ID A0A1V2Q9T7_9PSEU Unreviewed; 461 AA.
AC A0A1V2Q9T7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=ALI22I_30775 {ECO:0000313|EMBL:ONI84864.1};
OS Saccharothrix sp. ALI-22-I.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI84864.1, ECO:0000313|Proteomes:UP000188617};
RN [1] {ECO:0000313|EMBL:ONI84864.1, ECO:0000313|Proteomes:UP000188617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI84864.1,
RC ECO:0000313|Proteomes:UP000188617};
RX PubMed=28087533;
RA Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA Kuske C.R.;
RT "Polysaccharide degradation capability of Actinomycetales soil isolates
RT from a semi-arid grassland of the Colorado Plateau.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
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:ONI84864.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MTQP01000066; ONI84864.1; -; Genomic_DNA.
DR RefSeq; WP_077009023.1; NZ_MTQP01000066.1.
DR AlphaFoldDB; A0A1V2Q9T7; -.
DR STRING; 1933778.ALI22I_30775; -.
DR OrthoDB; 9815836at2; -.
DR Proteomes; UP000188617; Unassembled WGS sequence.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
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; PF00553; CBM_2; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00591; GH10_1; 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|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:UP000188617};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:ONI84864.1}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..461
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012257049"
FT DOMAIN 32..335
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 361..461
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 336..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 269
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 461 AA; 48494 MW; 23D5E801B24EBBC3 CRC64;
MKLTSRSVLR AVLVSTLVTA TTGAAVLLAT SANAGTTLGT AAAESGRYFG TAVAAGRLGD
STYAGLLQRE FNMVTAENEM KIDATEPNQN QFTFGNADRI VNLARSQGKR VRGHTLAWHS
QQPGWMQNMS GSALRSAMLN HVTRVAGYYA GKIYAWDVVN EAFQDGSSGA RRDSNLQRTG
NDWIEAAFRA ARAADPNAKL CYNDYNTDDW THAKTQAVYR LVQDFKQRGV PIDCVGLQSH
FNPQSPVPGN YQTTLQNFAN LGVDVQITEL DIEGSGSAQA ANYERVVKAC LAVARCTGIT
VWGIRDTDSW RASGTPLLFD GSGNKKPAYT STLNALNSAG PTVPTSTTTT TTGPTTTTTT
SVPGPGGCTA SVTLNSWTGG FTATVNVTAG SAAINGWTVT LTLPSGATVT NAWNADRSGN
SGTIQWKNVS YNGRVAAGQS TEFGFQGNGT GAGMTPTCSA S
//
