ID A0A371PIC9_9BACL Unreviewed; 379 AA.
AC A0A371PIC9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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 ECO:0000313|EMBL:REK75971.1};
GN ORFNames=DX130_02540 {ECO:0000313|EMBL:REK75971.1};
OS Paenibacillus paeoniae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2292705 {ECO:0000313|EMBL:REK75971.1, ECO:0000313|Proteomes:UP000261905};
RN [1] {ECO:0000313|EMBL:REK75971.1, ECO:0000313|Proteomes:UP000261905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M4BSY-1 {ECO:0000313|EMBL:REK75971.1,
RC ECO:0000313|Proteomes:UP000261905};
RA Tuo L.;
RT "Paenibacillus sp. M4BSY-1, whole genome shotgun sequence.";
RL Submitted (AUG-2018) 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 -!- 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:REK75971.1}.
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DR EMBL; QUBQ01000001; REK75971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371PIC9; -.
DR OrthoDB; 9814695at2; -.
DR Proteomes; UP000261905; 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}; Reference proteome {ECO:0000313|Proteomes:UP000261905}.
FT DOMAIN 1..323
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
SQ SEQUENCE 379 AA; 41808 MW; 9669451264EA108C CRC64;
MELFWFIPLH GDGRYLGTSK GARALDFDYI RQIAQASDRL GYHGVLVPTG KACEDAWIAA
SSLISATQNL KFLVAVRPGL MSPSAAARMA STFDRLSGGR LLVNVVTGGD PHELGGDGIF
LSHSERYEQT DEFMTIWRRL MEGEEVNFAG KYLRIESGEV MFPALQKPYP PIYFGGSSPS
ALRIAADHVD YYLTWGEPPA EVAKKLEDVR RLAEASGRKV KFGIRLHVIV RETEEEAWDA
ANRLIQHVDE GTIEEAQRIL SRYDSVGQRR MGDLHKGDKT SLEISPNLWA GIGLVRGGAG
TALVGDADNV AARIQEYKEL GIETFILSGY PHLEEAYRTA ELLFPKLPLS PRQIAETAGI
PAIGEIVAYN KRPRAALQP
//
