ID E6UGC8_RUMA7 Unreviewed; 829 AA.
AC E6UGC8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
DE Flags: Precursor;
GN OrderedLocusNames=Rumal_1460 {ECO:0000313|EMBL:ADU21966.1};
OS Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 /
OS 7).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=697329 {ECO:0000313|EMBL:ADU21966.1, ECO:0000313|Proteomes:UP000006919};
RN [1] {ECO:0000313|EMBL:ADU21966.1, ECO:0000313|Proteomes:UP000006919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7
RC {ECO:0000313|Proteomes:UP000006919};
RX PubMed=21914885; DOI=10.1128/JB.05621-11;
RA Suen G., Stevenson D.M., Bruce D.C., Chertkov O., Copeland A., Cheng J.F.,
RA Detter C., Detter J.C., Goodwin L.A., Han C.S., Hauser L.J., Ivanova N.N.,
RA Kyrpides N.C., Land M.L., Lapidus A., Lucas S., Ovchinnikova G.,
RA Pitluck S., Tapia R., Woyke T., Boyum J., Mead D., Weimer P.J.;
RT "Complete genome of the cellulolytic ruminal bacterium Ruminococcus albus
RT 7.";
RL J. Bacteriol. 193:5574-5575(2011).
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}.
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DR EMBL; CP002403; ADU21966.1; -; Genomic_DNA.
DR RefSeq; WP_013498134.1; NZ_JHYT01000043.1.
DR AlphaFoldDB; E6UGC8; -.
DR STRING; 697329.Rumal_1460; -.
DR KEGG; ral:Rumal_1460; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_341911_0_0_9; -.
DR OrthoDB; 9809277at2; -.
DR Proteomes; UP000006919; Chromosome.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF02018; CBM_4_9; 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; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
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 Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
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}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:ADU21966.1}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..829
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038943925"
FT DOMAIN 184..537
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT REGION 714..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 457
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 829 AA; 91789 MW; EEA4CBD1A0C189DF CRC64;
MKKHKKILAS LMALSCLTTA MPQFTAPVYA QEVVYDSFEI NYDGWHGTDT SIELTAIDNG
GYDSSRGMKV TGRTSTEDGA ASSKGLYLFG GVKYDYSMQV LSEKDTTFRL DLKYIDEETD
EVTVVTLDEK KVKGGKWAEL TADYKAPENT YEYELTLTND NTDDFIFDDV KVTAEKSAAI
AAAAPYGKGL KDEFADYFRV GNILNGNTVN NSAIKGIMLK DHNAIECENE TKPDATIVQN
GSSDTNVKVS LSRCASILDF CAKNNIAFRG HTLVWHSQTP EWFFKQGFNN NNGYVNSYTM
DQRMESYIKN MFNAYATQYP SVNLYAYDVC NEVIYDGTAN NGGLRPTNGT NGQNGSSAWV
RVYGNNSFVE KAFTYARKYA PKGCKLYYND YNEFARDKKN CIKNTILVPL HNKGLLDGMG
MQSHIDCSAY NSWGSTQEYL AAMDDYLSLG IDVQVTELDI SRDGYKYSDQ QQAEKYKAIF
QHCVDVNKSG KYKGKVTLVQ VWGPNDNNSW VGKTGNLPLL YDGNNQPKTA YNYITSIIPD
SQWGDGSKFN GGAEVKPIEP NQYGWYFNYG FEGSTDNFNS RGAASIASST NTAFVGNSSL
YVSGRESAWN GASYTLDTRA FKAGTEYSFS AIVNYLEGPS TDKFHFTMQY DDASGTTNYT
KIATETVTKG QWTQLANKNF KIPDGASNVQ IYVETDSSTT SFYVDEVIGA VAGTGIKGPE
KTNTDPDPDP QQTYGDTYPQ NIRLNYSAQY HQIQFTWSAV SNAQNYGIAV YLAGKWRVQT
QSISGSTLSY VTPKNLTPGM SYKVAIAAKV NGTWDVANAI RNAVLVTVI
//
