ID Q288H9_9FLAO Unreviewed; 371 AA.
AC Q288H9;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN Name=xyn10 {ECO:0000313|EMBL:AAY98787.1};
OS Flavobacterium sp. MSY2.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=334781 {ECO:0000313|EMBL:AAY98787.1};
RN [1] {ECO:0000313|EMBL:AAY98787.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSY2 {ECO:0000313|EMBL:AAY98787.1};
RX PubMed=16450065; DOI=10.1007/s00284-005-4583-9;
RA Lee C.C., Smith M., Kibblewhite-Accinelli R.E., Williams T.G., Wagschal K.,
RA Robertson G.H., Wong D.W.;
RT "Isolation and characterization of a cold-active xylanase enzyme from
RT Flavobacterium sp.";
RL Curr. Microbiol. 52:112-116(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000256|RuleBase:RU361174};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|RuleBase:RU361174}.
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DR EMBL; DQ059337; AAY98787.1; -; Genomic_DNA.
DR AlphaFoldDB; Q288H9; -.
DR SMR; Q288H9; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361174};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361174};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Xylan degradation {ECO:0000313|EMBL:AAY98787.1}.
FT DOMAIN 24..366
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 260
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 371 AA; 42138 MW; 2914116857044C4A CRC64;
MKFINHCLPL LSLMILGSCN VKKTELSSSL KNSYKNDFYI GTALSADQIE EKDAKVDSLI
CRQFNAITAE NSMKSMFVHP QKDKYDFALT DKFVAFGEKN KMFIHGHTLI WHSQLAPWME
KIKDSTEMKA VMKDHITTIV SKYKGRINSW DVVNEALNDD GTLRKSVFLN TLGESYLADA
FKLAAKADPK VDLYYNDYNL EDPAKREGAI NLIKKIKAAG GKVDGIGSQG HWNLNSPSLE
EIEKSILAYS ALGVKVAFTE LDITVLPNPW DLKGADVNQK FEGNPKMNPY PETLPDSIQD
KLAQRYADIF KLFLKHKDKI SRVTFWGVHD GQSWLNDWPI KGRTNYPLLF DTKLQPKKAY
NSVMQLKEVK E
//
