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Database: UniProt
Entry: A0A0D0X5T5_9ACTN
LinkDB: A0A0D0X5T5_9ACTN
Original site: A0A0D0X5T5_9ACTN 
ID   A0A0D0X5T5_9ACTN        Unreviewed;       457 AA.
AC   A0A0D0X5T5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=TK50_13460 {ECO:0000313|EMBL:KIR66194.1};
OS   Micromonospora haikouensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=686309 {ECO:0000313|EMBL:KIR66194.1, ECO:0000313|Proteomes:UP000032254};
RN   [1] {ECO:0000313|EMBL:KIR66194.1, ECO:0000313|Proteomes:UP000032254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JXNU-1 {ECO:0000313|EMBL:KIR66194.1,
RC   ECO:0000313|Proteomes:UP000032254};
RA   Long Z., Huang Y., Jiang Y.;
RT   "Sequencing and annotation of Micromonospora carbonacea strain JXNU-1
RT   genome.";
RL   Submitted (JAN-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:KIR66194.1}.
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DR   EMBL; JXSX01000001; KIR66194.1; -; Genomic_DNA.
DR   RefSeq; WP_043963056.1; NZ_JXSX01000001.1.
DR   AlphaFoldDB; A0A0D0X5T5; -.
DR   PATRIC; fig|47853.6.peg.2844; -.
DR   OrthoDB; 3255194at2; -.
DR   Proteomes; UP000032254; 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:UP000032254};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:KIR66194.1}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..457
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038463574"
FT   DOMAIN          31..330
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   DOMAIN          357..457
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          332..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..359
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   457 AA;  47675 MW;  657C82BEDF23C0FF CRC64;
     MRRKRVLLTT VTLAVTGALT AGVLVTMAPA ASAGTTLRAA AAEKGRYFGA AVATGKLSNS
     TYTTILNREF NSVVAENEMK WDATEPQQGV FNYSGGDRLV SHARANGMSV RGHALLWHQQ
     EPGWAQGMSG SALRSAMINH VTQVATHFKG QIYAWDVVNE AFADGGSGGR RDSNLQRTGN
     DWIEAAFRAA RAADPGAKLC YNDYNTDGVN AKSTGIYNMV RDFKSRGVPI DCVGFQSHLG
     TTLASDYQAN LQRFADLGVD VQITELDVMT GGNQANIFGA VTRACMNVSR CTGITVWGVR
     DCDSWRGSDN ALLFDCNGNK KPAYDSVLNA LNAGTGIPNP TTTPPNPTTT PPNPTTPPPG
     GAGCSATVSA NSWTGGFVAT VKVTAGSGGT RGWNVSVTLP GGTSVTGTWS ATASGSSGTV
     RFANVDYNGQ LAAGQVTEFG FQGNGTAPTQ TPTCTAS
//
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