ID S4YBS3_SORCE Unreviewed; 287 AA.
AC S4YBS3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=SCE1572_49270 {ECO:0000313|EMBL:AGP41791.1};
OS Sorangium cellulosum So0157-2.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP41791.1, ECO:0000313|Proteomes:UP000014803};
RN [1] {ECO:0000313|EMBL:AGP41791.1, ECO:0000313|Proteomes:UP000014803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP41791.1,
RC ECO:0000313|Proteomes:UP000014803};
RX PubMed=23812535; DOI=10.1038/srep02101;
RA Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT milieu.";
RL Sci. Rep. 3:2101-2101(2013).
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; CP003969; AGP41791.1; -; Genomic_DNA.
DR AlphaFoldDB; S4YBS3; -.
DR STRING; 1254432.SCE1572_49270; -.
DR KEGG; scu:SCE1572_49270; -.
DR PATRIC; fig|1254432.3.peg.11113; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_041139_0_0_7; -.
DR Proteomes; UP000014803; Chromosome.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide 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.
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}.
FT DOMAIN 1..283
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 218
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 287 AA; 32816 MW; 9944400FDEC569BB CRC64;
MGKFVGNITT NGNVRDGFAK YWNQITPENE GKWGSVERSR GNRDWSALDR IYKYAQDNNI
IFKHHVFVWG AQQPDWVGRL SGGEQQAAVR DWMKAFCERY PETKYIDVVN EPPPHTTPSY
KNGIGGDGAS GWDWIVNSFK WAREFCPDAV LILNDYNNIE YENDHNNFMR IARAVIGAGA
PVDALGAQAH DAYKINTNTV KGYIDKMASL GKPVYITEYD IGIADDNQQK RVMEEQFTMF
WNHPSVPGIT LWGYIVGATW RDNTGLQHPD GRLRPAMQWL MDFLERN
//
