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ENDSF_BACTN
ID   ENDSF_BACTN             Reviewed;         508 AA.
AC   Q8A2F6;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Endo-4-O-sulfatase {ECO:0000303|PubMed:25002587};
DE            EC=3.1.6.- {ECO:0000269|PubMed:25002587};
GN   OrderedLocusNames=BT_3349 {ECO:0000312|EMBL:AAO78455.1};
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of its two
RT   dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=25002587; DOI=10.1074/jbc.m114.573303;
RA   Ulmer J.E., Vilen E.M., Namburi R.B., Benjdia A., Beneteau J., Malleron A.,
RA   Bonnaffe D., Driguez P.A., Descroix K., Lassalle G., Le Narvor C.,
RA   Sandstroem C., Spillmann D., Berteau O.;
RT   "Characterization of glycosaminoglycan (GAG) sulfatases from the human gut
RT   symbiont Bacteroides thetaiotaomicron reveals the first GAG-specific
RT   bacterial endosulfatase.";
RL   J. Biol. Chem. 289:24289-24303(2014).
CC   -!- FUNCTION: Endosulfatase involved in the degradation of the
CC       glycosaminoglycans (GAGs) chondroitin sulfate (CS) and dermatan sulfate
CC       (DS). Efficiently hydrolyzes sulfate groups from a broad range of
CC       substrate size, including disaccharide to high molecular weight CS and
CC       DS polymers. Has a strict specificity for the 4-O-sulfate groups of
CC       galactosamine (PubMed:25002587). GAG-specific sulfatases play a key
CC       role in the persistence of the major human gut symbiont
CC       B.thetaiotaomicron in the host gastrointestinal tract
CC       (PubMed:25002587). {ECO:0000269|PubMed:25002587,
CC       ECO:0000305|PubMed:25002587}.
CC   -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC       FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC       residue in eukaryotes, is critical for catalytic activity.
CC       {ECO:0000250|UniProtKB:Q9X759}.
CC   -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR   EMBL; AE015928; AAO78455.1; -; Genomic_DNA.
DR   RefSeq; NP_812261.1; NC_004663.1.
DR   PDB; 6S21; X-ray; 2.80 A; A/B/C=17-508.
DR   PDBsum; 6S21; -.
DR   AlphaFoldDB; Q8A2F6; -.
DR   SMR; Q8A2F6; -.
DR   STRING; 226186.BT_3349; -.
DR   PaxDb; Q8A2F6; -.
DR   PRIDE; Q8A2F6; -.
DR   EnsemblBacteria; AAO78455; AAO78455; BT_3349.
DR   KEGG; bth:BT_3349; -.
DR   PATRIC; fig|226186.12.peg.3417; -.
DR   eggNOG; COG3119; Bacteria.
DR   HOGENOM; CLU_006332_9_3_10; -.
DR   InParanoid; Q8A2F6; -.
DR   OMA; DHGETMC; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0004065; F:arylsulfatase activity; IBA:GO_Central.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR000917; Sulfatase_N.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Reference proteome.
FT   CHAIN           1..508
FT                   /note="Endo-4-O-sulfatase"
FT                   /id="PRO_0000446228"
FT   MOD_RES         84
FT                   /note="3-oxoalanine (Ser)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X759"
FT   STRAND          26..30
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           41..44
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           62..68
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   STRAND          71..75
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           84..93
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           97..100
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           122..128
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   STRAND          132..138
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   STRAND          176..182
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   STRAND          187..189
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   STRAND          192..194
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           206..219
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   TURN            220..222
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   STRAND          231..236
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           252..255
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   TURN            256..260
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           263..265
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           277..281
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           282..305
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           308..310
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   STRAND          311..317
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   STRAND          331..335
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           338..341
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   STRAND          345..348
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   TURN            350..352
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   STRAND          356..358
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           364..366
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           367..374
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           378..380
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           391..395
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   STRAND          405..414
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   STRAND          425..444
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   STRAND          446..448
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   STRAND          451..458
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   TURN            459..461
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           472..474
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           475..492
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   HELIX           495..498
FT                   /evidence="ECO:0007829|PDB:6S21"
FT   TURN            499..505
FT                   /evidence="ECO:0007829|PDB:6S21"
SQ   SEQUENCE   508 AA;  57857 MW;  5609AC6B0E822904 CRC64;
     MGGLTLFAAQ GCKAPKQVAE QAEHPNIIYV FPDQYRNQAM GFWNQEGFRD KVNFRGDPVH
     TPNIDTFARE SMVLTSAQSN CPLSSPHRGM LLTGMYPNRS GVPLNCNSTR PISSLRDDAE
     CIGDVFSKAG YDCAYFGKLH ADFPTPNDPE NPGQYVETQR PVWDAYTPKE QRHGFNYWYS
     YGTFDEHKNP HYWDTDGKRH DPKEWSPLHE SGKVVSYLKN EGNVRDTKKP FFIMVGMNPP
     HSPYRSLNDC EEQDFNLYKD QPLDSLLIRP NVDLNMKKAE SVRYYFASVT GVDRAFGQIL
     EALKQLGLDK NTVVIFASDH GETMCSQRTD DPKNSPYSES MNIPFLVRFP GKIQPRVDDL
     LLSAPDIMPT VLGLCGLGDS IPSEVQGRNF APLFFDEKAE IVRPAGALYI QNLDGEKDKD
     GLVQSYFPSS RGIKTARYTL ALYIDRKTKQ LKKSLLFDDV NDPYQLNNLP LDENKEVVEQ
     LYREMGTMLK EIDDPWYTEK ILSDRIPY
 
 
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