ID A0A1H1SFK0_9ACTN Unreviewed; 457 AA.
AC A0A1H1SFK0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=SAMN04489716_0843 {ECO:0000313|EMBL:SDS46588.1};
OS Actinoplanes derwentensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=113562 {ECO:0000313|EMBL:SDS46588.1, ECO:0000313|Proteomes:UP000198688};
RN [1] {ECO:0000313|EMBL:SDS46588.1, ECO:0000313|Proteomes:UP000198688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43941 {ECO:0000313|EMBL:SDS46588.1,
RC ECO:0000313|Proteomes:UP000198688};
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; LT629758; SDS46588.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1SFK0; -.
DR STRING; 113562.SAMN04489716_0843; -.
DR OrthoDB; 3255194at2; -.
DR Proteomes; UP000198688; Chromosome i.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000198688};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Xylan degradation {ECO:0000313|EMBL:SDS46588.1}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..337
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 364..457
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 338..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 271
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 457 AA; 48914 MW; 9D0B7A3BBE9CE06F CRC64;
MKEQRRSGRW KAVAVTGMAV VMTAATAVVW QGTSSAASTL GASAAERGRY FGVAIAGSRL
GDSQYATIAN REFNMVSAEN EMKPDATEPN QNQFSFGAGD QIANWARSNG KQVRGHTLAW
HSQQPGWIQR MEGSGLRSAM LNHVTRVASY YQGKIHSWDV VNEAFADGSS GARRDSNLQR
TGNDWIEAAF RAARAADPGA KLCYNDYNTD NWSHAKTQGV YRMVQDFKSR GVPIDCVGFQ
AHFNSGNPVP SNYHTTLQNF ADLGVDVQIT ELDIEGSGSS QAEQYRGIVQ ACLAVTRCNG
ITVWGVRDTD SWRASGTPLL FNGSGQKKAA YDAVLAQLNT PGGNDPSGTP SGSPTPGPSG
SPTTPPPSGT CTATYSEGQK WNDRFNGQVT VTGSGNWIVT VTVSSPQRIT ATWNVSATWD
SSGNVMTGRP NGSGDTFGFT VQHGGNWTWP ALTCRTA
//
