ID SSUD_RHIE6 Reviewed; 389 AA.
AC B3Q1C3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
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};
GN OrderedLocusNames=RHECIAT_PA0000133;
OS Rhizobium etli (strain CIAT 652).
OG Plasmid pA.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652;
RX PubMed=20048063; DOI=10.1128/aem.02039-09;
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P., Fernandez J.L.,
RA Hernandez Gonzalez I.L., Diaz R., Flores M., Palacios R., Mora J.,
RA Davila G.;
RT "Conserved symbiotic plasmid DNA sequences in the multireplicon pangenomic
RT structure of Rhizobium etli.";
RL Appl. Environ. Microbiol. 76:1604-1614(2010).
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}.
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DR EMBL; CP001075; ACE93479.1; -; Genomic_DNA.
DR AlphaFoldDB; B3Q1C3; -.
DR SMR; B3Q1C3; -.
DR KEGG; rec:RHECIAT_PA0000133; -.
DR HOGENOM; CLU_027853_1_0_5; -.
DR Proteomes; UP000008817; Plasmid pA.
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; FMN; Monooxygenase; Oxidoreductase; Plasmid.
FT CHAIN 1..389
FT /note="Alkanesulfonate monooxygenase"
FT /id="PRO_0000403216"
SQ SEQUENCE 389 AA; 41586 MW; 125C86A4B32F2A2C CRC64;
MMAIDKPLDF LWFIPSSGDG QYLGSDDLSR PADPGYFREI AKAADRLGYS GVLIPTGAAC
EESFILAADL AAHTERLKFL VAIRPGTASP AYYARLAATL DRVSNGRLLI NIVVGGSAQE
LAGDGIFLPH DERYDHAGEF FQVFNSLVET GKANLDGKYI KAIDARLGLP PVQEPRPPLY
FGGSSDAAIA FSGGITDKYL TWGEPPAQVA EKIAKVRKAA AAQGKHVTFG IRLHFIVRET
DEEAWAAADR LISKLSDETI AAAQEVFAKS SDSVGQARMV ALHQGRRDKL EVSPNLWAGI
GLVRTGAGTA LVGSPKTIAE RLREYQALGI DTVIASGYPH LEEAYRVSEL LFPEIGLPGP
HGQIRSSFGE RRVFGGGGHG GNVKIASAS
//
