ID A0A063BEJ6_9BURK Unreviewed; 385 AA.
AC A0A063BEJ6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=LIG30_2106 {ECO:0000313|EMBL:KDB08796.1};
OS Burkholderia sp. lig30.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1192124 {ECO:0000313|EMBL:KDB08796.1, ECO:0000313|Proteomes:UP000027020};
RN [1] {ECO:0000313|EMBL:KDB08796.1, ECO:0000313|Proteomes:UP000027020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LIG30 {ECO:0000313|Proteomes:UP000027020};
RA Woo H.L., Utturkar S.M., Klingeman D.M., Simmons B.A., DeAngelis K.M.,
RA Brown S.D., Hazen T.C.;
RT "Draft Genome of the Lignin-degrading Burkholderia sp. Strain LIG30,
RT Isolated from Wet Tropical Forest Soil.";
RL Submitted (MAR-2014) 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:KDB08796.1}.
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DR EMBL; JGVW01000067; KDB08796.1; -; Genomic_DNA.
DR RefSeq; WP_038711541.1; NZ_JGVW01000067.1.
DR AlphaFoldDB; A0A063BEJ6; -.
DR STRING; 1192124.LIG30_2106; -.
DR PATRIC; fig|1192124.4.peg.1937; -.
DR eggNOG; COG2141; Bacteria.
DR OrthoDB; 9814695at2; -.
DR Proteomes; UP000027020; 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:UP000027020}.
FT DOMAIN 1..330
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
SQ SEQUENCE 385 AA; 41796 MW; F774887DF32E5237 CRC64;
MNVFWFIPTH GDSRYLGTTE GARAADYDYF KQVAVAADTL GYEGVLLPTG RSCEDAWVVA
SSLIPATRRL KFLVAVRPGV ALPALSARMA ATFDRLSGGR LLINVVTGGD AAELEGDGLF
ADHDTRYRIT DDFLHIWRGL LSASHDSGSF DYIGSHLQLK GGKALYPPVQ RPHPPLWFGG
SSPAAHAIAA DHIDTYLTWG EPPEAVAKKI ADVRASAAER GRQIKFGIRL HVIVRETEEE
AWADADRLIS RLDDDTVARA QQVFANMDSE GQRRMAALHG GKRGGRKELE VYPNLWAGVG
LVRGGAGTAL VGNPEQVAAR MREYAELGIE TFILSGYPHL EESYRFAELV FPLIKGRDAA
NSTGALSGPR GEIVGNNYVP RASQS
//