ID A0A2S2FHD8_9GAMM Unreviewed; 391 AA.
AC A0A2S2FHD8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:AWL30364.1};
GN ORFNames=DJ533_18275 {ECO:0000313|EMBL:AWL30364.1};
OS Acinetobacter defluvii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1871111 {ECO:0000313|EMBL:AWL30364.1, ECO:0000313|Proteomes:UP000245977};
RN [1] {ECO:0000313|Proteomes:UP000245977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCHA30 {ECO:0000313|Proteomes:UP000245977};
RA Hu Y., Qin J., Feng Y., Zong Z.;
RT "The complete genome of Acinetobacter defluvii strain WCHAD010030.";
RL Submitted (MAY-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}.
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DR EMBL; CP029397; AWL30364.1; -; Genomic_DNA.
DR RefSeq; WP_065994547.1; NZ_CP029397.2.
DR AlphaFoldDB; A0A2S2FHD8; -.
DR STRING; 1871111.GCA_001704615_00642; -.
DR KEGG; adv:DJ533_18275; -.
DR OrthoDB; 9814695at2; -.
DR Proteomes; UP000245977; Chromosome.
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:UP000245977}.
FT DOMAIN 1..327
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
SQ SEQUENCE 391 AA; 43346 MW; 28203600864D7B9B CRC64;
MKIFWFIPTH GDSRYLGTSK GARQVDHAYM KQIAVAVDNL GYEGVLIPTG RSCEDPWITA
ASLIDATKNL KFLVALRPGV TTPALAARMA ATFDRLSNGR IRLNLVTGGD EQELKGDGLY
EDHATRYKTA AEYTTIWREI LTRSHTAESF TFHGEQLSVD DAKLLYPPIQ KPYPPLWFGG
SSEDALELAA EQVDTYLTWG EPPAAVKEKI TAVKAKADAK GRTLNYGIRL HVIVRETNEQ
AWQAAEELIQ YVDDATIAAA QKKFKHMDSV GQRRMAELHN GDRTKLEVSP NLWAGVGLVR
GGAGTALVGD PQTVAERIQE YADLGISTFI FSGYPHLEES IRFAELVFPL LPLETREKLA
QPNLTGPFGE IVANNYVPEE TKYKKPEKEL A
//
