ID A0A1U7MPL8_9MICO Unreviewed; 389 AA.
AC A0A1U7MPL8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=BJF81_04565 {ECO:0000313|EMBL:OLT20551.1};
OS Ornithinimicrobium sp. CNJ-824.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Ornithinimicrobium.
OX NCBI_TaxID=1904966 {ECO:0000313|EMBL:OLT20551.1, ECO:0000313|Proteomes:UP000185694};
RN [1] {ECO:0000313|EMBL:OLT20551.1, ECO:0000313|Proteomes:UP000185694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNJ-824 {ECO:0000313|EMBL:OLT20551.1,
RC ECO:0000313|Proteomes:UP000185694};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
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:OLT20551.1}.
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DR EMBL; MKKA01000044; OLT20551.1; -; Genomic_DNA.
DR RefSeq; WP_075958560.1; NZ_MKKA01000044.1.
DR AlphaFoldDB; A0A1U7MPL8; -.
DR STRING; 1904966.BJF81_04565; -.
DR OrthoDB; 9815836at2; -.
DR Proteomes; UP000185694; 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:OLT20551.1};
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:UP000185694};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:OLT20551.1}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..389
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012504882"
FT DOMAIN 63..373
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT REGION 27..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 42953 MW; 1D9A9F98B899F58D CRC64;
MRHLTRSVVV AAATTALAAA AAVPAATAAP PDHAQGHQDT LRRQAPKDLQ IGSAVWGQRD
LIGYDRKNLT DHQRVLAREF GSITPENDMK WAEVHPEPDV YDFSGADALM EFARANNQEV
RGHTLLWHSQ NPEWVNEAAA DWSCEEARDV LEDHVRTVVG RYAGEIYEWD VANEIIQDDW
DAGGVRLRTE ANPFLAACAD DPVALIGDTF RWAHETDPQA RLFLNDYNAE GINAKTDAYY
ALAQELLADG VPLHGFGAQG HLSLQYGFDT SIQANFERFA ALGLDVAVTE ADVRVPIEEG
WDGPTPEQVD LHAERHDAML EACLAVPSCT SFTVWGFPDA NSWVPDVFPG EEWATIFTDD
YTPKPAYHAM LESLREATPG VSPRTPRGR
//
