BDS1_YEAST
ID BDS1_YEAST Reviewed; 646 AA.
AC Q08347; D6W1Q6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Alkyl/aryl-sulfatase BDS1 {ECO:0000303|PubMed:15947202};
DE EC=3.1.6.-;
DE AltName: Full=Bacterially-derived sulfatase 1 {ECO:0000303|PubMed:15947202};
GN Name=BDS1; OrderedLocusNames=YOL164W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP INDUCTION.
RX PubMed=12414795; DOI=10.1074/jbc.m209759200;
RA Boer V.M., de Winde J.H., Pronk J.T., Piper M.D.W.;
RT "The genome-wide transcriptional responses of Saccharomyces cerevisiae
RT grown on glucose in aerobic chemostat cultures limited for carbon,
RT nitrogen, phosphorus, or sulfur.";
RL J. Biol. Chem. 278:3265-3274(2003).
RN [4]
RP FUNCTION.
RX PubMed=15947202; DOI=10.1128/ec.4.6.1102-1115.2005;
RA Hall C.R., Brachat S., Dietrich F.S.;
RT "Contribution of horizontal gene transfer to the evolution of Saccharomyces
RT cerevisiae.";
RL Eukaryot. Cell 4:1102-1115(2005).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Alkyl/aryl-sulfatase. Enables the use of SDS and 4-
CC nitrocatechol as sulfur source. {ECO:0000269|PubMed:15947202}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9I5I9};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9I5I9};
CC -!- INDUCTION: Expression is increased in sulfur-limited chemostat
CC cultures. {ECO:0000269|PubMed:12414795}.
CC -!- MISCELLANEOUS: The presence of this bacterial-like protein in
CC S.cerevisiae results probably from a recent horizontal gene transfer
CC event. {ECO:0000269|PubMed:15947202}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Type III
CC sulfatase family. {ECO:0000305}.
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DR EMBL; Z74906; CAA99186.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10622.1; -; Genomic_DNA.
DR PIR; S66863; S66863.
DR RefSeq; NP_014478.1; NM_001183417.1.
DR AlphaFoldDB; Q08347; -.
DR SMR; Q08347; -.
DR BioGRID; 34254; 15.
DR STRING; 4932.YOL164W; -.
DR iPTMnet; Q08347; -.
DR PaxDb; Q08347; -.
DR PRIDE; Q08347; -.
DR EnsemblFungi; YOL164W_mRNA; YOL164W; YOL164W.
DR GeneID; 854000; -.
DR KEGG; sce:YOL164W; -.
DR SGD; S000005524; BDS1.
DR VEuPathDB; FungiDB:YOL164W; -.
DR eggNOG; ENOG502RJJX; Eukaryota.
DR HOGENOM; CLU_014655_1_0_1; -.
DR InParanoid; Q08347; -.
DR OMA; NPARLWP; -.
DR BioCyc; YEAST:G3O-33551-MON; -.
DR PRO; PR:Q08347; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08347; protein.
DR GO; GO:0018741; F:alkyl sulfatase activity; IMP:SGD.
DR GO; GO:0004065; F:arylsulfatase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0018909; P:dodecyl sulfate metabolic process; IMP:SGD.
DR CDD; cd07710; arylsulfatase_Sdsa1-like_MBL-fold; 1.
DR Gene3D; 1.25.40.880; -; 1.
DR Gene3D; 3.30.1050.10; -; 1.
DR InterPro; IPR038536; Alkyl/aryl-sulf_dimr_sf.
DR InterPro; IPR029229; Alkyl_sulf_C.
DR InterPro; IPR029228; Alkyl_sulf_dimr.
DR InterPro; IPR044097; Bds1/SdsA1_MBL-fold.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR Pfam; PF14864; Alkyl_sulf_C; 1.
DR Pfam; PF14863; Alkyl_sulf_dimr; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF55718; SSF55718; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..646
FT /note="Alkyl/aryl-sulfatase BDS1"
FT /id="PRO_0000227682"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 646 AA; 72646 MW; 153BA6F9831F4642 CRC64;
MIGAFKRNRG SSQSFAKECQ PSTLKANLEV AKELPFSDRR DFEDATQGYI GSLSDEQIIG
PDGGVVWCMK SYGFLEPETP ANTVNPSLWR QAQLNAIHGL FKITDNVYQV RGLDISNMTI
IEGNTSLIII DTLFTTETAQ ESLKLYYRHR PQKPVRTVIY THSHSDHYGG VKGIVKEADV
KSGEVQIIAP VGFMESVVAE NILAGNAMHR RSQYQFGMLL SPSVKGHVDC GIGKAASHGT
VTLIAPTIII EEPVEERTID GVDFVFQLAP GSEAPSEMLI YMPQQRVLNM AEDVTHHMHN
LYALRGVEVR DGNQWAKYID AARVAFGSKT DVLIAQHHWP TTGQMRINEL LKKQRDMYKF
IHDQTLRLLN QGYTSRDIAE TLRMPSSLEQ EWSTRGYYGT LSHNVKAVYQ KYLGWYDANP
ANLNPLPPVA YAKKAVEYMG GADAVLARAY KDFQKGEFRW VASVVNQLVF ADPNNHQARE
LCADALEQLG YQAEASTWRN AYLVGAMELR QGVPKRRSTG KRNNIAVLNN EMFFDFLAVR
LNATKAEGKI IVSNWCFINS NERFVITLEN CALTYIQGWQ TDADATITLK RTTFEALLAN
EITMVDFLRS KEVEIEGNRL RIEELLKLFD DFDQSFPVVE PMGGST
