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Database: UniProt
Entry: A0A014LVW9_9GAMM
LinkDB: A0A014LVW9_9GAMM
Original site: A0A014LVW9_9GAMM 
ID   A0A014LVW9_9GAMM        Unreviewed;       381 AA.
AC   A0A014LVW9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=BG55_20985 {ECO:0000313|EMBL:EXU73696.1};
OS   Erwinia mallotivora.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU73696.1, ECO:0000313|Proteomes:UP000019918};
RN   [1] {ECO:0000313|EMBL:EXU73696.1, ECO:0000313|Proteomes:UP000019918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU73696.1,
RC   ECO:0000313|Proteomes:UP000019918};
RA   Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA   Mat Amin N.;
RT   "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT   pathogen.";
RL   Submitted (FEB-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   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01229}.
CC   -!- MISCELLANEOUS: FMNH(2) which is absolutely required for this enzymatic
CC       reaction, is provided by SsuE. {ECO:0000256|HAMAP-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:EXU73696.1}.
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DR   EMBL; JFHN01000074; EXU73696.1; -; Genomic_DNA.
DR   RefSeq; WP_034941107.1; NZ_JFHN01000074.1.
DR   AlphaFoldDB; A0A014LVW9; -.
DR   STRING; 69222.BG55_20985; -.
DR   PATRIC; fig|69222.5.peg.4287; -.
DR   OrthoDB; 9814695at2; -.
DR   Proteomes; UP000019918; 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:UP000019918}.
FT   DOMAIN          5..325
FT                   /note="Luciferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00296"
SQ   SEQUENCE   381 AA;  41668 MW;  CB358E93F3247D19 CRC64;
     MSLSVFWFLP THGDGHYLGT AEGARPVDYG YLQQVAQAVD RMGFGGVLIP TGRSCEDAWL
     VAASLIPVTQ RLRFLVALRP GVISPTQAAR QAATLDRLSN GRTLFNLVTG GDAEELAGDG
     VFLDHRERYV ESAEFTRVWR RVLEGETVDY EGKYVHVRGA RLMFKPVQKP RPPLWFGGSS
     EPAQDLAAEQ VDVYLTWGEP PALVKEKIEQ VRAKAAAQGR QVKFGIRLHV IVRETTEEAW
     RAADRLISHL DDATIAKAQS ALARTDSVGQ HRMAALHGGR RDKLEVSPNL WAGVGLVRGG
     AGTALVGDGE TVAARMQEYA DLGIETFILS GYPHLEEAYR VGELLFPHLD LKVPEIPQPG
     KISAHGEAVA HDFAPQKVSQ S
//
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