ID   XYLS_SACS2              Reviewed;         731 AA.
AC   Q9P999;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Alpha-xylosidase;
DE            EC=3.2.1.177;
GN   Name=xylS; OrderedLocusNames=SSO3022;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, SUBUNIT, SUBSTRATE
RP   SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2, and DSM 5833 / MT-4;
RX   PubMed=10801892; DOI=10.1074/jbc.m910392199;
RA   Moracci M., Ponzano B.C., Trincone A., Fusco S., De Rosa M.,
RA   van der Oost J., Sensen C.W., Charlebois R.L., Rossi M.;
RT   "Identification and molecular characterization of the first alpha-
RT   xylosidase from an Archaeon.";
RL   J. Biol. Chem. 275:22082-22089(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC   -!- FUNCTION: Catalyzes the liberation of alpha-xylose from the non-
CC       reducing terminal glucose of xyloglucan oligosaccharides. Has high
CC       hydrolytic activity on the disaccharide isoprimeverose. Follows a
CC       retaining mechanism of substrate hydrolysis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-xylose residues
CC         with release of alpha-D-xylose.; EC=3.2.1.177;
CC         Evidence={ECO:0000269|PubMed:10801892};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=17 mM for maltose {ECO:0000269|PubMed:10801892};
CC         KM=3.45 mM for maltotriose {ECO:0000269|PubMed:10801892};
CC         KM=28.9 mM for isoprimeverose {ECO:0000269|PubMed:10801892};
CC         KM=1.72 mM for 4-nitrophenyl-beta-isoprimeveroside
CC         {ECO:0000269|PubMed:10801892};
CC       pH dependence:
CC         Optimum pH is 5.5. {ECO:0000269|PubMed:10801892};
CC       Temperature dependence:
CC         Optimum temperature is 90 degrees Celsius.
CC         {ECO:0000269|PubMed:10801892};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10801892}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR   EMBL; AJ251975; CAB99206.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK43123.1; -; Genomic_DNA.
DR   PIR; D90483; D90483.
DR   RefSeq; WP_009992679.1; NC_002754.1.
DR   AlphaFoldDB; Q9P999; -.
DR   SMR; Q9P999; -.
DR   STRING; 273057.SSO3022; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   PRIDE; Q9P999; -.
DR   DNASU; 1453042; -.
DR   EnsemblBacteria; AAK43123; AAK43123; SSO3022.
DR   GeneID; 44128744; -.
DR   KEGG; sso:SSO3022; -.
DR   PATRIC; fig|273057.12.peg.3115; -.
DR   eggNOG; arCOG03663; Archaea.
DR   HOGENOM; CLU_000631_7_3_2; -.
DR   InParanoid; Q9P999; -.
DR   OMA; IEPWGPN; -.
DR   PhylomeDB; Q9P999; -.
DR   BioCyc; MetaCyc:MON-16613; -.
DR   BRENDA; 3.2.1.177; 6163.
DR   SABIO-RK; Q9P999; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0061634; F:alpha-D-xyloside xylohydrolase; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 2.
DR   InterPro; IPR033403; DUF5110.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR000322; Glyco_hydro_31.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF17137; DUF5110; 1.
DR   Pfam; PF01055; Glyco_hydro_31; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
PE   1: Evidence at protein level;
KW   Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..731
FT                   /note="Alpha-xylosidase"
FT                   /id="PRO_0000185369"
FT   ACT_SITE        353
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        356
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        428
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   731 AA;  84485 MW;  85328243A00C4F3E CRC64;
     MRIGNLNVEI EFIADNIVRV LYYYGREAIV DNSLVVLPNL EKLSIKGEST GPSIISFSSE
     SLSVDINTSN GELIMKDNKG GIVVKEKRRD LKFNEELSTY NVEQEFELSE GERVYGLGQH
     AGGNGLGQSS AYKLDYSGLS TTLSQRNTDI GIPFIVSSKG YGILWDNYSL GSISLRRNKL
     KVWFEAGKKI DYYVIYGDSI DDVIKGYRKL TGDAPLLPKW AYGYWQSKER YKSQDEITSV
     VKEFRERKIP LDVIVLDWRY WGKYGWNAFK FDETDFPRPK DMVEEIHKMG AKLAISIWPT
     FGKETEVFKD MESKGCIILG TTAFNPFKDE CRELFWSYVK GFYDLGIDAY WLDASEPETG
     LGLVFFSPIH DVDLEIGKGY EYLNAYPLME TKAVYEGQRR ISNKRVVILT RSAFAGQQRH
     SAISWSGDVL GDWATLRAQI PAGLNFSISG IPYWTTDTGG FFSGNPETKA YAEIFVRWFQ
     WSTFCPILRV HGTIFPKEPW RFPREYQEVI LKYIRLRYKL LPYIYSLAWM TYSIGYTIMR
     PLVMDFRDDQ NVYDFDEQYM FGPYILISPV TLPSIIEKEV YLPSKEYWYD FWTGEKLEGG
     RMMDVKVTLD TIPLFVRSGA VLPLLGKNVN NAEEYWDVID LRVYPGKNGY FELYDDDGIT
     YEYEKGKYYI IPITWDEDKQ ELTIGKKRGE LEMSKKIIKI IWVEKGKGIE HTKPDVEIEY
     NGKETITVKR G