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SSUD_CUPTR
ID   SSUD_CUPTR              Reviewed;         390 AA.
AC   B3R2K7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=RALTA_A1783;
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
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; CU633749; CAQ69725.1; -; Genomic_DNA.
DR   RefSeq; WP_012353045.1; NC_010528.1.
DR   AlphaFoldDB; B3R2K7; -.
DR   SMR; B3R2K7; -.
DR   STRING; 977880.RALTA_A1783; -.
DR   EnsemblBacteria; CAQ69725; CAQ69725; RALTA_A1783.
DR   GeneID; 29761036; -.
DR   KEGG; cti:RALTA_A1783; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_1_0_4; -.
DR   OMA; NIFWFLP; -.
DR   OrthoDB; 919913at2; -.
DR   BioCyc; CTAI977880:RALTA_RS08595-MON; -.
DR   Proteomes; UP000001692; 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.
FT   CHAIN           1..390
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_1000139614"
SQ   SEQUENCE   390 AA;  42041 MW;  B96DAB0B608A1D29 CRC64;
     MQVFWFIPTH GDSRYLGTSE GARAVGFDYL RQVAVAADTL GYEGVLIPTG RSCEDPWVVA
     SALAAVTQRL KFLVAVRPGL MAPTLAARMA ATFDRISNGR LLINLVTGGD RAELEGDGLF
     LDHAARYEAS AEFLRIWRQV LAASHDGDKV DYDGKHLSVK GATVLYPPLQ RPHPPVYFGG
     SSAPAHALAG EQVDTYLTWG EPPAAVAQKL DDVRRHAARH GRTVKFGIRL HVIVRETDAA
     AWAAAEDLIS RLDDDTVARA QAVFANMDSE GQRRMAALHA GGTRRTREAL EISPNLWAGV
     GLVRGGAGTA LVGDPATVAE RLREYAALGI DTFVLSGYPH LEEAYRFAEL VFPLLPRAVR
     AKFDNLPGKV LSGPFGEVMA TGIVPRAAQS
 
 
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