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Database: UniProt
Entry: A0A1V4EG84_9ACTN
LinkDB: A0A1V4EG84_9ACTN
Original site: A0A1V4EG84_9ACTN 
ID   A0A1V4EG84_9ACTN        Unreviewed;       486 AA.
AC   A0A1V4EG84;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=B1L11_17030 {ECO:0000313|EMBL:OPG11916.1};
OS   Microbispora sp. GKU 823.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Microbispora.
OX   NCBI_TaxID=1652100 {ECO:0000313|EMBL:OPG11916.1, ECO:0000313|Proteomes:UP000190255};
RN   [1] {ECO:0000313|EMBL:OPG11916.1, ECO:0000313|Proteomes:UP000190255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GKU 823 {ECO:0000313|EMBL:OPG11916.1,
RC   ECO:0000313|Proteomes:UP000190255};
RA   Kruasuwan W.;
RT   "Draft genome sequence of sugarcane root-associated plant growth promoting
RT   Microbispora sp. GKU 823.";
RL   Submitted (FEB-2017) 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:OPG11916.1}.
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DR   EMBL; MWJN01000028; OPG11916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4EG84; -.
DR   OrthoDB; 4241492at2; -.
DR   Proteomes; UP000190255; 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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 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:OPG11916.1}.
FT   DOMAIN          42..346
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   DOMAIN          385..486
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          350..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..385
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..405
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        280
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   486 AA;  50433 MW;  DC4F4B6F1E6FBAC7 CRC64;
     MGENPLPADG GRRLVGTRRL LVAGALGVLG TATALAASVP AGAAAGTLGA AAAQSGRYYG
     AAIAAGHMND STYVATWDRE FNAVTPENEM KWDATEPSRG SFRFTSADQI VSHAQSKGMK
     IRGHTLVWHN QLPSWVGGLS ASDLRSAMTN HINNVMGHYK GKIYAWDVVN EAFADGGAVG
     TLRSSVFTQK LGNGFIEEAF RAARAADPNA KLCYNDYNID DANANKTRGV YNMIKDFKAR
     GVPIDCVGLQ SHLSSGSVPS NYQQNIAQFA ALGVDVQITE LDIGGSGSAQ ADAYRRVTQA
     CTAVPRCTGI TVWGITDKYS WRSGDTPLLF DGNFNKKQAY TAVLDALNAA TPNTSPSPTT
     SPNTSPSPTT SPNTSPSPNT SPSPTPPVGG ACSATIETTN SWPGGFQSTV TVRAGSSAVN
     GWTVKWTWPS GQSISSLWNG TQSGSGSSVT VSNASYNGSI AAGSSTTFGF TANGSAATPT
     ATCTSP
//
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