ID A0A0M2RBD4_9ACTN Unreviewed; 270 AA.
AC A0A0M2RBD4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
DE Flags: Fragment;
GN ORFNames=LQ51_30685 {ECO:0000313|EMBL:KKJ93260.1};
OS Micromonospora sp. HK10.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1538294 {ECO:0000313|EMBL:KKJ93260.1, ECO:0000313|Proteomes:UP000034330};
RN [1] {ECO:0000313|EMBL:KKJ93260.1, ECO:0000313|Proteomes:UP000034330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK10 {ECO:0000313|EMBL:KKJ93260.1,
RC ECO:0000313|Proteomes:UP000034330};
RA Talukdar M., Das D., Borah C., Deka Boruah H.P., Bora T.C., Singh A.K.;
RT "Draft genome sequence of Micromonospora HK10, isolated from Kaziranga
RT National park, Assam, India.";
RL Submitted (NOV-2014) 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:KKJ93260.1}.
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DR EMBL; JTGL01000269; KKJ93260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2RBD4; -.
DR STRING; 1538294.LQ51_30685; -.
DR HOGENOM; CLU_1032492_0_0_11; -.
DR Proteomes; UP000034330; 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; 3.20.20.80; Glycosidases; 1.
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 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:KKJ93260.1};
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:KKJ93260.1}.
FT DOMAIN 1..270
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKJ93260.1"
FT NON_TER 270
FT /evidence="ECO:0000313|EMBL:KKJ93260.1"
SQ SEQUENCE 270 AA; 29686 MW; 8DC881F8637950E7 CRC64;
GDSTYSTIAA REFNMITAEN EMKPDATEPQ RGQFNFNSGD QIYNWATQRG LKVRGHTLAW
HAQQPGWMQS LSGSSLRQAM IDHINGVMAH YKGKLAAWDV VNEAFNEDGS RRSSNLQGTG
NDWIEVAFRT ARNADPSVKL CYNDYNIENW SYAKTQGVYR MIQDFKSRGV PIDCVGLQTH
FTGGSSLPSN FQTTLSSFAA LGVDVALTEV DVTNSSTTQY AGLTQACINV PRCIGITVWG
VRDSDSWRSG ESPLLFDGGG NKKAAYNSVL
//
