XAMOC_XANP2
ID XAMOC_XANP2 Reviewed; 122 AA.
AC Q9ZET5;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Alkene monooxygenase system, ferredoxin component {ECO:0000303|PubMed:9312093};
DE AltName: Full=Alkene monooxygenase 13.3 kDa subunit {ECO:0000303|PubMed:9312093};
GN Name=xamoC {ECO:0000303|PubMed:10103255, ECO:0000312|EMBL:CAA09913.1};
GN Synonyms=aamC {ECO:0000303|PubMed:10103255};
GN OrderedLocusNames=Xaut_4859 {ECO:0000312|EMBL:ABS70070.1};
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OG Plasmid pXAUT01 {ECO:0000312|EMBL:ABS70070.1,
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:CAA09913.1};
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:ABS70070.1};
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 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 [4]
RP FUNCTION, 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: Ferredoxin component of the alkene monooxygenase
CC multicomponent enzyme system which catalyzes the O2- and NADH-dependent
CC epoxidation of short chain (C2 to C6) alkenes to their corresponding
CC epoxides (PubMed:10103255, PubMed:9312093). Functions as an
CC intermediate electron transfer protein (PubMed:9312093).
CC {ECO:0000269|PubMed:10103255, ECO:0000269|PubMed:9312093}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:9312093};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- SUBUNIT: Homodimer. The alkene monooxygenase multicomponent enzyme
CC system is composed of an electron transfer component and a
CC monooxygenase component interacting with the effector protein XamoD.
CC The electron transfer component is composed of a ferredoxin reductase
CC (XamoF) and a ferredoxin (XamoC), and the monooxygenase component is
CC formed by a heterohexamer (dimer of heterotrimers) of two alpha
CC subunits (XamoA), two beta subunits (XamoE) and two gamma subunits
CC (XamoB). {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 bacterial ring-hydroxylating dioxygenase
CC ferredoxin component family. {ECO:0000305}.
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DR EMBL; AJ012090; CAA09913.1; -; Genomic_DNA.
DR EMBL; CP000782; ABS70070.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZET5; -.
DR SMR; Q9ZET5; -.
DR STRING; 78245.Xaut_4859; -.
DR EnsemblBacteria; ABS70070; ABS70070; Xaut_4859.
DR KEGG; xau:Xaut_4859; -.
DR eggNOG; COG2146; Bacteria.
DR HOGENOM; CLU_055690_5_0_5; -.
DR OMA; ICKAHEW; -.
DR PhylomeDB; Q9ZET5; -.
DR BioCyc; MetaCyc:MON-13287; -.
DR Proteomes; UP000002417; Plasmid pXAUT01.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Plasmid; Reference proteome; Transport.
FT CHAIN 1..122
FT /note="Alkene monooxygenase system, ferredoxin component"
FT /id="PRO_0000442695"
FT DOMAIN 16..111
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 55
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 57
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 75
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 122 AA; 13392 MW; F8D69D591EB600E8 CRC64;
MNLHAPNAEQ DDIEYVDVCA VDDLWDGEMD VFDVGEHEVL LVKHEGRFHA YDGICPHQSV
SLVEGHLTED GVLICKAHEW QFSVEGGQGI NPANVCLQSF PLKVEGGRVL IGTEPLPKEG
EA
