ID   A0A0M9VMA0_9MICO        Unreviewed;       425 AA.
AC   A0A0M9VMA0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=XI38_04455 {ECO:0000313|EMBL:KOS11782.1};
OS   Microbacterium chocolatum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=84292 {ECO:0000313|EMBL:KOS11782.1, ECO:0000313|Proteomes:UP000037737};
RN   [1] {ECO:0000313|EMBL:KOS11782.1, ECO:0000313|Proteomes:UP000037737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIT 101 {ECO:0000313|EMBL:KOS11782.1,
RC   ECO:0000313|Proteomes:UP000037737};
RA   Li X., Xu Y.;
RT   "Complete genome sequence of Microbacterium chocolatum SIT 101, a bacterium
RT   enantioselectively hydrolyzing mesomeric diesters.";
RL   Submitted (APR-2015) 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:KOS11782.1}.
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DR   EMBL; LAVO01000003; KOS11782.1; -; Genomic_DNA.
DR   RefSeq; WP_053547096.1; NZ_KQ440285.1.
DR   AlphaFoldDB; A0A0M9VMA0; -.
DR   KEGG; mcw:A8L33_01745; -.
DR   PATRIC; fig|84292.3.peg.924; -.
DR   OrthoDB; 3255194at2; -.
DR   Proteomes; UP000037737; 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:KOS11782.1};
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:UP000037737};
KW   Xylan degradation {ECO:0000313|EMBL:KOS11782.1}.
FT   DOMAIN          66..366
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
SQ   SEQUENCE   425 AA;  46668 MW;  D96D248F727B46E9 CRC64;
     MFHDLSPRFR DVSLRILDAD GAPADPASVV VEQTRHAFGF GNIGFDFLGL LGGATSGPDG
     DREALAAADV ALAEHLLEAW LAVFDTVTLP FYWRFFEPAP GHPDTARLQA TARWFADRGV
     RVKGHPLVWH TLAPAWLLDR TDAEVEAAIR ARIRREATDF AGLVDQWDAI NEVVILPDFT
     AEDNAVTRLA RSRGRVEMVR MAFETAREAD PSARLVLNDF DLSPRYERLI EECQAAGIRI
     DAIGLQTHMH QGFRGEDQLA SILERFARFG LPLQLTETTL VSGDLMPPEI VDLNDHVVSE
     WPSTPEGEAR QADELERHYR TALAHPAVES LTMWGITDAG AWLGAPVGLL RADGSEKPSY
     AMLRNLIRGE WWHAPRAIAP DADGLIRVRG FAGDYRATAA AGSATFSIAP DADAAAAALE
     VRLTR
//