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Database: UniProt
Entry: A0A1G5VW90_9BACT
LinkDB: A0A1G5VW90_9BACT
Original site: A0A1G5VW90_9BACT 
ID   A0A1G5VW90_9BACT        Unreviewed;       365 AA.
AC   A0A1G5VW90;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=SAMN03080617_00743 {ECO:0000313|EMBL:SDA49696.1};
OS   Algoriphagus alkaliphilus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=279824 {ECO:0000313|EMBL:SDA49696.1, ECO:0000313|Proteomes:UP000198756};
RN   [1] {ECO:0000313|EMBL:SDA49696.1, ECO:0000313|Proteomes:UP000198756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22703 {ECO:0000313|EMBL:SDA49696.1,
RC   ECO:0000313|Proteomes:UP000198756};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FMXE01000004; SDA49696.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5VW90; -.
DR   STRING; 279824.SAMN03080617_00743; -.
DR   OrthoDB; 9809277at2; -.
DR   Proteomes; UP000198756; 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; 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; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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   Xylan degradation {ECO:0000313|EMBL:SDA49696.1}.
FT   DOMAIN          19..365
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   ACT_SITE        260
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   365 AA;  41741 MW;  2028A305B7805DBB CRC64;
     MRKLTVLILL LPLLLACQKP ELESLKNRFQ EDFFIGAAVN LAQVTGREVG ADSLLELHFS
     SITSENGLKW GPVHPKEGEY NFEFGDAYVA MGEKMGAFTI GHTLVWHQQT PAWVFQNGEG
     QFLNQMDLIR RMEDHIATVV GRYKGKIDGW DVVNEAFEDD GSWRKTHWYN ITGTEFIKAA
     FRKANEIDPD VELYYNDYNV WKPEKRKAIL ALAKELRAEG IRIDGIGMQG HYRLNSPSLD
     QIEQAIVEIH DAGFQVMFTE LDVDVLPRPS DSEGADLNIN FAESPEWNPY ADSLPQAVAQ
     ELAARYVSLF QLFRKHSDKI SRVTFWGLHD GRSWLNNWPV RGRTNYALIF DREMKLKAGF
     LEGIE
//
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