ID   YAGH_ECOLI              Reviewed;         536 AA.
AC   P77713; Q2MCF1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Putative beta-xylosidase;
DE            EC=3.2.1.37;
DE   AltName: Full=1,4-beta-D-xylan xylohydrolase;
DE   AltName: Full=Xylan 1,4-beta-xylosidase;
GN   Name=yagH; OrderedLocusNames=b0271, JW0264;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR   EMBL; U70214; AAB08692.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73374.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76055.1; -; Genomic_DNA.
DR   PIR; G64752; G64752.
DR   RefSeq; NP_414805.1; NC_000913.3.
DR   RefSeq; WP_000406871.1; NZ_LN832404.1.
DR   AlphaFoldDB; P77713; -.
DR   SMR; P77713; -.
DR   BioGRID; 4261986; 9.
DR   IntAct; P77713; 5.
DR   STRING; 511145.b0271; -.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   jPOST; P77713; -.
DR   PaxDb; P77713; -.
DR   PRIDE; P77713; -.
DR   EnsemblBacteria; AAC73374; AAC73374; b0271.
DR   EnsemblBacteria; BAE76055; BAE76055; BAE76055.
DR   GeneID; 944949; -.
DR   KEGG; ecj:JW0264; -.
DR   KEGG; eco:b0271; -.
DR   PATRIC; fig|1411691.4.peg.2009; -.
DR   EchoBASE; EB3131; -.
DR   eggNOG; COG3507; Bacteria.
DR   HOGENOM; CLU_016508_2_1_6; -.
DR   InParanoid; P77713; -.
DR   OMA; LVNYYNT; -.
DR   PhylomeDB; P77713; -.
DR   BioCyc; EcoCyc:G6143-MON; -.
DR   PRO; PR:P77713; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Multifunctional enzyme;
KW   Polysaccharide degradation; Reference proteome; Xylan degradation.
FT   CHAIN           1..536
FT                   /note="Putative beta-xylosidase"
FT                   /id="PRO_0000057697"
FT   ACT_SITE        14
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A7LXU0"
FT   ACT_SITE        186
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:A7LXU0"
FT   SITE            127
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   536 AA;  60825 MW;  60D3F038215CD216 CRC64;
     MEITNPILTG FNPDPSLCRQ GEDYYIATST FEWFPGVRIY HSRDLKNWSL VSTPLDRVSM
     LDMKGNPDSG GIWAPCLSYA DGKFWLLYTD VKIVDSPWKN GRNFLVTAPS IEGPWSEPIP
     MGNGGFDPSL FHDDDGRKYY IYRPWGPRHH SNPHNTIVLQ AFDPQTGTLS PERKTLFTGT
     PLCYTEGAHL YRHAGWYYLM AAEGGTSYEH AVVVLRSKNI DGPYELHPDV TMMTSWHLPE
     NPLQKSGHGS LLQTHTGEWY MAYLTSRPLR LPGVPLLASG GRGYCPLGRE TGIARIEWRD
     GWPYVEGGKH AQLTVKGPQV AEQPAAVPGN WRDDFDASSL DPELQTLRIP FDDTLGSLTA
     RPGFLRLYGN DSLNSTFTQS TVARRWQHFA FRAETRMEFS PVHFQQSAGL TCYYNSKNWS
     YCFVDYEEGQ GRTIKVIQLD HNVPSWPLHE QPIPVPEHAE SVWLRVDVDT LVYRYSYSFD
     GETWHTVPVT YEAWKLSDDY IGGRGFFTGA FVGLHCEDIS GDGCYADFDY FTYEPV