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Database: UniProt
Entry: A0A1G9MNJ3_9ACTN
LinkDB: A0A1G9MNJ3_9ACTN
Original site: A0A1G9MNJ3_9ACTN 
ID   A0A1G9MNJ3_9ACTN        Unreviewed;       524 AA.
AC   A0A1G9MNJ3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=SAMN05216298_5081 {ECO:0000313|EMBL:SDL75694.1};
OS   Glycomyces sambucus.
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Glycomyces.
OX   NCBI_TaxID=380244 {ECO:0000313|EMBL:SDL75694.1, ECO:0000313|Proteomes:UP000198662};
RN   [1] {ECO:0000313|EMBL:SDL75694.1, ECO:0000313|Proteomes:UP000198662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3147 {ECO:0000313|EMBL:SDL75694.1,
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|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
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DR   EMBL; FNGF01000009; SDL75694.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9MNJ3; -.
DR   STRING; 380244.SAMN05216298_5081; -.
DR   OrthoDB; 9815836at2; -.
DR   Proteomes; UP000198662; Unassembled WGS sequence.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR044846; GH10.
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; PF02018; CBM_4_9; 1.
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; SSF49785; Galactose-binding domain-like; 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|RuleBase:RU361174, ECO:0000313|EMBL:SDL75694.1};
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:SDL75694.1}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..524
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011655611"
FT   DOMAIN          184..518
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
SQ   SEQUENCE   524 AA;  58232 MW;  1FAF529B46A607FC CRC64;
     MPTPSPRASR RALLAGAAAA GGAAVLPLAT AGPAHADDLL LSTDFSSGTT EGWYPRGAVA
     LSVNAEGNLL VEGRTATWNG PAIDITAHIE VGVRYQLRVL LRLPSGTDAA DLRTTVQRDA
     AGSTAYETVR WNTAVTPDAW TEFTGTYSIT QPADLLQFYV ESDSSLTPVL VDDFTLTRIQ
     EPEIQDLLPL KDFLECDFPI GCAVEPPEVV GKPAELLAKH FAQVTTGNQM KPDAIQPTEG
     VFTFDRADQI VAFAEANGMR IWGHTLLWHN QTPAWWFLDA AGNPLQPTRA HRALLLARFE
     AHVTALAEHY GDRVWAWDVV NEVVDPEQAD GLRRSRWYEV FGGGAYIGEV FKIARRVLPR
     KVKLFINDYN TEFPDKREAL YNLVQDLKRG RVPVDGVGHQ AHVDYKRDPQ LLGESIDAFR
     RLRVLQAVTE LDVSVSDYME ESLPSTPPER LAAQGRYYQE LFAVLRARAR HLESVTMWGL
     YDAVSWLRTW PVSRPHEAPL FFDDRLQAKA AYWGVVDPAQ LPPE
//
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