ID E6WJR0_PANSA Unreviewed; 390 AA.
AC E6WJR0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
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 OrderedLocusNames=Pat9b_5163 {ECO:0000313|EMBL:ADU71322.1};
OS Pantoea sp. (strain At-9b).
OG Plasmid pPAT9B01 {ECO:0000313|EMBL:ADU71322.1,
OG ECO:0000313|Proteomes:UP000001624}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU71322.1, ECO:0000313|Proteomes:UP000001624};
RN [1] {ECO:0000313|EMBL:ADU71322.1, ECO:0000313|Proteomes:UP000001624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=At-9b {ECO:0000313|EMBL:ADU71322.1,
RC ECO:0000313|Proteomes:UP000001624};
RC PLASMID=Plasmid pPAT9B01 {ECO:0000313|Proteomes:UP000001624};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT "Complete sequence plasmid1 of Pantoea sp. At-9b.";
RL Submitted (DEC-2010) 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}.
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DR EMBL; CP002434; ADU71322.1; -; Genomic_DNA.
DR RefSeq; WP_013511153.1; NC_014838.1.
DR AlphaFoldDB; E6WJR0; -.
DR KEGG; pao:Pat9b_5163; -.
DR HOGENOM; CLU_027853_1_0_6; -.
DR OrthoDB; 9814695at2; -.
DR Proteomes; UP000001624; Plasmid pPAT9B01.
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}; Plasmid {ECO:0000313|EMBL:ADU71322.1}.
FT DOMAIN 10..331
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
FT REGION 363..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 390 AA; 42202 MW; 86A7CD478E547F92 CRC64;
MADSVNENIN VFWFLPTHGD GRYLGTTEGG RPVDLGYLQQ VALAADNLGF YGVLIPTGKS
CEDSWLVASA LAPLTRRLRY LVAVRPGLQP PTLAARMAST LDRLSDGRLL INVVTGGDPI
ENKGDGIFLS HSERYAVTKE FLDVYSRLLR GEKVDYKGQH IHVEGAEVLF PPVQENGPPL
YFGGSSDEAI DVAAGQIDTY LTWGEPPAQV AEKLAVVRAR AEARGRKLEY GIRLHVIVRE
TEEEAKAAAD KLIAHLDEET IAQAQKIFAR MDSAGQARMS ALHNGSRDNL YIAPNLWAGV
GLVRGGAGTA LVGSPEQVAA RIREYQALGV TNFILSGYPH LEEAHRVAEL LLPLLPLAHG
QQQRARSVNT GPFGETIGGD KRPTKQASAS
//
