HEXSF_BACTN
ID HEXSF_BACTN Reviewed; 481 AA.
AC Q8A7C8;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Delta 4,5-hexuronate-2-O-sulfatase {ECO:0000303|PubMed:25002587};
DE EC=3.1.6.- {ECO:0000269|PubMed:25002587};
GN OrderedLocusNames=BT_1596 {ECO:0000312|EMBL:AAO76703.1};
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).
RN [4] {ECO:0007744|PDB:3B5Q}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ZINC.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of a putative sulfatase (NP_810509.1) from Bacteroides
RT thetaiotaomicron VPI-5482 at 2.40 A resolution.";
RL Submitted (OCT-2007) to the PDB data bank.
RN [5] {ECO:0007744|PDB:5G2T, ECO:0007744|PDB:5G2U}
RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 13-481.
RA Cartmell A., Lowe E.C., Basle A., Crouch L.I., Czjzek M., Turnbull J.,
RA Henrissat B., Terrapon N., Thomas S., Murray H., Firbank S.J., Bolam D.N.;
RT "Metabolism of host GAGs by the human gut bacterium Bacteroides
RT thetaiotaomicron.";
RL Submitted (APR-2016) to the PDB data bank.
CC -!- FUNCTION: Exosulfatase involved in the degradation of the
CC glycosaminoglycans (GAGs) chondroitin sulfate (CS), dermatan sulfate
CC (DS) and heparan sulfate (HS). 2-O-sulfatase active on unsaturated non-
CC reducing end hexuronate units. Has a slight preference for HS-derived
CC structures (PubMed:25002587). GAG-specific sulfatases play a key role
CC in the persistence of the major human gut symbiont B.thetaiotaomicron
CC in the host gastrointestinal tract (PubMed:25002587).
CC {ECO:0000269|PubMed:25002587, ECO:0000305|PubMed:25002587}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|Ref.4};
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; AAO76703.1; -; Genomic_DNA.
DR RefSeq; NP_810509.1; NC_004663.1.
DR PDB; 3B5Q; X-ray; 2.40 A; A/B=1-481.
DR PDB; 5G2T; X-ray; 1.90 A; A/B/C/D=13-481.
DR PDB; 5G2U; X-ray; 1.43 A; A=13-481.
DR PDBsum; 3B5Q; -.
DR PDBsum; 5G2T; -.
DR PDBsum; 5G2U; -.
DR AlphaFoldDB; Q8A7C8; -.
DR SMR; Q8A7C8; -.
DR STRING; 226186.BT_1596; -.
DR PaxDb; Q8A7C8; -.
DR PRIDE; Q8A7C8; -.
DR DNASU; 1075809; -.
DR EnsemblBacteria; AAO76703; AAO76703; BT_1596.
DR KEGG; bth:BT_1596; -.
DR PATRIC; fig|226186.12.peg.1634; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_9_1_10; -.
DR InParanoid; Q8A7C8; -.
DR OMA; DICEWAR; -.
DR EvolutionaryTrace; Q8A7C8; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0004065; F:arylsulfatase activity; IBA:GO_Central.
DR GO; GO:0015024; F:glucuronate-2-sulfatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR032506; DUF4976.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF16347; DUF4976; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..481
FT /note="Delta 4,5-hexuronate-2-O-sulfatase"
FT /id="PRO_0000446229"
FT REGION 453..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3B5Q"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3B5Q"
FT BINDING 462
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3B5Q"
FT BINDING 469
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:3B5Q"
FT MOD_RES 64
FT /note="3-oxoalanine (Ser)"
FT /evidence="ECO:0000250|UniProtKB:Q9X759"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:5G2U"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:5G2U"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:5G2U"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:5G2U"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:5G2U"
FT TURN 121..126
FT /evidence="ECO:0007829|PDB:5G2U"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:5G2U"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 146..163
FT /evidence="ECO:0007829|PDB:5G2U"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:5G2U"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 239..267
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:5G2U"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:5G2U"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 356..360
FT /evidence="ECO:0007829|PDB:5G2U"
FT STRAND 371..390
FT /evidence="ECO:0007829|PDB:5G2U"
FT STRAND 392..399
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:5G2U"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:5G2U"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 427..443
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:5G2U"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:5G2U"
FT HELIX 474..477
FT /evidence="ECO:0007829|PDB:5G2U"
SQ SEQUENCE 481 AA; 53650 MW; 1B9A5C1E9B0A9655 CRC64;
MGLALCGAAA QAQEKPNFLI IQCDHLTQRV VGAYGQTQGC TLPIDEVASR GVIFSNAYVG
CPLSQPSRAA LWSGMMPHQT NVRSNSSEPV NTRLPENVPT LGSLFSESGY EAVHFGKTHD
MGSLRGFKHK EPVAKPFTDP EFPVNNDSFL DVGTCEDAVA YLSNPPKEPF ICIADFQNPH
NICGFIGENA GVHTDRPISG PLPELPDNFD VEDWSNIPTP VQYICCSHRR MTQAAHWNEE
NYRHYIAAFQ HYTKMVSKQV DSVLKALYST PAGRNTIVVI MADHGDGMAS HRMVTKHISF
YDEMTNVPFI FAGPGIKQQK KPVDHLLTQP TLDLLPTLCD LAGIAVPAEK AGISLAPTLR
GEKQKKSHPY VVSEWHSEYE YVTTPGRMVR GPRYKYTHYL EGNGEELYDM KKDPGERKNL
AKDPKYSKIL AEHRALLDDY ITRSKDDYRS LKVDADPRCR NHTPGYPSHE GPGAREILKR
K
