XYNB_BUTFI
ID XYNB_BUTFI Reviewed; 635 AA.
AC P26223;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Endo-1,4-beta-xylanase B;
DE Short=Xylanase B;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase B;
GN Name=xynB;
OS Butyrivibrio fibrisolvens.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=831;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H17C;
RX PubMed=1909424; DOI=10.1007/bf00282447;
RA Lin L.-L., Thomson J.A.;
RT "Cloning, sequencing and expression of a gene encoding a 73 kDa xylanase
RT enzyme from the rumen anaerobe Butyrivibrio fibrisolvens H17c.";
RL Mol. Gen. Genet. 228:55-61(1991).
CC -!- FUNCTION: B.fibrisolvens is located in the rumen of ruminant animals,
CC where it contributes to the animal's digestion of plant material by
CC hydrolyzing hemicellulose with its xylanases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
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DR EMBL; X61495; CAA43712.1; -; Genomic_DNA.
DR PIR; S16567; S16567.
DR AlphaFoldDB; P26223; -.
DR SMR; P26223; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR ESTHER; butfi-xynb; Hormone-sensitive_lipase_like.
DR UniPathway; UPA00114; -.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Xylan degradation.
FT CHAIN 1..635
FT /note="Endo-1,4-beta-xylanase B"
FT /id="PRO_0000184062"
FT DOMAIN 1..337
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 150
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 255
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 635 AA; 73185 MW; D2CC7A638FA0F317 CRC64;
MNLKTAYEPY FKIGAAISRW NLHTPAHTKL LAEQFNSFTC ENDMKPMYYL DREANKKDPE
KYNLSPALTF ENAIPYLEFA KDNKIAMRGH TLVWHNQTPK WFFCERYNEN FPMADRETIL
ARLESYIHGV LDFVQTNYPG IIYAWDVVNE IVDEGAFRKS IWTETVGEDF FIKAFEFARK
YAAPEVSLFY NDYETAQPWK RDFILEKVLG PLIDKKLIDG MGMQSHLLMD HPDISEYRTA
LEMYGSTGLQ IHITELDMHN ADPSEESMHA LATRYQEFFQ TYLDAKKSGK ANITSVTFWN
LLDENSWLSG FRRETSYPLV FKGKCEAKEA YYAVLKAAVS DDSIDKWVPD YSEEDYKLQG
MPTPDIKRFR ENIWQENEYN YEASYGFIPN LFAYLHNDDV KRDCMLVIPG GGYCMCCSHE
GELAAMEFYN RGMNAFVLSY TTDITMSVPL HKQPLEDISR AVRFIRKNAS KYNIDGKKLV
IMGFSAGSHV CGSLAVHFDD VKDNNPEYAD ISGRPDGVIL SYPVITTGRY THADSVRTLL
GANPTDEELT YFSLEKQVKD NTPPCFIWQT EEDSVVPVEN SYLFANALRE KKIPFAHYVF
PRGFHGLTVA NDEFFSGWSG GEYSMEQTMR ARFAV
