ID A0A1F8PZ82_9CHLR Unreviewed; 337 AA.
AC A0A1F8PZ82;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=A2Z16_09310 {ECO:0000313|EMBL:OGO28464.1};
OS Chloroflexi bacterium RBG_16_54_18.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797648 {ECO:0000313|EMBL:OGO28464.1, ECO:0000313|Proteomes:UP000177170};
RN [1] {ECO:0000313|EMBL:OGO28464.1, ECO:0000313|Proteomes:UP000177170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO28464.1}.
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DR EMBL; MGNP01000131; OGO28464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8PZ82; -.
DR STRING; 1797648.A2Z16_09310; -.
DR Proteomes; UP000177170; 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; 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; 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|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 18..333
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
SQ SEQUENCE 337 AA; 37883 MW; CFBC38AF7A20C003 CRC64;
MPFDPFSFPA QFASPTLEPS LRSLASARGL WLGTAADGGH LFEIPYAELI GSQFNLLTPE
NAMKWERVQP ARGVYDFREA DALVTFAEQN GMAVYGHVLV WHLQLPDWVL QGEHSREIWI
QILCSHVKTV VNHFRGRILV WNVVNEAMAN EGYLYDNIWL TRIGPDYLDM AFQWAHEADP
QAILAYNDHS AEGLNPKSNA IYSMVKTMVE NGVPIHAVGL QMHISLINAP SHQDLAANIQ
RLANLGLQTH ITEMDVRIQY GKGTRTEKLA LQAEIYRDIL SVCLEQPNCR FFSTWGASDL
HSWIPGITGR PDAPLLFDEQ GQPKPAYEAL IELLSQP
//