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Dimethyl-sulfide monooxygenase (EC 1.14.13.131) (Dimethylsulfide monooxygenase large subunit)

 DMOA_HYPSL              Reviewed;         480 AA.
E9JFX9;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
05-APR-2011, sequence version 1.
12-SEP-2018, entry version 24.
RecName: Full=Dimethyl-sulfide monooxygenase;
EC=1.14.13.131;
AltName: Full=Dimethylsulfide monooxygenase large subunit;
Name=dmoA;
Hyphomicrobium sulfonivorans.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Hyphomicrobiaceae; Hyphomicrobium.
NCBI_TaxID=121290;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
SUBUNIT, COFACTOR, AND ACTIVITY REGULATION.
STRAIN=ATCC BAA-113 / DSM 13863 / S1;
PubMed=21216999; DOI=10.1128/JB.00977-10;
Boden R., Borodina E., Wood A.P., Kelly D.P., Murrell J.C.,
Schafer H.;
"Purification and characterization of dimethylsulfide monooxygenase
from Hyphomicrobium sulfonivorans.";
J. Bacteriol. 193:1250-1258(2011).
-!- FUNCTION: Monooxygenase that mediates oxidation of dimethyl
sulfide, the first step in dimethyl sulfide degradation pathway.
Has much lower activity with diethyl sulfide and other short-chain
alkyl methyl sulfides. {ECO:0000269|PubMed:21216999}.
-!- CATALYTIC ACTIVITY: Dimethyl sulfide + O(2) + NADH = methanethiol
+ formaldehyde + NAD(+) + H(2)O. {ECO:0000269|PubMed:21216999}.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:21216999};
-!- ACTIVITY REGULATION: Inhibited by umbelliferone, 8-
anilinonaphthalenesulfonate, a range of metal-chelating agents,
and Hg(2+), Cd(2+) and Pb(2+) ions. {ECO:0000269|PubMed:21216999}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=17.2 uM for Dimethyl sulfide;
Vmax=1.25 umol/min/mg enzyme;
-!- SUBUNIT: Heterodimer of 2 subunits, DmoA and DmoB.
{ECO:0000269|PubMed:21216999}.
-!- MISCELLANEOUS: DmoB has not been identified yet. Only a peptide
from the protein encoded by a putative flavin reductase (AC
E0XCR3) was obtained by mass spectrometry, which is insufficient
for linking this gene to DmoB (PubMed:21216999).
{ECO:0000305|PubMed:21216999}.
-!- SIMILARITY: Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase
family. {ECO:0000305}.
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EMBL; GQ980036; ADU77278.1; -; Genomic_DNA.
ProteinModelPortal; E9JFX9; -.
SMR; E9JFX9; -.
KEGG; ag:ADU77278; -.
KO; K16967; -.
BioCyc; MetaCyc:MONOMER-16507; -.
BRENDA; 1.14.13.131; 12611.
GO; GO:0018633; F:dimethyl sulfide monooxygenase activity; IDA:CACAO.
CDD; cd01095; Nitrilotriacetate_monoxgenase; 1.
Gene3D; 3.20.20.30; -; 1.
InterPro; IPR011251; Luciferase-like_dom.
InterPro; IPR036661; Luciferase-like_sf.
InterPro; IPR016215; NTA_MOA.
Pfam; PF00296; Bac_luciferase; 1.
PIRSF; PIRSF000337; NTA_MOA; 1.
SUPFAM; SSF51679; SSF51679; 1.
TIGRFAMs; TIGR03860; FMN_nitrolo; 1.
1: Evidence at protein level;
Flavoprotein; FMN; Monooxygenase; NAD; Oxidoreductase.
CHAIN 1 480 Dimethyl-sulfide monooxygenase.
/FTId=PRO_0000418929.
NP_BIND 154 158 FMN binding. {ECO:0000250}.
NP_BIND 227 230 FMN binding. {ECO:0000250}.
BINDING 58 58 FMN; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 104 104 FMN. {ECO:0000250}.
SEQUENCE 480 AA; 53116 MW; 0AEC2DE5548A33FF CRC64;
MKKRIVLNAF DMTCVSHQSA GTWRHPSSQA ARYNDLEYWT NMAMELERGC FDCLFIADVV
GVYDVYRGSA EMALRDADQV PVNDPFGAIS AMAAVTEHVG FGVTAAITFE QPYLLARRLS
TLDHLTKGRV AWNVVSSYLN SAALNIGMDQ QLAHDERYEM ADEYMEVMYK LWEGSWEDDA
VKRDKKSGVF TDGSKVHPIN HQGKYYKVPG FHICEPSPQR TPVIFQAGAS GRGSKFAASN
AEGMFILTTS VEQARQITTD IRNQAEAAGR SRDSIKIFML LTVITGDSDE AAEAKYQEYL
SYANPEGMLA LYGGWTGIDF AKLDPDEPLQ AMENDSLRTT LESLTHGENA KKWTVRDVIR
ERCIGGLGPV LVGGPQKVAD ELERWVDEGG VDGFNLAYAV TPGSVTDFID YIVPELRKRG
RAQDSYKPGS LRRKLIGTND GRVESTHPAA QYRDAYVGKE SVADRTQPSP FANAKAPVAE


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