GALSF_BACTN
ID GALSF_BACTN Reviewed; 511 AA.
AC Q8A2H2;
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=N-acetylgalactosamine-6-O-sulfatase {ECO:0000303|PubMed:25002587};
DE EC=3.1.6.- {ECO:0000269|PubMed:25002587};
GN OrderedLocusNames=BT_3333 {ECO:0000312|EMBL:AAO78439.1};
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: Exosulfatase involved in the degradation of the
CC glycosaminoglycans (GAGs) chondroitin sulfate (CS) and dermatan sulfate
CC (DS). Catalyzes the hydrolysis of the 6-sulfate groups of the N-acetyl-
CC D-galactosamine 6-sulfate units (PubMed:25002587). GAG-specific
CC sulfatases play a key role in the persistence of the major human gut
CC symbiont 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; AAO78439.1; -; Genomic_DNA.
DR RefSeq; NP_812245.1; NC_004663.1.
DR RefSeq; WP_011108775.1; NC_004663.1.
DR PDB; 6S20; X-ray; 1.98 A; C=22-511.
DR PDBsum; 6S20; -.
DR AlphaFoldDB; Q8A2H2; -.
DR SMR; Q8A2H2; -.
DR STRING; 226186.BT_3333; -.
DR PaxDb; Q8A2H2; -.
DR PRIDE; Q8A2H2; -.
DR EnsemblBacteria; AAO78439; AAO78439; BT_3333.
DR GeneID; 60924512; -.
DR KEGG; bth:BT_3333; -.
DR PATRIC; fig|226186.12.peg.3400; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_10_3_10; -.
DR InParanoid; Q8A2H2; -.
DR OMA; IPRIGWM; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR032158; DUF4994.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF16385; DUF4994; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
DR PROSITE; PS00149; SULFATASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..511
FT /note="N-acetylgalactosamine-6-O-sulfatase"
FT /id="PRO_0000446230"
FT MOD_RES 83
FT /note="3-oxoalanine (Ser)"
FT /evidence="ECO:0000250|UniProtKB:Q9X759"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:6S20"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:6S20"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:6S20"
FT TURN 287..291
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 296..318
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 325..333
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:6S20"
FT TURN 345..348
FT /evidence="ECO:0007829|PDB:6S20"
FT TURN 354..357
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:6S20"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 396..403
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 450..453
FT /evidence="ECO:0007829|PDB:6S20"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:6S20"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:6S20"
FT TURN 480..482
FT /evidence="ECO:0007829|PDB:6S20"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:6S20"
FT HELIX 495..510
FT /evidence="ECO:0007829|PDB:6S20"
SQ SEQUENCE 511 AA; 56324 MW; 3919271135DD47B1 CRC64;
MKNVSRLLPL LPGIALLTGC NQKVQKDNGQ NSQKPNIIYI FADDLGIGDL SCYGATKVST
PHIDRLAGQG VQFTNAYATS ATSTPSRFGL LTGMYPWRQE NTGIAPGNSE LIIDTACVTM
ADMLKEAGYA TGVVGKWHLG LGPKGGTDFN GHITPNAQSI GFDYEFVIPA TVDRVPCVFV
ENGHVVGLDP NDPITVNYEH KVGDWPTGEE NPELVKLKPS QGHNNTIING IPRIGWMTGG
KSALWKDEDI ADIITNKAKS FIVSHKEEPF FLYMGTQDVH VPRVPHPRFA GKSGLGTRGD
VILQLDWTIG EIMNTLDSLQ LTDNTILIFT SDNGPVIDDG YQDQAFERLN GHTPMGIYRG
GKYSAYEAGT RIPFIVRWPA KVKPNKQQAL FSQIDIFASL AALLKQPLPE DAAPDSQEHL
NTLLGKDYTS REYIVQQNLN NTLAIVKGQW KYIEPSDAPA IEYWTKMELG NDRHPQLYDL
SADPSEKNNV AKQHPEVVRE LSELLESVKT R