XAMOF_XANP2
ID XAMOF_XANP2 Reviewed; 327 AA.
AC A7IPX7; Q9ZET2;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Alkene monooxygenase system, ferredoxin--NAD(+) reductase component {ECO:0000303|PubMed:10103255};
DE EC=1.18.1.3 {ECO:0000269|PubMed:9312093};
DE AltName: Full=Alkene monooxygenase 35.5 kDa subunit {ECO:0000303|PubMed:9312093};
DE AltName: Full=Alkene monooxygenase system, electron transfer component {ECO:0000303|PubMed:9312093};
DE AltName: Full=Ferredoxin--NAD(+) reductase {ECO:0000305};
GN Name=xamoF {ECO:0000303|PubMed:10103255, ECO:0000312|EMBL:CAA09916.1};
GN Synonyms=aamF {ECO:0000303|PubMed:10103255};
GN OrderedLocusNames=Xaut_4862 {ECO:0000312|EMBL:ABS70073.1};
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OG Plasmid pXAUT01 {ECO:0000312|EMBL:ABS70073.1,
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:CAA09916.1};
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:ABS70073.1};
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, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, SUBSTRATE
RP SPECIFICITY, 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: Reductase 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). Ferredoxin reductase
CC catalyzes the transfer of electrons from NADH to ferredoxin (XamoC)
CC (PubMed:9312093). NADPH is also effective but with a rate approximately
CC 3-fold lower than with NADH (PubMed:9312093).
CC {ECO:0000269|PubMed:10103255, ECO:0000269|PubMed:9312093}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.18.1.3;
CC Evidence={ECO:0000269|PubMed:9312093};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={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. {ECO:0000255|PROSITE-ProRule:PRU00465};
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 bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABS70073.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ012090; CAA09916.1; -; Genomic_DNA.
DR EMBL; CP000782; ABS70073.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A7IPX7; -.
DR SMR; A7IPX7; -.
DR STRING; 78245.Xaut_4862; -.
DR EnsemblBacteria; ABS70073; ABS70073; Xaut_4862.
DR KEGG; xau:Xaut_4862; -.
DR eggNOG; COG0543; Bacteria.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_7_0_5; -.
DR PhylomeDB; A7IPX7; -.
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:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW NAD; Oxidoreductase; Plasmid; Reference proteome.
FT CHAIN 1..327
FT /note="Alkene monooxygenase system, ferredoxin--NAD(+)
FT reductase component"
FT /id="PRO_0000442696"
FT DOMAIN 1..89
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 96..194
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 32
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 37
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 40
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 73
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 327 AA; 34205 MW; 553B7D827145E694 CRC64;
MRLNDGRSFS CRSDQTVLHA ALAAGIDMPY ECASGSCGSC RCRLSHGSVS LLWPEAPGLS
ARDRQKGDRI LACQSTPSSD LEINVRAGDA LLEPPPRRHA ARVTVKETLC ASVIRLVLNV
GGPIHFLPGQ FFILDLPGAG RRAYSVANLE NAAGGIELLI KRKIGGAGTA ALFDQCAPGM
GLVIEGPYGR AYLRADSARG IVAVAGGSGL APMLSILRGA LARGFGGPMD LYFGVNTAEE
LFCVPELSAL QAAGARVHLA LRDGGPGPAG LHRQAGLIGD ALVAGEPDLK AKDLYVAGPA
PMTDDILART VRQEAIPADR VFFDRFV
