ID A0A180EQB3_9BACT Unreviewed; 640 AA.
AC A0A180EQB3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=A3850_003300 {ECO:0000313|EMBL:OAV43579.1};
OS Lewinella sp. 4G2.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC Lewinella.
OX NCBI_TaxID=1803372 {ECO:0000313|EMBL:OAV43579.1, ECO:0000313|Proteomes:UP000076582};
RN [1] {ECO:0000313|EMBL:OAV43579.1, ECO:0000313|Proteomes:UP000076582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G2 {ECO:0000313|EMBL:OAV43579.1,
RC ECO:0000313|Proteomes:UP000076582};
RA Wong S.-K., Yoshizawa S., Ogura Y., Tetsuya H., Nakajima Y., Hamasaki K.;
RT "Lewinella sp. 4G2 Genome sequencing.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAV43579.1}.
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DR EMBL; LVWJ02000014; OAV43579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180EQB3; -.
DR STRING; 1803372.A3850_003300; -.
DR OrthoDB; 9809277at2; -.
DR Proteomes; UP000076582; Unassembled WGS sequence.
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 InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000076582}.
FT DOMAIN 76..410
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 640 AA; 70382 MW; 7AF774CE0ED8FD8D CRC64;
MSAWRCELVG KWGILGFPKT INMRSTITRI CLLFATFTAV VSLSAQTPLK DIADQKKVYV
GNIISNQHLD NPAGFNGGRA DANLRGEYNA AVLENYMKMS FVLPFREPAN IHELTVDQLR
GQLRTSQMET FLSRSGWQGL RKRGHAMIWF SQAPAWLNNS APSWTAEQVF DFSRKYILAL
GQVAGDRIEE WDVINEAISD NFPATWRPGT WYRKANDGSE TSWGTATYEN YIKMLFVWAR
EAQPNSRLYY NDYSIERFGS STNSKNGFMR SKFKALRACG APVDGIGFQS HFVLSNLVSS
TGAMNTSFLR SVRQTMEDLD AAGLDVAITE LDIRICNNGR PEAFQETAFR EFVAMALSQP
NCRELLFWGL RDEDNWITLT NNPPFNGCQD AAIFEGNYVP KAAYNGVVDA LNGLPDRDEY
GFAELVAGDA GPADCGGEPD LGGDAILAVV APDIVRQGET VNVEVTYESA TNRDIVIYFQ
YDRNPYTVFQ EARLAVTQGE GTVSIPVAIP NDVPIAADDY QFQTLIATTG GGWNERISNI
EKTDIDVVSG ATSITSPGGD QFVASAFPNP TDGRVKLALR SAPVVTDYVV FNATGQLVQQ
GQAPIGVTDL SLILADVPAG LYTVVLQRGG RSNVVRVVRL
//
