ID A0A0C1R701_9CYAN Unreviewed; 391 AA.
AC A0A0C1R701;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-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=DA73_0204345 {ECO:0000313|EMBL:KIE13399.1}, DA73_0400024870
GN {ECO:0000313|EMBL:KAF3888361.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE13399.1};
RN [1] {ECO:0000313|EMBL:KIE13399.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE13399.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
RN [2] {ECO:0000313|EMBL:KAF3888361.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KAF3888361.1};
RA Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA Tripathy S.;
RT "Improved Assembly of Tolypothrix boutellei genome.";
RL Submitted (NOV-2019) 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:KIE13399.1}.
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DR EMBL; JHEG04000001; KAF3888361.1; -; Genomic_DNA.
DR EMBL; JHEG02000019; KIE13399.1; -; Genomic_DNA.
DR RefSeq; WP_038089927.1; NZ_JHEG04000001.1.
DR AlphaFoldDB; A0A0C1R701; -.
DR STRING; 1479485.DA73_0204345; -.
DR OrthoDB; 9809277at2; -.
DR Proteomes; UP000029738; Unassembled WGS sequence.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
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:UP000029738};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 73..384
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 301
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 391 AA; 44104 MW; B817A1C8B3C29FBA CRC64;
MFNNSPLRRR HFLYLGLSGL AGGVAVGARK QMYRVQQTQQ TRALDHPKRE FTVVGQAPLK
KRAVAKGLIY GAAATQYDLA SDAKFTASFV QQCGILVPDL DLKWDALRPA PDKFDFTKAD
WLTEFAQRNS MLFRGHTLVW EQALPKWFKE TVSPQNAERF LIEHINTVVK RYAGKMHSWD
VVNEAVAKSL SDRSDGLSVN PWLSFLDKNY IDLSFRVAAQ ADPTALLVYN DRWLDYDTPR
DSGQRLAVLK LLEHLKSIGT PVHALGIQAH LNGAETRFNA TKLRNFLKDV ASLGLKILIT
ELDVSDRELP SAPAVRDRIV AAAYEDYLSV VLDERVVIAV LTWQLSDRYT WLSMYPRSDA
ALVRPLPLSS NLEPKLAWNA IARAFDNAPK R
//
