ID A0A1G9MQP7_9ACTN Unreviewed; 478 AA.
AC A0A1G9MQP7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=SAMN05216298_5109 {ECO:0000313|EMBL:SDL76237.1};
OS Glycomyces sambucus.
OC Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC Glycomyces.
OX NCBI_TaxID=380244 {ECO:0000313|EMBL:SDL76237.1, ECO:0000313|Proteomes:UP000198662};
RN [1] {ECO:0000313|EMBL:SDL76237.1, ECO:0000313|Proteomes:UP000198662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3147 {ECO:0000313|EMBL:SDL76237.1,
RC ECO:0000313|Proteomes:UP000198662};
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}.
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DR EMBL; FNGF01000009; SDL76237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9MQP7; -.
DR STRING; 380244.SAMN05216298_5109; -.
DR Proteomes; UP000198662; Unassembled WGS sequence.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
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; PF00553; CBM_2; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
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 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};
KW Xylan degradation {ECO:0000313|EMBL:SDL76237.1}.
FT DOMAIN 42..355
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 374..478
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 355..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 277
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 478 AA; 51242 MW; 76D451C6A43D5D5C CRC64;
MLLSRPHLSR QRPSRQRRRA VIAGVVTVAT AALGLGLSTQ FASAQTTLRG AADDLNKDIG
VAVSYNLLQN NAQYRNLVAT EFNSLTAENA MKWDATEPSD GNYTFTQADA IVDFAEDNDQ
TVHGHTFVWH QQTPSWVQNL SGTALQTAMV EHINTVANRY EGRVDSWDVV NEVVSDSNGA
MRDSFWLRGL GEGYITTAFQ TARAADPNAD LYINDYSIDG INAKSNKVYS IAQGLKSQNI
LDGVGFQAHL ILGQVPSDME ANLQRFVNLG LKVRITELDI RIQTPADANE LQQQANDYRR
VTEICAELAD CSGVTVWGVR DGDSWVPGVF PGYGAPLLFN DDLSKKPAYN AVLDALGGDG
NEEPTTSNPV TTTPPPSGSG CTATLSVQSP WNTGATYSGT VKANQNLTGW TVTWTWPGSE
RISNAWSVQG NLSGATVTGS NVGYNGTVAS GQTTTFGFNI TKANGSTASV PTVTCTPA
//
