXAUT01 of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBSTRATE
RP   SPECIFICITY.
RC   STRAIN=ATCC BAA-1158 / Py2;
RX   PubMed=1444418; DOI=10.1128/aem.58.9.3038-3046.1992;
RA   Ensign S.A., Hyman M.R., Arp D.J.;
RT   "Cometabolic degradation of chlorinated alkenes by alkene monooxygenase in
RT   a propylene-grown Xanthobacter strain.";
RL   Appl. Environ. Microbiol. 58:3038-3046(1992).
RN   [4]
RP   INDUCTION.
RC   STRAIN=ATCC BAA-1158 / Py2;
RX   PubMed=8572713; DOI=10.1128/aem.62.1.61-66.1996;
RA   Ensign S.A.;
RT   "Aliphatic and chlorinated alkenes and epoxides as inducers of alkene
RT   monooxygenase and epoxidase activities in Xanthobacter strain Py2.";
RL   Appl. Environ. Microbiol. 62:61-66(1996).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RC   STRAIN=ATCC BAA-1158 / Py2;
RX   PubMed=9312093; DOI=10.1074/jbc.272.40.24913;
RA   Small F.J., Ensign S.A.;
RT   "Alkene monooxygenase from Xanthobacter strain Py2. Purification and
RT   characterization of a four-component system central to the bacterial
RT   metabolism of aliphatic alkenes.";
RL   J. Biol. Chem. 272:24913-24920(1997).
CC   -!- FUNCTION: Component of the alkene monooxygenase multicomponent enzyme
CC       system which catalyzes the O2- and NADH-dependent epoxidation of short
CC       chain (C2 to C6) alkenes to their corresponding epoxides
CC       (PubMed:10103255, PubMed:1444418, PubMed:9312093). Also able to
CC       catalyze the oxidation of a number of chlorinated alkenes, including
CC       trichloroethylene, cis- and trans-1,2-dichloroethylene, vinyl chloride,
CC       1-chloropropylene, 1,3-dichloropropylene and 2,3-dichloropropylene
CC       (PubMed:1444418). {ECO:0000269|PubMed:10103255,
CC       ECO:0000269|PubMed:1444418, ECO:0000269|PubMed:9312093}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + O2 + propene = 1,2-epoxypropane + H2O + NAD(+);
CC         Xref=Rhea:RHEA:11792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16052, ChEBI:CHEBI:38685,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.69;
CC         Evidence={ECO:0000269|PubMed:1444418, ECO:0000269|PubMed:9312093};
CC   -!- ACTIVITY REGULATION: Inhibited by propyne.
CC       {ECO:0000269|PubMed:1444418}.
CC   -!- SUBUNIT: The alkene monooxygenase multicomponent enzyme system is
CC       composed of an electron transfer component and a monooxygenase
CC       component interacting with the effector protein XamoD. The electron
CC       transfer component is composed of a ferredoxin reductase (XamoF) and a
CC       ferredoxin (XamoC), and the monooxygenase component is formed by a
CC       heterohexamer (dimer of heterotrimers) of two alpha subunits (XamoA),
CC       two beta subunits (XamoE) and two gamma subunits (XamoB).
CC       {ECO:0000269|PubMed:9312093}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9312093}.
CC   -!- INDUCTION: Induced during growth on aliphatic alkenes (such as
CC       propylene, ethylene and 1-butylene), epoxides (such as propylene oxide
CC       and 1,2-epoxybutane) and chlorinated alkenes and epoxides (such as
CC       vinyl chloride, cis- and trans-1,2-dichloroethylene, 1-chloropropylene,
CC       1,3-dichloropropylene, epichlorohydrin, and epifluorohydrin). Repressed
CC       during growth on other carbon sources. {ECO:0000269|PubMed:8572713}.
CC   -!- SIMILARITY: Belongs to the TmoE/XamoE family. {ECO:0000305}.
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DR   EMBL; AJ012090; CAA09915.1; -; Genomic_DNA.
DR   EMBL; CP000782; ABS70072.1; -; Genomic_DNA.
DR   RefSeq; WP_011992976.1; NC_009717.1.
DR   AlphaFoldDB; Q9ZET3; -.
DR   SMR; Q9ZET3; -.
DR   STRING; 78245.Xaut_4861; -.
DR   EnsemblBacteria; ABS70072; ABS70072; Xaut_4861.
DR   KEGG; xau:Xaut_4861; -.
DR   eggNOG; ENOG502Z7R0; Bacteria.
DR   HOGENOM; CLU_061948_0_0_5; -.
DR   OMA; ESMYLAS; -.
DR   OrthoDB; 561064at2; -.
DR   PhylomeDB; Q9ZET3; -.
DR   BioCyc; MetaCyc:MON-13291; -.
DR   Proteomes; UP000002417; Plasmid pXAUT01.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0018645; F:alkene monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR   CDD; cd01058; AAMH_B; 1.
DR   Gene3D; 1.10.620.20; -; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012078; MP_mOase_hydro.
DR   InterPro; IPR003430; Phenol_Hydrox.
DR   InterPro; IPR012348; RNR-like.
DR   Pfam; PF02332; Phenol_Hydrox; 1.
DR   PIRSF; PIRSF000040; MMOH_comp; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Monooxygenase; NAD; Oxidoreductase; Plasmid; Reference proteome.
FT   CHAIN           1..341
FT                   /note="Alkene monooxygenase system, oxygenase component
FT                   subunit beta"
FT                   /id="PRO_0000442694"
SQ   SEQUENCE   341 AA;  38223 MW;  46FC7B78A11572CD CRC64;
     MTQQRPTRTR ERKKTWTAFG NLGRKPTDYE VVTHNMNHTM RGTPLELSPT VHANVWLKKN
     RDEIALKVDS WDLFRDPDRT TYDTYVKMQD DQETYVDNLL LSYTGEGRYD EELSSRSLDL
     LSAGLTPTRY LGHGLQMLAA YIQQLAPSAY VGNCAVFQTS DALRRVQRVA YRTRQLADAH
     PARGFGSGDR AVWEKSPDWQ PIRKAIEELL VTFEWDKALA GTNFVVKPIL DELFLNHLAR
     LLHVEGDELD SLVLRNLHGD AQRHARWTAA LGRFAVEQNV NNRTVLRDAI AGWHETGEAV
     LAAGAGMLAS RAPSADAAKI ADEVRATLAQ LHANAGLGHD A