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Database: UniProt
Entry: A0A1G9MKY2_9ACTN
LinkDB: A0A1G9MKY2_9ACTN
Original site: A0A1G9MKY2_9ACTN 
ID   A0A1G9MKY2_9ACTN        Unreviewed;       606 AA.
AC   A0A1G9MKY2;
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=SAMN05421869_13046 {ECO:0000313|EMBL:SDL74932.1};
OS   Nonomuraea jiangxiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=633440 {ECO:0000313|EMBL:SDL74932.1, ECO:0000313|Proteomes:UP000199202};
RN   [1] {ECO:0000313|EMBL:SDL74932.1, ECO:0000313|Proteomes:UP000199202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6533 {ECO:0000313|EMBL:SDL74932.1,
RC   ECO:0000313|Proteomes:UP000199202};
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; FNDJ01000030; SDL74932.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9MKY2; -.
DR   STRING; 633440.SAMN05421869_13046; -.
DR   OrthoDB; 9815836at2; -.
DR   Proteomes; UP000199202; 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; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR044846; GH10.
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; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 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|RuleBase:RU361174, ECO:0000313|EMBL:SDL74932.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199202};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:SDL74932.1}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..606
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011557949"
FT   DOMAIN          262..548
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
SQ   SEQUENCE   606 AA;  65722 MW;  21F9D061F78F2A5D CRC64;
     MGRWTKARRR LAYVIPGALL AALGLAAPAA AADPPTEIMP AHVLEAFTQF TGNPAPRTTI
     VDVQGQPDFD QALQITVTGQ PASPGLDGEY SLGVGAPSAL PTVKGEAMLA TFWARSITPT
     PTGSGLAHFV FEQNGGGYTK STQAAMKFGG TWQRYRLPFR MAADYAAGQV RINFWLGYGP
     QVLQIAGVSV LRYGAGTPDG WPQATYAGRE AGAAWRAAAA DRIERNRKGN LYVKVVDAEG
     HLVPGATVQA DMTRHAFKFG SAADGVRLMT QNTSAQKYRD TLLANFNQFT LGNNLKWNHW
     ENLPERNGYT LPALQWGRDH GLFVRGHTLI WPSCGNMPAD VCGLRGDPAA LRSRIDAHIT
     EEAGALAGLI DEWDVVNEPY ANHDVQDVLG DGELDRWFRL TRQADPGPRL YLNDYDIVED
     NGWEARHQDH FTARVRALKD GGAPIGGIGI QGHFAGEQLT PPADLVTLIN RFGGLGLPVA
     ITEFDVGTTD EQLQADYTRD FLTTMFSMPQ VTGVSTFGFW EGDTWDPKRA LFRTDWTLKP
     NGRAWRDLIY GTWWTKATAT TGPTGSTTVR GFLGDYTVKV TAGGVTKEVA VSMPTISGKA
     ITVVVG
//
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