DMOA_HYPSL
ID DMOA_HYPSL Reviewed; 480 AA.
AC E9JFX9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Dimethyl-sulfide monooxygenase;
DE EC=1.14.13.131;
DE AltName: Full=Dimethylsulfide monooxygenase large subunit;
GN Name=dmoA;
OS Hyphomicrobium sulfonivorans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=121290;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=ATCC BAA-113 / DSM 13863 / S1;
RX PubMed=21216999; DOI=10.1128/jb.00977-10;
RA Boden R., Borodina E., Wood A.P., Kelly D.P., Murrell J.C., Schafer H.;
RT "Purification and characterization of dimethylsulfide monooxygenase from
RT Hyphomicrobium sulfonivorans.";
RL J. Bacteriol. 193:1250-1258(2011).
CC -!- FUNCTION: Monooxygenase that mediates oxidation of dimethyl sulfide,
CC the first step in dimethyl sulfide degradation pathway. Has much lower
CC activity with diethyl sulfide and other short-chain alkyl methyl
CC sulfides. {ECO:0000269|PubMed:21216999}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethyl sulfide + H(+) + NADH + O2 = formaldehyde + H2O +
CC methanethiol + NAD(+); Xref=Rhea:RHEA:31355, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16007,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:17437, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.14.13.131;
CC Evidence={ECO:0000269|PubMed:21216999};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:21216999};
CC -!- ACTIVITY REGULATION: Inhibited by umbelliferone, 8-
CC anilinonaphthalenesulfonate, a range of metal-chelating agents, and
CC Hg(2+), Cd(2+) and Pb(2+) ions. {ECO:0000269|PubMed:21216999}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17.2 uM for Dimethyl sulfide;
CC Vmax=1.25 umol/min/mg enzyme;
CC -!- SUBUNIT: Heterodimer of 2 subunits, DmoA and DmoB.
CC {ECO:0000269|PubMed:21216999}.
CC -!- MISCELLANEOUS: DmoB has not been identified yet. Only a peptide from
CC the protein encoded by a putative flavin reductase (AC E0XCR3) was
CC obtained by mass spectrometry, which is insufficient for linking this
CC gene to DmoB (PubMed:21216999). {ECO:0000305|PubMed:21216999}.
CC -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GQ980036; ADU77278.1; -; Genomic_DNA.
DR PDB; 6AK1; X-ray; 2.28 A; A/B=1-480.
DR PDBsum; 6AK1; -.
DR AlphaFoldDB; E9JFX9; -.
DR SMR; E9JFX9; -.
DR STRING; 121290.APY04_0470; -.
DR KEGG; ag:ADU77278; -.
DR BioCyc; MetaCyc:MON-16507; -.
DR BRENDA; 1.14.13.131; 12611.
DR GO; GO:0018633; F:dimethyl sulfide monooxygenase activity; IDA:CACAO.
DR CDD; cd01095; Nitrilotriacetate_monoxgenase; 1.
DR Gene3D; 3.20.20.30; -; 1.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR InterPro; IPR016215; NTA_MOA.
DR Pfam; PF00296; Bac_luciferase; 1.
DR PIRSF; PIRSF000337; NTA_MOA; 1.
DR SUPFAM; SSF51679; SSF51679; 1.
DR TIGRFAMs; TIGR03860; FMN_nitrolo; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; Monooxygenase; NAD; Oxidoreductase.
FT CHAIN 1..480
FT /note="Dimethyl-sulfide monooxygenase"
FT /id="PRO_0000418929"
FT REGION 423..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:O34974"
FT BINDING 104
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:O34974"
FT BINDING 154..158
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:O34974"
FT BINDING 227..230
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:O34974"
FT STRAND 6..21
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:6AK1"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:6AK1"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:6AK1"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:6AK1"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:6AK1"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 157..173
FT /evidence="ECO:0007829|PDB:6AK1"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:6AK1"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:6AK1"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6AK1"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:6AK1"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 232..240
FT /evidence="ECO:0007829|PDB:6AK1"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 251..267
FT /evidence="ECO:0007829|PDB:6AK1"
FT STRAND 274..284
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 289..300
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 305..316
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 335..344
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:6AK1"
FT TURN 363..367
FT /evidence="ECO:0007829|PDB:6AK1"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 375..387
FT /evidence="ECO:0007829|PDB:6AK1"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 403..411
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 413..418
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 431..435
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 448..452
FT /evidence="ECO:0007829|PDB:6AK1"
FT TURN 453..458
FT /evidence="ECO:0007829|PDB:6AK1"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:6AK1"
SQ 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
