XAMOD_XANP2
ID XAMOD_XANP2 Reviewed; 101 AA.
AC Q9ZET4;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Alkene monooxygenase system, effector subunit {ECO:0000303|PubMed:10103255};
DE AltName: Full=Alkene monooxygenase 11 kDa subunit {ECO:0000303|PubMed:9312093};
GN Name=xamoD {ECO:0000303|PubMed:10103255, ECO:0000312|EMBL:CAA09914.1};
GN Synonyms=aamD {ECO:0000303|PubMed:10103255};
GN OrderedLocusNames=Xaut_4860 {ECO:0000312|EMBL:ABS70071.1};
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OG Plasmid pXAUT01 {ECO:0000312|EMBL:ABS70071.1,
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:CAA09914.1};
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:ABS70071.1};
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, 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: Effector component of the alkene monooxygenase multicomponent
CC enzyme system which catalyzes the O2- and NADH-dependent epoxidation of
CC short chain (C2 to C6) alkenes to their corresponding epoxides
CC (PubMed:10103255, PubMed:9312093). One possible role of this small
CC protein might be to facilitate electron transfer between the reductase
CC and ferredoxin components (PubMed:9312093).
CC {ECO:0000269|PubMed:10103255, ECO:0000269|PubMed:9312093}.
CC -!- SUBUNIT: Monomer. The alkene monooxygenase multicomponent enzyme system
CC is 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 TmoD/XamoD family. {ECO:0000305}.
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DR EMBL; AJ012090; CAA09914.1; -; Genomic_DNA.
DR EMBL; CP000782; ABS70071.1; -; Genomic_DNA.
DR RefSeq; WP_011992975.1; NC_009717.1.
DR AlphaFoldDB; Q9ZET4; -.
DR SMR; Q9ZET4; -.
DR STRING; 78245.Xaut_4860; -.
DR EnsemblBacteria; ABS70071; ABS70071; Xaut_4860.
DR KEGG; xau:Xaut_4860; -.
DR eggNOG; COG3445; Bacteria.
DR HOGENOM; CLU_148539_1_0_5; -.
DR OMA; FAGRMRY; -.
DR OrthoDB; 1816585at2; -.
DR PhylomeDB; Q9ZET4; -.
DR BioCyc; MetaCyc:MON-13286; -.
DR Proteomes; UP000002417; Plasmid pXAUT01.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR Gene3D; 3.90.56.10; -; 1.
DR InterPro; IPR003454; MOase_MmoB_DmpM.
DR InterPro; IPR036889; mOase_MmoB_DmpM_sf.
DR Pfam; PF02406; MmoB_DmpM; 1.
DR SUPFAM; SSF56029; SSF56029; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Plasmid; Reference proteome.
FT CHAIN 1..101
FT /note="Alkene monooxygenase system, effector subunit"
FT /id="PRO_0000442693"
SQ SEQUENCE 101 AA; 11195 MW; 01F19FF8A3C853CC CRC64;
MSNATVDDMD ENLVGPVIRA GDLADAVIDA VIADNPGKEV HVIERGDYVR IHTDRDCRLT
RASIEQALGR SFVLAAIEAE MSSFKGRMSS SDSEMRWYYK S