XYL3A_PRER2
ID XYL3A_PRER2 Reviewed; 861 AA.
AC D5EY15; C0LJN1;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Xylan 1,4-beta-xylosidase {ECO:0000250|UniProtKB:P45702};
DE EC=3.2.1.37 {ECO:0000269|PubMed:19304844};
DE AltName: Full=1,4-beta-D-xylan xylohydrolase {ECO:0000250|UniProtKB:P45702};
DE AltName: Full=Alpha-L-arabinofuranosidase {ECO:0000250|UniProtKB:P96463};
DE Short=Arabinosidase {ECO:0000250|UniProtKB:P96463};
DE EC=3.2.1.55 {ECO:0000269|PubMed:19304844};
DE AltName: Full=Beta-D-xylosidase;
DE AltName: Full=Exo-1,4-beta-xylosidase;
DE Flags: Precursor;
GN Name=xyl3A {ECO:0000312|EMBL:ACN78955.1}; OrderedLocusNames=PRU_2730;
GN ORFNames=02829;
OS Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=264731;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ACN78955.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, GENE NAME, SUBUNIT,
RP AND MUTAGENESIS OF ARG-149; TYR-237; ASP-269; GLU-594 AND GLU-616.
RC STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000269|PubMed:19304844};
RX PubMed=19304844; DOI=10.1128/jb.01628-08;
RA Dodd D., Kocherginskaya S.A., Spies M.A., Beery K.E., Abbas C.A.,
RA Mackie R.I., Cann I.K.;
RT "Biochemical analysis of a beta-D-xylosidase and a bifunctional xylanase-
RT ferulic acid esterase from a xylanolytic gene cluster in Prevotella
RT ruminicola 23.";
RL J. Bacteriol. 191:3328-3338(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ADE82109.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000269|PubMed:20585943};
RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA Coutinho P.M., Henrissat B., Nelson K.E.;
RT "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT bryantii: insights into their environmental niche.";
RL Microb. Ecol. 60:721-729(2010).
CC -!- FUNCTION: Involved in degradation of plant cell wall polysaccharides.
CC Has beta-xylosidase activity via its capacity to hydrolyze glycosidic
CC linkages of beta-1,4-xylo-oligosaccharides of various lengths (X2 to
CC X6), releasing xylose monomers. To a much lesser extent, also has
CC alpha-L-arabinofuranosidase activity. Does not possess beta-D-
CC glucosidase activity. Acts synergistically with Xyn10D-Fae1A to
CC increase the release of xylose from xylan.
CC {ECO:0000269|PubMed:19304844}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC Evidence={ECO:0000269|PubMed:19304844};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC Evidence={ECO:0000269|PubMed:19304844};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 mM for pNP-beta-D-xylopyranoside (pNPX) (at 37 degrees Celsius
CC and pH 5.0) {ECO:0000269|PubMed:19304844};
CC Note=kcat is 9.7 sec(-1) for the beta-xylosidase activity with pNPX
CC as substrate (at 37 degrees Celsius and pH 5.0).;
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:19304844};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000269|PubMed:19304844}.
CC -!- SUBUNIT: Exists as a large polymeric species, presumably as a
CC homononamer. {ECO:0000269|PubMed:19304844}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ713438; ACN78955.1; -; Genomic_DNA.
DR EMBL; CP002006; ADE82109.1; -; Genomic_DNA.
DR RefSeq; WP_013064096.1; NC_014033.1.
DR AlphaFoldDB; D5EY15; -.
DR SMR; D5EY15; -.
DR STRING; 264731.PRU_2730; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblBacteria; ADE82109; ADE82109; PRU_2730.
DR GeneID; 31502261; -.
DR KEGG; pru:PRU_2730; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_3_10; -.
DR OMA; NMTEFRY; -.
DR OrthoDB; 419160at2; -.
DR BRENDA; 3.2.1.37; 768.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000000927; Chromosome.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 2.
DR InterPro; IPR044993; BXL.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42721; PTHR42721; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
DR PROSITE; PS51820; PA14; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Signal; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..861
FT /note="Xylan 1,4-beta-xylosidase"
FT /id="PRO_0000422406"
FT DOMAIN 458..600
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT ACT_SITE 269
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 616
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT MUTAGEN 149
FT /note="R->L: Abolishes xylosidase activity."
FT /evidence="ECO:0000269|PubMed:19304844"
FT MUTAGEN 237
FT /note="Y->F: 6-fold decrease in xylosidase activity."
FT /evidence="ECO:0000269|PubMed:19304844"
FT MUTAGEN 269
FT /note="D->A,N: Abolishes xylosidase activity."
FT /evidence="ECO:0000269|PubMed:19304844"
FT MUTAGEN 594
FT /note="E->Q: No effect on xylosidase activity."
FT /evidence="ECO:0000269|PubMed:19304844"
FT MUTAGEN 616
FT /note="E->A: Moderately reduces xylosidase activity."
FT /evidence="ECO:0000269|PubMed:19304844"
SQ SEQUENCE 861 AA; 96224 MW; 830308889FE67800 CRC64;
MKYQLFLSLA LCVGLGASAQ TLPYQNPNLS AKERAVDLCS RLTLEEKAML MLDESPAIPR
LGIKKFFWWS EALHGAANMG NVTNFPEPVG MAASFNPHLL FKVFDIASTE FRAQYNHRMY
DLNGEDMKMR SLSVWTPNVN IFRDPRWGRG QETYGEDPYL TSVMGVQVVK GLQGPEDARY
RKLWACAKHY AVHSGPEYTR HTANLTDVSA RDFWETYMPA FKTLVKDAKV REVMCAYQRL
DDDPCCGSTR LLQQILRDEW GFEYLVVSDC GAVSDFYENH KSSSDAVHGT SKAVLAGTDV
ECGFNYAYKS LPEAVRKGLL SEKEVDKHVI RLLEGRFDLG EMDDPSLVEW SKIPYSAMST
KASANVALDM ARQTIVLLQN KNNILPLKKN AEKIAIIGPN AHNEPMMWGN YNGTPNHTVT
ILDGVKAKQK KLVYIPGCDL TNDKVMECHL ATDCVTPDGK KGLKGTFWNN TEMAGKPFTT
EYYTKPVNVT TAGMHVFAPN LPIEDFSAKY ETTFTAKEAG EYVVNVESTG HFELYVNGKQ
QFVNHIWRAT PTRTVLKAEK GQKFDIEVRF QTVKTWGASM KIDVARELNI DYQETIAQLK
GINKVIFCGG IAPSLEGEEM PVNIEGFKGG DRTSIELPKV QREFLKALKA AGKQVIYVNC
SGSAIALQPE TESCDAIVQA WYPGQEGGTA VADVLFGDYN PGGKLSVTFY KNDQQLPDYE
DYSMKGRTYR YFDDALFPFG YGLSYTTFEV GEAKVEAATD GALYNVQIPV TNTGTKNGSE
TIQLYIRNLQ DPDGPLKSLR GFERLDIKAG KTATANLKLT KESLEFWDAE TNTMRTKPGK
YEILYGTSSL DKDLKKLTIT L
