ID A0A139D675_9FIRM Unreviewed; 625 AA.
AC A0A139D675;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
DE Flags: Fragment;
GN ORFNames=AWL62_1439 {ECO:0000313|EMBL:KXS49019.1};
OS Halanaerobium sp. T82-1.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=1794808 {ECO:0000313|EMBL:KXS49019.1, ECO:0000313|Proteomes:UP000070487};
RN [1] {ECO:0000313|EMBL:KXS49019.1, ECO:0000313|Proteomes:UP000070487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T82-1 {ECO:0000313|EMBL:KXS49019.1};
RA Wolfe R., Daly R., Wrighton K.;
RT "Halanaerobium-1 T82 Annotated.";
RL Submitted (JAN-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:KXS49019.1}.
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DR EMBL; LSBN01000057; KXS49019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139D675; -.
DR PATRIC; fig|1794808.3.peg.1342; -.
DR Proteomes; UP000070487; 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; cd00005; CBM9_like_1; 1.
DR Gene3D; 2.60.40.1190; -; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR010502; Carb-bd_dom_fam9.
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; PF06452; CBM9_1; 2.
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; 2.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {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|RuleBase:RU361174};
KW Xylan degradation {ECO:0000313|EMBL:KXS49019.1}.
FT DOMAIN 1..267
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 180
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KXS49019.1"
SQ SEQUENCE 625 AA; 71004 MW; 3CEE3A08AD0C2472 CRC64;
DKIREFTKEN EMVMRGHTLV WHSQVPDWFF EDEEGELVSK EVLLDRMRKH IEKTMEHYKG
DIDSWDVVNE AIDPASTETN GLRNSKWYQI AGIDYIKEAF IHANKIDPEA KLYINDYSLL
SDPAKRDIMY RVVKELLAED IPVDGIGMQG HINIESPSIA TMEKTLDKFA SLGVDLQITE
LDLSVYTNNS QSYDSFSEEL AVKQGHRYRE IFNLFKQYSD SITNVTLWGI ADDHTWLTGF
PVERNNWPLL FDQSLKAKPA FWGVVNPDRL PVITKEFDIS QGSPEIDAES DLIWQNSGDT
LDLEENEYLG GEVKLSWDEN NIYLYAQIED ESKNAEDALE IFVDEANAKT ADSEAIKHYQ
IKRSGESNLK TAAVEKDNSY LIEAVIPVES RNLKVGDQVG FDLKINDAES ETSIIWNDFT
KKQTESAENY GTLNLKEEPV ITEAVYGQAE IDAEMDESWE KANTIKTEKI ISGENPATAE
VKTMWDENTL YIFAEVKDSA LSLAGEQVHE EDSVEIFVDE NNDKSTEYQS DDTQYRINYL
NQQSFNPERE GLKTATRVTE TGYIVEAAVP FVEITAEEGQ IIGFDFQVND DGNGDGTRDG
VAIWNDQSGE GWRNMSGLGN LIFVK
//