SSUD_CUPNH
ID SSUD_CUPNH Reviewed; 387 AA.
AC Q0K9I0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Alkanesulfonate monooxygenase {ECO:0000255|HAMAP-Rule:MF_01229};
DE EC=1.14.14.5 {ECO:0000255|HAMAP-Rule:MF_01229};
DE AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase {ECO:0000255|HAMAP-Rule:MF_01229};
GN Name=ssuD {ECO:0000255|HAMAP-Rule:MF_01229}; OrderedLocusNames=H16_A2244;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
CC -!- FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates.
CC {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01229};
CC -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000255|HAMAP-
CC Rule:MF_01229}.
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; AM260479; CAJ93341.1; -; Genomic_DNA.
DR RefSeq; WP_011615572.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0K9I0; -.
DR SMR; Q0K9I0; -.
DR STRING; 381666.H16_A2244; -.
DR EnsemblBacteria; CAJ93341; CAJ93341; H16_A2244.
DR GeneID; 57644373; -.
DR KEGG; reh:H16_A2244; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_1_0_4; -.
DR OMA; NIFWFLP; -.
DR OrthoDB; 919913at2; -.
DR Proteomes; UP000008210; Chromosome 1.
DR GO; GO:0008726; F:alkanesulfonate monooxygenase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.30; -; 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 Pfam; PF00296; Bac_luciferase; 1.
DR SUPFAM; SSF51679; SSF51679; 1.
DR TIGRFAMs; TIGR03565; alk_sulf_monoox; 1.
PE 3: Inferred from homology;
KW Flavoprotein; FMN; Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..387
FT /note="Alkanesulfonate monooxygenase"
FT /id="PRO_1000066832"
SQ SEQUENCE 387 AA; 41893 MW; 18305833343DE89B CRC64;
MQVFWFIPTH GDSRYLGTSE GAREVSFDYL KQVAVAADTL GYEGVLIPTG RSCEDPWVAA
SALAAVTQRL KFLVAVRPGL MAPTLAARMA ATFDRISNGR LLINLVTGGD TAELEGDGLF
LDHTARYEAS AEFLRIWRQV LAASHDGDKV DYEGKHLSVK GATVLYPPLQ QPHPPVYFGG
SSAPAHALAG EQVDTYLTWG EPPADVAQKL DDVRRQAARH GRTVKFGIRL HVIVRETEAA
AWAAADDLIS RLDDETVARA QAVFAKMDSE GQRRMAALHA GGARRTREAL EISPNLWAGV
GLVRGGAGTA LVGDPHTVAE RMREYAELGI DTFVLSGYPH LEEAYRFAEL VFPLLPRSVR
DKLPGKVLSG PFGEVMATGI VPRAAQS