ID   XLOA_VIBSX              Reviewed;         535 AA.
AC   A9ZND1;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Xylan 1,3-beta-xylosidase;
DE            EC=3.2.1.72;
GN   Name=xloA;
OS   Vibrio sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=678;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21 AND 357-376,
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RC   STRAIN=XY-214;
RX   PubMed=17993567; DOI=10.1128/aem.01793-07;
RA   Umemoto Y., Onishi R., Araki T.;
RT   "Cloning of a novel gene encoding beta-1,3-xylosidase from a marine
RT   bacterium, Vibrio sp. strain XY-214, and characterization of the gene
RT   product.";
RL   Appl. Environ. Microbiol. 74:305-308(2008).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA   Shearer A.G., Altman T., Rhee C.D.;
RT   "Finding sequences for over 270 orphan enzymes.";
RL   PLoS ONE 9:E97250-E97250(2014).
CC   -!- FUNCTION: Beta-1,3-xylosidase that hydrolyzes beta-1,3-
CC       xylooligosaccharides to D-xylose. {ECO:0000269|PubMed:17993567}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of successive xylose residues from the non-reducing
CC         termini of (1->3)-beta-D-xylans.; EC=3.2.1.72;
CC         Evidence={ECO:0000269|PubMed:17993567};
CC   -!- ACTIVITY REGULATION: Inhibited by Ag(+), Cu(2+), Hg(2+), Mn(2+),
CC       Pb(2+), Zn(2+) and p-chloromercuric benzoic acid.
CC       {ECO:0000269|PubMed:17993567}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.244 mM for p-nitrophenyl-beta-D-xylopyranoside
CC         {ECO:0000269|PubMed:17993567};
CC         Vmax=1.82 umol/min/mg enzyme with p-nitrophenyl-beta-D-xylopyranoside
CC         as substrate {ECO:0000269|PubMed:17993567};
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:17993567};
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius.
CC         {ECO:0000269|PubMed:17993567};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR   EMBL; AB300564; BAF98235.1; -; mRNA.
DR   AlphaFoldDB; A9ZND1; -.
DR   SMR; A9ZND1; -.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   BioCyc; MetaCyc:MON-16529; -.
DR   BRENDA; 3.2.1.72; 6640.
DR   GO; GO:0033914; F:xylan 1,3-beta-xylosidase activity; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR   Gene3D; 2.115.10.20; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR041542; GH43_C2.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   Pfam; PF17851; GH43_C2; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:17993567"
FT   CHAIN           2..535
FT                   /note="Xylan 1,3-beta-xylosidase"
FT                   /id="PRO_0000430455"
FT   ACT_SITE        16
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A7LXU0"
FT   ACT_SITE        189
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:A7LXU0"
FT   SITE            130
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A7LXU0"
SQ   SEQUENCE   535 AA;  60835 MW;  2BA98D822876D42E CRC64;
     MTTTIQNPIL KGFNPDPSIV RVGDDYYIAT STFEWFPGIQ LHHSRDLINW RLVGHALTRT
     SQLNMMGMDN SEGVYAPALT YSDGTFWLCF SNVHSCRGGN WMATPSYVVT ADSIEGPWSE
     PVPIGNYGFD PSLFHDDDGK KYMLNMIWGG RAKTNFFGGI IMQEFDADEG KLVGAPKTVF
     EGTELGCTEG PQLLKKDDYY YLITAEGGTE RNHAVTVCRS KHIWGPYEVH PENPILTSRF
     QEHAELSRAG HGFLVETQTG EWYMSHLCGR RIPNPEGYQF MPKYDNGFSI LGRESALQKA
     HWQDDWPYIA TGKTPVVEVE APNLPLHPWP ESPARDEFID PTLSLISTLR EPVSEKWLSL
     SERPGFLRLK GRHYLYSRYE QSMVARRFQA HNATVETKLE FKPNTPYEMA GLCAYYARNG
     HYFLKMTAND LGERVLQVVG NINDVYGEYS NDVVIGDADT VYMRLELKTQ WYQYSYSLDG
     VDWYEIGPAL NSTPLSDEGG PDIFRFTGSF AALFVADITG QKRHADFDYF EYLEH