ID R9PH24_AGAAL Unreviewed; 374 AA.
AC R9PH24;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=AALB_0722 {ECO:0000313|EMBL:GAD00642.1};
OS Agarivorans albus MKT 106.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Agarivorans.
OX NCBI_TaxID=1331007 {ECO:0000313|EMBL:GAD00642.1, ECO:0000313|Proteomes:UP000014461};
RN [1] {ECO:0000313|EMBL:GAD00642.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yasuike M., Nakamura Y., Kai W., Fujiwara A., Fukui Y., Satomi M., Sano M.;
RT "Draft Genome Sequence of Agarivorans albus Strain MKT 106T, an Agarolytic
RT Marine Bacterium.";
RL Genome Announc. 1:e00367-13(2013).
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:GAD00642.1}.
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DR EMBL; BARX01000003; GAD00642.1; -; Genomic_DNA.
DR AlphaFoldDB; R9PH24; -.
DR STRING; 1331007.AALB_0722; -.
DR Proteomes; UP000014461; 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 Reference proteome {ECO:0000313|Proteomes:UP000014461};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:GAD00642.1}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..374
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004487864"
FT DOMAIN 63..372
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 286
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 374 AA; 41428 MW; 2F18A61FFDCE2032 CRC64;
MRVLPLALLS TAISIGLSAC GGSSSDSGEP IEVPQVESLK ALSTTYMGAA VPAGYEDQFS
NGIETRPELQ DVVIQHFDQI TAENIMKSAY IQPRQGDFTF QDADNLVDWA LDNNITMHAH
ALVWHSQMPS WMENYQGDWL TMMDTHVSTV ADHFKGRVVS WDVVNEAFND NNDNGYATYR
DTDANSGGHG SPWYQNLGKD YIPEAFKMAH AADSGAELYY NDYNIEDDGA KLASVLRMAD
ELLADDIPID GIGFQMHVNY DWPSAQAIGT SFAKVVAKGL KVKVTELDIK MNPNGDRNTF
TTAMAEEQKL RYQEIIKAYY DNVPANLRGG ITVWGVSDAD SWIPHFTGHN DWPLLFNSSL
EQKPAIEGVA NELK
//
