ID A0A1C6US97_9ACTN Unreviewed; 811 AA.
AC A0A1C6US97;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=GA0070603_2312 {ECO:0000313|EMBL:SCL56922.1};
OS Micromonospora chersina.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47854 {ECO:0000313|EMBL:SCL56922.1, ECO:0000313|Proteomes:UP000198605};
RN [1] {ECO:0000313|EMBL:SCL56922.1, ECO:0000313|Proteomes:UP000198605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44151 {ECO:0000313|EMBL:SCL56922.1,
RC ECO:0000313|Proteomes:UP000198605};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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 -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC Evidence={ECO:0000256|ARBA:ARBA00001462};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|RuleBase:RU361174}.
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DR EMBL; FMIB01000002; SCL56922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6US97; -.
DR STRING; 47854.GA0070603_2312; -.
DR OrthoDB; 4241492at2; -.
DR Proteomes; UP000198605; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08987; GH62; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR005193; GH62_arabinosidase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR40631; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR PANTHER; PTHR40631:SF1; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF03664; Glyco_hydro_62; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW Glycosidase {ECO:0000256|RuleBase:RU361174, ECO:0000313|EMBL:SCL56922.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000313|EMBL:SCL56922.1}.
FT DOMAIN 44..342
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT REGION 490..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 811 AA; 86825 MW; 16A8FFEB7B57D384 CRC64;
MAMSPSLHRG GSRRRLSPAV RALLAGAVSA VTVAAVAVMM PSANAAASTL GAAAAQSGRY
FGTAIAAGRL GDSTYTTIAG REFNMVTAEN EMKPDATEPQ RGQFNFSSGD QIYNWATQRG
MKVRGHTLAW HAQQPGWMQS LSGSSLRQAM IDHINGVMAH YKGKLAAWDV VNEAFNEDGS
RRQSNLQGTG NDWIEVAFRT ARTADPSVKL CYNDYNIENW SYGKTQGVYR MIQDFKSRGV
PIDCVGLQTH FTGGSSLPSN FQTTLSSFAA LGVDVALTEV DVTNASTSQY AGLTQACMNV
PRCIGITVWG VRDSDSWRSN ENPLLFDGGG NKKAAYTSVL NALNAAAPTS GPTTTPTTGP
PPSGGAGRIV GVQSGRCIDV PNATQTNGTR VQLWDCNGQS NQQWTYTTSK QLMVYGTKCL
DANGAATGNG TGIIIWDCNG QSNQQWNVNS NGTISGVQSG RCLDVWGTGN GQQIQLYDCH
GQTNQQWRTD FGGTTPPTTP PPTTTPPPGG CALPSTYRWS STGALANPQN GWVSLKDFTN
VVYNGKHLVY GSNVNSSGQY GSMNFSLFTN WSDMASAGQT GMSQGTVAPT LLYFAPKNIW
VLAYQWGPTS FSYKTSSDPT NANGWSSAQT LSTATLPDAP YGVIDQTLIG DDQNMYLFFA
GDNGKIYRSS MPLGNFPGSF GSNYTTIMTD STNNLFEGVE VYKVAGQNQY LMIVEAIGSQ
GRYFRSFTSN SLSGSWTPQA ASESNPFAGK ANSGATWTND ISHGDLVRTN PDQTKTIDAC
NLQFLYQGKN PSAGGDYNLL PWRPGVLTLQ R
//
