ID A0A1G0XXV2_9BACT Unreviewed; 617 AA.
AC A0A1G0XXV2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=A2X48_00545 {ECO:0000313|EMBL:OGV38489.1};
OS Lentisphaerae bacterium GWF2_49_21.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798573 {ECO:0000313|EMBL:OGV38489.1, ECO:0000313|Proteomes:UP000178513};
RN [1] {ECO:0000313|EMBL:OGV38489.1, ECO:0000313|Proteomes:UP000178513}
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|ARBA:ARBA00007495, 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:OGV38489.1}.
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DR EMBL; MHBH01000058; OGV38489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0XXV2; -.
DR STRING; 1798573.A2X48_00545; -.
DR Proteomes; UP000178513; 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; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 SUPFAM; SSF49785; Galactose-binding domain-like; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..617
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009569824"
FT DOMAIN 267..560
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
SQ SEQUENCE 617 AA; 69086 MW; 6DC53C7B9E0FF4B7 CRC64;
MKILSCLILA GGMIIPFADF AGAEDAVQKL PEGKSMTPEN AIAAAVPMGQ KGTIEKVAVE
GRSFKEALRI TVSEKCKAPW DMQFAIPCGM KLSKGDAVVV RMWARTLSAV NETGEAYISG
GAQRNKAPHE KPVWASLSVP REWQRVEFGG ISNIDIPQNE VMLFMHLGQN IQSLEIADIQ
MVNLGQGIPK NLLPIMKLTY DGRKPDAPWR KPADESIEKI RKGNISVKVA DADGKPVEGA
DVQIKMKKHA FPFGTCVNAD FLGGVRDENN PEVKKYREEF LKLFNCAVVE NHLKPPRWED
PKSRECVLKA LKWLKGNDIL IRGHTAVWPS ERHFASSWKK IIGYKEGDHV RNKEQLLTAV
TEDNKKKLQD AVQNHVTDIF TATKGYCFQW DVMNEPYSEH TLMDLFGDQV MVDWFKAAKL
ADPDTRLCIN DYGIVMDGNH AEHYMKTIKY LLDNGAPVEG IGEQGHYGQQ PPAISKVLQT
YDMLGSFGLP VMCTEFDIDS QDEEIQADFL VDYMTALFSH PSCGGFLMWG FWEGAHWKPE
AALLRKDWKQ KPSYKAYCDL VLKKWWTDAA GKSGKDGAYG VRGFLGDYEI TVSKDGKTKT
EKLKLGKDDT SISIKLE
//
