ID F6FTN6_ISOV2 Unreviewed; 425 AA.
AC F6FTN6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN OrderedLocusNames=Isova_1396 {ECO:0000313|EMBL:AEG44163.1};
OS Isoptericola variabilis (strain 225).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236};
RN [1] {ECO:0000313|EMBL:AEG44163.1, ECO:0000313|Proteomes:UP000009236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=225 {ECO:0000313|Proteomes:UP000009236};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Siebers A., Allgaier M., Thelen M.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Isoptericola variabilis 225.";
RL Submitted (MAY-2011) 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; CP002810; AEG44163.1; -; Genomic_DNA.
DR AlphaFoldDB; F6FTN6; -.
DR STRING; 743718.Isova_1396; -.
DR KEGG; iva:Isova_1396; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_640435_0_0_11; -.
DR Proteomes; UP000009236; Chromosome.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide 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};
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:UP000009236}.
FT DOMAIN 67..368
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
SQ SEQUENCE 425 AA; 48002 MW; 24F60DEF404D0955 CRC64;
MPVTLFTAPV DHTPDLTLAH RRADAVVTVL GADGTPLDDT EVVVEQTRHA FGFGCIGFDL
VDLANGTSAD PDYDNVFAER WLDVFNTTTL PFYWGTFEPE EQGKPRTAEL QAAAWWFADR
GVAVKGHPLV WHTVQPRWLL GRPLEEVERL QRERIRRDVA DFAGVIDTWD AINEVVIMPV
FTAEENAITP LARVKGRVEM IRMAFEEARA ANPHATLLLN DFDMSTAYEC LIEAVLEAGI
RIDYLGLQSH MHQGYWGEEK TLRILERFSR YGIPIHFTET TLLSGDLMPP EIVDLNDYQV
ETWPSTPEGE ERQADEVERH YRTLLSHPAV EAATYWGLSD RGMWLGAPGG LLRADGSPKP
AYERLRRLVK EEWWLPPTRL RTDEAGRVRV EGFRGDYRVS LPDGGASAEF GLTESGERTL
TLTTR
//