ID A0A1I1J4R3_9FIRM Unreviewed; 1389 AA.
AC A0A1I1J4R3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=SAMN02910398_02184 {ECO:0000313|EMBL:SFC40933.1};
OS Butyrivibrio sp. YAB3001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520812 {ECO:0000313|EMBL:SFC40933.1, ECO:0000313|Proteomes:UP000198944};
RN [1] {ECO:0000313|EMBL:SFC40933.1, ECO:0000313|Proteomes:UP000198944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YAB3001 {ECO:0000313|EMBL:SFC40933.1,
RC ECO:0000313|Proteomes:UP000198944};
RA de Groot N.N.;
RL Submitted (OCT-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOKR01000009; SFC40933.1; -; Genomic_DNA.
DR STRING; 1520812.SAMN02910398_02184; -.
DR Proteomes; UP000198944; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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 CDD; cd20907; CBM86; 1.
DR CDD; cd00005; CBM9_like_1; 1.
DR Gene3D; 2.60.40.1190; -; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR010502; Carb-bd_dom_fam9.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
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; PF06452; CBM9_1; 1.
DR Pfam; PF01473; Choline_bind_1; 1.
DR Pfam; PF19127; Choline_bind_3; 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; SSF49344; CBD9-like; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR PROSITE; PS51170; CW; 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, ECO:0000313|EMBL:SFC40933.1};
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:UP000198944};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:SFC40933.1}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1389
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038858237"
FT DOMAIN 448..820
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT REPEAT 1264..1283
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REGION 34..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1188
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1210
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1389 AA; 155996 MW; 84EB6F2238A2B46D CRC64;
MHKKWLGFSS VMMAGMLAVS SVSPAAFEAR AAELGEEKAV ITEEASLDET KDSEETKAQK
DTEEKASDEE AKEAAEGSSA ETSEKEEKAS TDVEESKEDD SKADEKESSD EKSEDKVKDD
TEEKKDSKEE ADEEESKDKD SKEKETKEDK EKSDNEDKSE EKDKKDDKKE TDKEKKDDAE
DAEKKDNSLI FFDRWNQSST FSGVLSFEKQ YQEYVYDLGE TYDASIVKSI KVKVSDQGDN
VCIKLYDDSL TEKQANYGCN GSSEYVMIPN YDGKVRYIAV MSMADGEDKY PYGITVDEVS
VDAEASTEQQ NEETVVFKGD DLKFSGRWDK KEVEGNTLTY EEAWSEYWFS FGREFAADSI
KSIKVKVKDQ DLSVAFKIYD ADGGEIQAFY GQNGKNEYVL YPSQDKGATH FAVMAMNDQT
YPGSITIESV EVKVDTTPES EKPEKGVEYD IVDLRDPMTE ILGDDFIVGT AISYQEFADS
AEMELVTKHF NGVTLGNELK PDSMLKKDAE IKTVELNGEE FAFPELNFSN PERYLDFFVD
WNNEHPDKKI RIRGHVLVWH SQTPEFFFHE DYDTSKPYVT PEVMNKRLEY YIKSVAEHFT
AEGSKYRDLF YGWDVVNEAV SDSTGTYRNA SENSSWWAVY NSCEFIQNAF VYANRYMPSN
IALFYNDYNE TGTNKMGGIC ELLKTVKNTE GARIDGMGMQ AHYQIESNSP SMDQFKVAAK
TYGEIVDQVQ ITELDFKGSA NSTDERLAER YKAVYDTIRR LKAEGTNITG MTIWGVVDKH
SWLQTANNNG GGSNGSSRQY PLLFDDNYKA KNSFWALANA GELEPEIKNI ILIQNINGDF
TTGNEYSFGE GESKLSFVPM WDENGVAVKV TVLDGNAEDN DSFTVYADDG NSIKAVTVTR
SEATAVEGGY ESVVRLDVDK DVLASNKLKL DVTFKDGEKT FAFGDTTFKQ ADSSKYFAET
VVKPLLSVNK GTVVVDGDPS DEDWAKAKEL QLTINTGANV TANAKTLWDE ENLYVLVDVK
DPVLNKDSSQ NHEQDSLEVF IDENNHKTTS YEEDDKQYRI NYENTQSFNG KKCLEENMKS
AAVVTEDGYR IEAAFKWTDI TPQAGNKVGL ELQINDADDS GKRIGTLSWA DKTGNGWSSP
EVFGTILLTV ENADTPDTPV DPDPADEPVD PNPSDDPVDP NPTDDPVDPN PSDDPEDPNP
SDDPEDPNPS DDPVDPNPSD DPVDPDPTDD PVDPAPIVEP EKEEARLVSF LGFTFYVTAD
GTRLTGFHTI DGNDYYFGST GIMYRLSWIN ENGNWYYAKL DGTLAKNEIV SRLLSRYIFN
EEGVMQTGFV HFNGNDYYCG TSGAIYTNSF ITVDCKTYYA KNDGRLAKNE TIWRLFRRYR
FDENGVLVK
//
