SSUD_ECOLI
ID SSUD_ECOLI Reviewed; 381 AA.
AC P80645; P75852; Q9RM46;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Alkanesulfonate monooxygenase {ECO:0000303|PubMed:10480865};
DE EC=1.14.14.5 {ECO:0000269|PubMed:10480865};
DE AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase;
DE AltName: Full=Sulfate starvation-induced protein 6;
DE Short=SSI6;
GN Name=ssuD; Synonyms=ycbN; OrderedLocusNames=b0935, JW0918;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10506196; DOI=10.1074/jbc.274.41.29358;
RA Van der Ploeg J.R., Iwanicka-Nowicka R., Bykowski T., Hryniewicz M.M.,
RA Leisinger T.;
RT "The Escherichia coli ssuEADCB gene cluster is required for the utilization
RT of sulfur from aliphatic sulfonates and is regulated by the transcriptional
RT activator Cbl.";
RL J. Biol. Chem. 274:29358-29365(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-21.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8774726; DOI=10.1111/j.1432-1033.1996.0773u.x;
RA Quadroni M., Staudenmann W., Kertesz M.A., James P.;
RT "Analysis of global responses by protein and peptide fingerprinting of
RT proteins isolated by two-dimensional gel electrophoresis. Application to
RT the sulfate-starvation response of Escherichia coli.";
RL Eur. J. Biochem. 239:773-781(1996).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, INDUCTION, AND MUTAGENESIS OF ARG-298.
RX PubMed=10480865; DOI=10.1074/jbc.274.38.26639;
RA Eichhorn E., van der Ploeg J.R., Leisinger T.;
RT "Characterization of a two-component alkanesulfonate monooxygenase from
RT Escherichia coli.";
RL J. Biol. Chem. 274:26639-26646(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=12445781; DOI=10.1016/s0022-2836(02)01069-0;
RA Eichhorn E., Davey C.A., Sargent D.F., Leisinger T., Richmond T.J.;
RT "Crystal structure of Escherichia coli alkanesulfonate monooxygenase
RT SsuD.";
RL J. Mol. Biol. 324:457-468(2002).
CC -!- FUNCTION: Involved in desulfonation of aliphatic sulfonates. Catalyzes
CC the conversion of pentanesulfonate to sulfite and pentaldehyde and is
CC able to desulfonate a wide range of sulfonated substrates including C-2
CC to C-10 unsubstituted linear alkanesulfonates, substituted
CC ethanesulfonic acids and sulfonated buffers.
CC {ECO:0000269|PubMed:10480865}.
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;
CC Evidence={ECO:0000269|PubMed:10480865};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23065;
CC Evidence={ECO:0000305|PubMed:10480865};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=35 uM for decanesulfonate {ECO:0000269|PubMed:10480865};
CC KM=44 uM for octanesulfonate {ECO:0000269|PubMed:10480865};
CC KM=114 uM for 1,3-dioxo-2-isoindolineethanesulfonate
CC {ECO:0000269|PubMed:10480865};
CC KM=139 uM for 2-(4-pyridyl)ethanesulfonate
CC {ECO:0000269|PubMed:10480865};
CC KM=95 uM for hexanesulfonate {ECO:0000269|PubMed:10480865};
CC KM=237 uM for N-phenyltaurine {ECO:0000269|PubMed:10480865};
CC KM=110 uM for 4-phenyl-1-butanesulfonate
CC {ECO:0000269|PubMed:10480865};
CC KM=189 uM for pentanesulfonate {ECO:0000269|PubMed:10480865};
CC KM=617 uM for MOPS {ECO:0000269|PubMed:10480865};
CC KM=870 uM for butanesulfonate {ECO:0000269|PubMed:10480865};
CC KM=1110 uM for PIPES {ECO:0000269|PubMed:10480865};
CC Vmax=1.4 umol/min/mg enzyme with decanesulfonate as substrate
CC {ECO:0000269|PubMed:10480865};
CC Vmax=1.6 umol/min/mg enzyme with octanesulfonate as substrate
CC {ECO:0000269|PubMed:10480865};
CC Vmax=4.1 umol/min/mg enzyme with 1,3-dioxo-2-
CC isoindolineethanesulfonate as substrate
CC {ECO:0000269|PubMed:10480865};
CC Vmax=3.8 umol/min/mg enzyme with 2-(4-pyridyl)ethanesulfonate as
CC substrate {ECO:0000269|PubMed:10480865};
CC Vmax=2.3 umol/min/mg enzyme with hexanesulfonate as substrate
CC {ECO:0000269|PubMed:10480865};
CC Vmax=4.6 umol/min/mg enzyme with N-phenyltaurine as substrate
CC {ECO:0000269|PubMed:10480865};
CC Vmax=1.8 umol/min/mg enzyme with 4-phenyl-1-butanesulfonate as
CC substrate {ECO:0000269|PubMed:10480865};
CC Vmax=2.0 umol/min/mg enzyme with pentanesulfonate as substrate
CC {ECO:0000269|PubMed:10480865};
CC Vmax=4.1 umol/min/mg enzyme with MOPS as substrate
CC {ECO:0000269|PubMed:10480865};
CC Vmax=3.3 umol/min/mg enzyme with butanesulfonate as substrate
CC {ECO:0000269|PubMed:10480865};
CC Vmax=2.4 umol/min/mg enzyme with PIPES as substrate
CC {ECO:0000269|PubMed:10480865};
CC pH dependence:
CC Optimum pH is 9.1. {ECO:0000269|PubMed:10480865};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10480865}.
CC -!- INTERACTION:
CC P80645; P80644: ssuE; NbExp=2; IntAct=EBI-561637, EBI-1121047;
CC -!- INDUCTION: Repressed by sulfate or cysteine.
CC {ECO:0000269|PubMed:10480865}.
CC -!- MISCELLANEOUS: FMNH(2) which is absolutely required for this enzymatic
CC reaction, is provided by SsuE. {ECO:0000269|PubMed:10480865}.
CC -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000305}.
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DR EMBL; AJ237695; CAB40391.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74021.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35690.1; -; Genomic_DNA.
DR PIR; F64833; F64833.
DR RefSeq; NP_415455.1; NC_000913.3.
DR RefSeq; WP_000056006.1; NZ_SSZK01000002.1.
DR PDB; 1M41; X-ray; 2.30 A; A/B=2-381.
DR PDB; 1NQK; X-ray; 2.20 A; A=1-381.
DR PDBsum; 1M41; -.
DR PDBsum; 1NQK; -.
DR AlphaFoldDB; P80645; -.
DR SMR; P80645; -.
DR BioGRID; 4260022; 16.
DR BioGRID; 849931; 1.
DR ComplexPortal; CPX-2117; Alkanesulfonate monooxygenase complex.
DR DIP; DIP-10928N; -.
DR IntAct; P80645; 10.
DR STRING; 511145.b0935; -.
DR PaxDb; P80645; -.
DR PRIDE; P80645; -.
DR EnsemblBacteria; AAC74021; AAC74021; b0935.
DR EnsemblBacteria; BAA35690; BAA35690; BAA35690.
DR GeneID; 945557; -.
DR KEGG; ecj:JW0918; -.
DR KEGG; eco:b0935; -.
DR PATRIC; fig|1411691.4.peg.1339; -.
DR EchoBASE; EB3470; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_1_0_6; -.
DR InParanoid; P80645; -.
DR OMA; NIFWFLP; -.
DR PhylomeDB; P80645; -.
DR BioCyc; EcoCyc:MON-162; -.
DR BioCyc; MetaCyc:MON-162; -.
DR BRENDA; 1.14.14.5; 2026.
DR EvolutionaryTrace; P80645; -.
DR PRO; PR:P80645; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990201; C:alkanesulfonate monooxygenase complex; IDA:EcoCyc.
DR GO; GO:0008726; F:alkanesulfonate monooxygenase activity; IDA:EcoCyc.
DR GO; GO:0046306; P:alkanesulfonate catabolic process; IDA:ComplexPortal.
DR GO; GO:0010438; P:cellular response to sulfur starvation; IC:ComplexPortal.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Flavoprotein; FMN; Monooxygenase;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8774726"
FT CHAIN 2..381
FT /note="Alkanesulfonate monooxygenase"
FT /id="PRO_0000216706"
FT VARIANT 298
FT /note="R -> C (in strain: K12 / MC4100; inactive)"
FT MUTAGEN 298
FT /note="R->C: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10480865"
FT CONFLICT 19
FT /note="G -> Q (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1NQK"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:1NQK"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:1NQK"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1NQK"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:1NQK"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1NQK"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1NQK"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:1NQK"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1NQK"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:1NQK"
FT HELIX 127..142
FT /evidence="ECO:0007829|PDB:1NQK"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1NQK"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1NQK"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:1NQK"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:1NQK"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:1NQK"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:1NQK"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1NQK"
FT HELIX 201..216
FT /evidence="ECO:0007829|PDB:1NQK"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:1NQK"
FT STRAND 223..235
FT /evidence="ECO:0007829|PDB:1NQK"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:1NQK"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1NQK"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:1NQK"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:1NQK"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:1NQK"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:1NQK"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:1NQK"
FT HELIX 309..320
FT /evidence="ECO:0007829|PDB:1NQK"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:1NQK"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:1NQK"
FT HELIX 334..344
FT /evidence="ECO:0007829|PDB:1NQK"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:1NQK"
SQ SEQUENCE 381 AA; 41736 MW; 4D05E510487999C6 CRC64;
MSLNMFWFLP THGDGHYLGT EEGSRPVDHG YLQQIAQAAD RLGYTGVLIP TGRSCEDAWL
VAASMIPVTQ RLKFLVALRP SVTSPTVAAR QAATLDRLSN GRALFNLVTG SDPQELAGDG
VFLDHSERYE ASAEFTQVWR RLLQRETVDF NGKHIHVRGA KLLFPAIQQP YPPLYFGGSS
DVAQELAAEQ VDLYLTWGEP PELVKEKIEQ VRAKAAAHGR KIRFGIRLHV IVRETNDEAW
QAAERLISHL DDETIAKAQA AFARTDSVGQ QRMAALHNGK RDNLEISPNL WAGVGLVRGG
AGTALVGDGP TVAARINEYA ALGIDSFVLS GYPHLEEAYR VGELLFPLLD VAIPEIPQPQ
PLNPQGEAVA NDFIPRKVAQ S
