ID B6HIR6_PENRW Unreviewed; 791 AA.
AC B6HIR6;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
DE AltName: Full=1,4-beta-D-xylan xylohydrolase xlnD {ECO:0000256|ARBA:ARBA00041684};
DE AltName: Full=Beta-xylosidase A {ECO:0000256|ARBA:ARBA00042744};
DE AltName: Full=Beta-xylosidase xlnD {ECO:0000256|ARBA:ARBA00041545};
DE AltName: Full=Xylobiase xlnD {ECO:0000256|ARBA:ARBA00041508};
GN ORFNames=Pc21g23540 {ECO:0000313|EMBL:CAP97251.1}, PCH_Pc21g23540
GN {ECO:0000313|EMBL:CAP97251.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP97251.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP97251.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
CC -!- FUNCTION: Xylan 1,4-beta-xylosidase involved in the hydrolysis of
CC xylan, a major structural heterogeneous polysaccharide found in plant
CC biomass representing the second most abundant polysaccharide in the
CC biosphere, after cellulose. {ECO:0000256|ARBA:ARBA00025331}.
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; AM920436; CAP97251.1; -; Genomic_DNA.
DR RefSeq; XP_002569321.1; XM_002569275.1.
DR AlphaFoldDB; B6HIR6; -.
DR STRING; 500485.B6HIR6; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR GeneID; 8310226; -.
DR KEGG; pcs:Pc21g23540; -.
DR VEuPathDB; FungiDB:PCH_Pc21g23540; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_3_1; -.
DR OMA; TWNFVED; -.
DR OrthoDB; 366914at2759; -.
DR BioCyc; PCHR:PC21G23540-MONOMER; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000000724; Contig Pc00c21.
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:SF13; EXO-1,4-BETA-XYLOSIDASE XLND; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 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:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724};
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..791
FT /note="xylan 1,4-beta-xylosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002843657"
FT DOMAIN 693..763
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 791 AA; 85406 MW; ABFCA7FD7D2D6B12 CRC64;
MPAFPLLALL AFAPTALSQA NTSYADYNTQ AQPDLYPGTT AKVDFSFPDC SNGPLSKTMV
CDTTAKPHDR AAALIAMFTF EELVNSTGNV MPAIPRLGLP PYQVWNEALH GLDRANLTEF
GDYSWATSFP SPILTMAALN RTLINQIGGI VSTQGRAFNN GGRYGLDVYS PNINSFRHPV
WGRGQETPGE DIQLCSVYGL EYITGLQGGL DPKELKLAAT AKHFAGYDIE NWGNHSRLGN
DMSISAFDFA SYYAPQFVTA VRDARVHSVM ASYNAVNGVP ASANSFLLQT LLRDTWNFVE
DGYVSSDCDS VYNVFNPHGY ASSASLAAAK SIQAGTDIDC GATYQLYLNQ SFTQGEISRS
EIERAATRFY SNLVSLGYFD GDNSKYRDLD WSDVVATDAW NISYEAAVEG IVLLKNDGTL
PLSKDTHSVA LIGPWANVTT TMQGNYYGAA PYLTGPLAAL QASDLDVNYA FGTNISSETT
SGFEAALSAA RKSDVVIFAG GIDNSVEAEG VDRETITWPG NQLQLIEQLS ELGKPLVVLQ
MGGGQVDSSS LKANKNVNSL VWGGYPGQSG GPAILDILTG KRAPAGRLTV TQYPAEYALQ
FPATDMSLRP KGSNPGQTYM WYTGKPVYEF GHGLFYTTFE TSLANSHGAN NGASFDIVKL
LSRSNAGYNV IEQVPFMNYT IEVENTGTVT SDYTAMAFVN TKAGPSPHPN KWLVGFDRLG
GIEPHATQTM TIPVSLDNVA RTDEDGNRIV YPGKYELALN NERSAVLSFT LTGDATTIAT
WPKEEQLVPP S
//
