ID S3K0D6_9ENTR Unreviewed; 381 AA.
AC S3K0D6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Alkanesulfonate monooxygenase {ECO:0000256|ARBA:ARBA00012113, ECO:0000256|HAMAP-Rule:MF_01229};
DE EC=1.14.14.5 {ECO:0000256|ARBA:ARBA00012113, ECO:0000256|HAMAP-Rule:MF_01229};
DE AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase {ECO:0000256|HAMAP-Rule:MF_01229};
GN Name=ssuD {ECO:0000256|HAMAP-Rule:MF_01229};
GN ORFNames=HMPREF0201_01334 {ECO:0000313|EMBL:EPF18729.1};
OS Cedecea davisae DSM 4568.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cedecea.
OX NCBI_TaxID=566551 {ECO:0000313|EMBL:EPF18729.1, ECO:0000313|Proteomes:UP000014585};
RN [1] {ECO:0000313|EMBL:EPF18729.1, ECO:0000313|Proteomes:UP000014585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4568 {ECO:0000313|EMBL:EPF18729.1,
RC ECO:0000313|Proteomes:UP000014585};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Palsikar V.B., Zhang X., Suruliraj S., Perna N.T., Plunkett G.,
RA Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates.
CC {ECO:0000256|HAMAP-Rule:MF_01229}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + 2 H(+) +
CC H2O + sulfite; Xref=Rhea:RHEA:23064, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17359,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:134249; EC=1.14.14.5; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01229};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01229}.
CC -!- MISCELLANEOUS: FMNH(2) which is absolutely required for this enzymatic
CC reaction, is provided by SsuE. {ECO:0000256|HAMAP-Rule:MF_01229}.
CC -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000256|ARBA:ARBA00007044,
CC ECO:0000256|HAMAP-Rule:MF_01229}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPF18729.1}.
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; ATDT01000006; EPF18729.1; -; Genomic_DNA.
DR RefSeq; WP_016535648.1; NZ_KE161030.1.
DR AlphaFoldDB; S3K0D6; -.
DR STRING; 566551.HMPREF0201_01334; -.
DR PATRIC; fig|566551.4.peg.1232; -.
DR HOGENOM; CLU_027853_1_0_6; -.
DR OrthoDB; 9814695at2; -.
DR Proteomes; UP000014585; Unassembled WGS sequence.
DR GO; GO:0008726; F:alkanesulfonate monooxygenase activity; IEA:UniProtKB-UniRule.
DR CDD; cd01094; Alkanesulfonate_monoxygenase; 1.
DR Gene3D; 3.20.20.30; Luciferase-like domain; 1.
DR HAMAP; MF_01229; Alkanesulf_monooxygen; 1.
DR InterPro; IPR019911; Alkanesulphonate_mOase_FMN-dep.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR NCBIfam; TIGR03565; alk_sulf_monoox; 1.
DR PANTHER; PTHR42847; ALKANESULFONATE MONOOXYGENASE; 1.
DR PANTHER; PTHR42847:SF4; ALKANESULFONATE MONOOXYGENASE-RELATED; 1.
DR Pfam; PF00296; Bac_luciferase; 1.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01229};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01229};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW Rule:MF_01229};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01229}.
FT DOMAIN 4..325
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
SQ SEQUENCE 381 AA; 41765 MW; ACF03F0CF3DA1539 CRC64;
MSLNLFWFLP THGDGHYLGS NEGARPVDHA YLQQIAQAAD RLGFTGVLIP TGRSCEDAWL
VAASMIPVTQ RLKFLVALRP SVVSPTLAAR QAATLDRLSN GRALFNLVTG GDAEELEGEG
VFLNHEERYE ASAEFTRIWR RVLEGETVDY EGKHIKVKGA KLLYPPVQQP RPPLYFGGSS
DAAQDLAAEQ VDLYLTWGEP PHLVKEKIEQ VRAKAAAQGR QVRFGIRLHV IVRETTQEAW
QAANRLISHL DDLTIAKAQA AFARSDSVGQ HRMAALHGGK RDKLEISPNL WAGVGLVRGG
AGTALVGDGP TVAARINEYA ELGIDSFILS GYPHLEEVYR AGELLFPHLD VAIPEIPQPR
QVQEKGEVVA NDFIPRKVAQ S
//
