ID   I0L712_9ACTN            Unreviewed;       488 AA.
AC   I0L712;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   Name=xlnA {ECO:0000313|EMBL:CCH19609.1};
GN   ORFNames=MILUP08_44484 {ECO:0000313|EMBL:CCH19609.1};
OS   Micromonospora lupini str. Lupac 08.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH19609.1, ECO:0000313|Proteomes:UP000003448};
RN   [1] {ECO:0000313|Proteomes:UP000003448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX   PubMed=22815450; DOI=10.1128/jb.00628-12;
RA   Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA   Carro L., Coll P., Trujillo M.E.;
RT   "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT   Nodules of Lupinus angustifolius.";
RL   J. Bacteriol. 194:4135-4135(2012).
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:CCH19609.1}.
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DR   EMBL; CAIE01000035; CCH19609.1; -; Genomic_DNA.
DR   RefSeq; WP_007461825.1; NZ_HF570108.1.
DR   AlphaFoldDB; I0L712; -.
DR   STRING; 1150864.MILUP08_44484; -.
DR   eggNOG; COG3693; Bacteria.
DR   OrthoDB; 3255194at2; -.
DR   Proteomes; UP000003448; 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   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 3.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   Pfam; PF14200; RicinB_lectin_2; 2.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000003448};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:CCH19609.1}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..488
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003631922"
FT   DOMAIN          29..328
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   ACT_SITE        263
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   488 AA;  52179 MW;  9EE2C31488D2CF8A CRC64;
     MRPKKALLAT ATLAVALTAG MTVALAPMAS AGTTLKASAA EKGRYFGAAV ATGKLSNSQY
     VGILNSEFNS VTPENEMKWD ATERSQGQFS YTGGDRLVSH AQANGMSVRG HALLWHAQQP
     PWAQGMSGTA LRNAAINHVT QVATHFRGKI YAWDVVNEAF ADGGSGGRRD SNLQRTGNDW
     IEAAFRAARA ADPGAKLCYN DYNTDGINAK STGIYNMVRD FKSRGVPIDC VGFQSHLGTT
     LAGDYQANLQ RFADLGVDVQ ITELDVMTGS NQANIYGSVT RACMAVSRCT GITTWGVRDS
     DSWRGSDNAL LFDGSGNKKA AYTSVLNALN GGSTNPTTPP PGTGVDTTAW YVLVNRNSGK
     ALDVYERSTT DGARIDQWAR NDGAWQQWQF VDSGSGYYRL KSRNSGKVLD VANRSTADSA
     PVVQWSDGNG TNQQFRLADS SGGYLRLINR NSGKAVEVQG SSTADGGNVV QYADWGGTNQ
     QWQLVRVG
//