ID A0A2H3BV38_9AGAR Unreviewed; 792 AA.
AC A0A2H3BV38;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
GN ORFNames=ARMSODRAFT_94104 {ECO:0000313|EMBL:PBK70842.1};
OS Armillaria solidipes.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=1076256 {ECO:0000313|EMBL:PBK70842.1, ECO:0000313|Proteomes:UP000218334};
RN [1] {ECO:0000313|Proteomes:UP000218334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-4 {ECO:0000313|Proteomes:UP000218334};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC Evidence={ECO:0000256|ARBA:ARBA00024574};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000256|ARBA:ARBA00004851}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; KZ293425; PBK70842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3BV38; -.
DR STRING; 1076256.A0A2H3BV38; -.
DR OrthoDB; 366914at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000218334; Unassembled WGS sequence.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR044993; BXL.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000218334};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..792
FT /note="xylan 1,4-beta-xylosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013628508"
FT DOMAIN 669..739
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 792 AA; 86025 MW; 19DDA61524C8C7DB CRC64;
MSITFTVAAL LLVTTARAAF PDCTNGVLKN NNVCNTSASP LDRATALISL FTIAEKLNNT
GNSSPGVPRI GLPPYQWWNE ALHGVAKSPG VQFTGSGDYS YATSFPQPIT MGAAFNDQLI
RDVGTVVSTE ARVFNNAGRA GLDFWTPNIN PFKDPRWGRG QETPGEDPYH LSSYVHALID
GLQGGYDPKY KRVVATCKHF AGYDIENWNG NFRYQFDAQI SSQDLAEYYM PSFQSCARDS
NVGSFMCSYN AVNGVPTCAD PYLLQTILRE HWGWTNEQQY VTSDCDAVQN IYIPHEYTAT
REEAVAAALI AGTDLDCGTY YQTYLPAAFE QGLFNESTLD QSLIRRYSAL VRLGYFDPPE
EQPYRQLSFD DVSTPEAQKL AYKAAVEGIV LLKNDGLLPL SLQNISSIAL IGSWANATQQ
MQGNYFGQAP YLHSPLYAAQ QLGVPINYAQ GVSGQGDPTT DNWLPVWTAA SKSDIIIFAD
GIDDSVESEG MDRVSISWTG AQLDMIEQLA SFGKPMIVLQ MGGGQIDSSP IKNNPNISAL
IWGGFPGQDG GVALIDIITG KAAPAGRLPV TQYPASYINE VPMTDMSLRP GPHSPGRTYK
WYNGTPIYDF GTGLHYTNFS ASITSSVMQN YDIAALTSNC TEKYLDRCSF LSSPFSVTVS
NTGTIASDYV ALAFLTGSFG PTPYPKKSLV AYQRLFDIAG GAVDTARLNL TLGSLARYDE
QGNRVLYPGD YAVVIDTAPL AMVNFTLTGE PRVLEEWPQP PGRRGGSGVE GLEGYFVGGY
GSGQGGEEQL LE
//
