ID A0A0D3LMG1_9BACT Unreviewed; 374 AA.
AC A0A0D3LMG1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=D770_24395 {ECO:0000313|EMBL:AHM63124.1};
OS Flammeovirgaceae bacterium 311.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae.
OX NCBI_TaxID=1257021 {ECO:0000313|EMBL:AHM63124.1, ECO:0000313|Proteomes:UP000064112};
RN [1] {ECO:0000313|EMBL:AHM63124.1, ECO:0000313|Proteomes:UP000064112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=311 {ECO:0000313|EMBL:AHM63124.1,
RC ECO:0000313|Proteomes:UP000064112};
RA Fang C.;
RT "Complete bacteria genome obtained just from illumina data.";
RL Submitted (NOV-2012) 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; CP004371; AHM63124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D3LMG1; -.
DR STRING; 1257021.D770_24395; -.
DR KEGG; fbt:D770_24395; -.
DR PATRIC; fig|1257021.3.peg.5530; -.
DR Proteomes; UP000064112; Chromosome.
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.
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:UP000064112};
KW Xylan degradation {ECO:0000313|EMBL:AHM63124.1}.
FT DOMAIN 25..372
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 374 AA; 41649 MW; 0A5DCEF59E9689D1 CRC64;
MLAVACLAAS CAGSGSERTS GQNSTAQTTT LKEALRDDFF IGAALNAGQV MGRDDKAATL
VKEQFNSISP ENSLKWGPIN PRPGVYNFEP ADAYVDFGEE NNMFVIGHTL VWHSQAPDWI
FEGTGGQPAT RDTLLQRMEN HIKVVAGRYK GRIDGWDVVN EALEDDGSMR QSKWYTLAGE
DFIEKAFEYA RVADPEAELY YNDYSLWKPE KRDGAVRLVR GLLDKGIKVD GIGMQGHYGV
DYPTLAQIEA SIEAFAALGV KVMVTELDID LLPNPTGRQG ADIVHTVEAQ EGFNPYAEGL
PDSVQQKLSK RYADIFALFH KHRDKISRVT FWGVADHHSW LNNWPMPGRT SYPMVFDRNY
QPKPAFHAIV EAVK
//
