XAMOA_XANP2
ID XAMOA_XANP2 Reviewed; 497 AA.
AC O87082;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Alkene monooxygenase system, oxygenase component subunit alpha {ECO:0000303|PubMed:10103255};
DE EC=1.14.13.69 {ECO:0000269|PubMed:1444418, ECO:0000269|PubMed:9312093};
GN Name=xamoA {ECO:0000303|PubMed:9688534, ECO:0000312|EMBL:CAA07366.1};
GN Synonyms=aamA {ECO:0000303|PubMed:10103255};
GN OrderedLocusNames=Xaut_4857 {ECO:0000312|EMBL:ABS70068.1};
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OG Plasmid pXAUT01 {ECO:0000312|EMBL:ABS70068.1,
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 COFACTOR.
RC STRAIN=ATCC BAA-1158 / Py2 {ECO:0000312|EMBL:CAA07366.1};
RX PubMed=9688534; DOI=10.1016/s0014-5793(98)00653-x;
RA Zhou N.Y., Jenkins A., Chion C.K.N.C.K.;
RT "The alkene monooxygenase from Xanthobacter Py2 is a binuclear non-haem
RT iron protein closely related to toluene 4-monooxygenase.";
RL FEBS Lett. 430:181-185(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC BAA-1158 / Py2 {ECO:0000312|EMBL:CAA09911.1};
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2 {ECO:0000312|Proteomes:UP000002417};
RC PLASMID=pXAUT01 {ECO:0000312|EMBL:ABS70068.1};
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 [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, 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 -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:9312093};
CC Note=Binds 2 Fe(2+) ions per subunit (PubMed:9312093). The two iron
CC ions could form a binuclear cluster (Probable).
CC {ECO:0000269|PubMed:9312093, ECO:0000305|PubMed:9688534};
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 TmoA/XamoA family. {ECO:0000305}.
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DR EMBL; AJ006979; CAA07366.1; -; Genomic_DNA.
DR EMBL; AJ012090; CAA09911.1; -; Genomic_DNA.
DR EMBL; CP000782; ABS70068.1; -; Genomic_DNA.
DR RefSeq; WP_011992972.1; NC_009717.1.
DR AlphaFoldDB; O87082; -.
DR SMR; O87082; -.
DR STRING; 78245.Xaut_4857; -.
DR EnsemblBacteria; ABS70068; ABS70068; Xaut_4857.
DR KEGG; xau:Xaut_4857; -.
DR eggNOG; COG3350; Bacteria.
DR HOGENOM; CLU_040795_0_0_5; -.
DR OMA; PTVWWNP; -.
DR OrthoDB; 147428at2; -.
DR PhylomeDB; O87082; -.
DR BioCyc; MetaCyc:MON-13290; -.
DR BRENDA; 1.14.13.69; 1641.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR003430; Phenol_Hydrox.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR007029; YHS_dom.
DR Pfam; PF02332; Phenol_Hydrox; 1.
DR Pfam; PF04945; YHS; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Iron; Metal-binding; Monooxygenase; NAD; Oxidoreductase;
KW Plasmid; Reference proteome.
FT CHAIN 1..497
FT /note="Alkene monooxygenase system, oxygenase component
FT subunit alpha"
FT /id="PRO_0000442691"
FT BINDING 104
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 137
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
FT BINDING 234
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00456"
SQ SEQUENCE 497 AA; 58041 MW; F2B9A7E88D3A6B18 CRC64;
MALLNRDDWY DIARDVDWTL SYVDRAVAFP EEWKGEKDIC GTAWDDWDEP FRVSFREYVM
VQRDKEASVG AIREAMVRAK AYEKLDDGHK ATSHLHMGTI TMVEHMAVTM QSRFVRFAPS
ARWRSLGAFG MLDETRHTQL DLRFSHDLLN DSPSFDWSQR AFHTDEWAVL ATRNLFDDIM
LNADCVEAAL ATSLTLEHGF TNIQFVALAS DAMEAGDVNF SNLLSSIQTD EARHAQLGFP
TLDVMMKHDP KRAQQILDVA FWRSYRIFQA VTGVSMDYYT PVAKRQMSFK EFMLEWIVKH
HERILRDYGL QKPWYWDTFE KTLDHGHHAL HIGTWFWRPT LFWDPNGGVS REERRWLNQK
YPNWEESWGV LWDEIISNIN AGNIEKTLPE TLPMLCNVTN LPIGSHWDRF HLKPEQLVYK
GRLYTFDSDV SKWIFELDPE RYAGHTNVVD RFIGGQIQPM TIEGVLNWMG LTPEVMGKDV
FNYRWAGDYA ENRIAAE
