ID A0A137QGG8_9AGAR Unreviewed; 2013 AA.
AC A0A137QGG8;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
GN ORFNames=AN958_10192 {ECO:0000313|EMBL:KXN86330.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN86330.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN86330.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN86330.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; KQ962369; KXN86330.1; -; Genomic_DNA.
DR STRING; 1714833.A0A137QGG8; -.
DR OrthoDB; 366914at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000070249; 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 CDD; cd12809; Esterase_713_like-2; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 2.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR029058; AB_hydrolase.
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; 2.
DR Pfam; PF01915; Glyco_hydro_3_C; 2.
DR SMART; SM01217; Fn3_like; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 2.
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:UP000070249};
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..2013
FT /note="xylan 1,4-beta-xylosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007295326"
FT DOMAIN 672..744
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT DOMAIN 1517..1589
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 2013 AA; 218368 MW; 437EA2920330A99E CRC64;
MYSFIVTTLL VVANVATAQF NYSFPDCTSG PLKSTVVCDT SKNPATRARA LIQMFTDEEL
TQNTDNVSPG VPRLGVPSYQ WWSEALVCLL TCTIYLDIHE EQHGVAGSPG VSFAPSGEFS
SATSFPQPIV LGATFDMDLV KAIATVISTE ARAFNNAGRA GLDFFTPNIN PFKDPRWGRG
QETPGEDPFH VSQYVLHLID GLQGGIDPRP YFKIAADCKH FAAYDLDSWE GIDRFHFDAK
VSPQDLSEYY LPSFQSCVRD AKVASVMCSY NSVNGVPACA SPYLLQNVLR DFWGFDEDRW
VTSDCDAINN IFSTHNFTSS FAEAAADALK AGTDVDCGNT YSTSLPDALN QSLIVREDLE
KALARQYTSL MRQLTWSDVN TPDAQALAHS AAVEGLVLLK NDGLLPLKPK GEKVAIIGPY
VNATTNMQGN YFGTAPFIVT PFQGAVNAGF QVQSSPGTGI NDTSEAGFAA AISVAEGADI
IIFAGGIDNT IERESRDRLS VAWTGNQLEL IKQLASLGKP VIVVQFGGGQ TDDTELLSND
AVRAILWAGY PGQSGGTAIF DIITGSASPA GRLSITQYPT NFVDQVGMTD MSLRASDTNP
GRTYKWYSGT PVLEFGHGLH FTTFGFSWGK QPAAQYNIQQ LVRAGGKGFL DLATFDTFQV
RIRNTGNVTS DYVALLFLSG DGGPTPHPIK SLVSFTRAHG IKVGSSAVVN LKVTLGSVAR
VDERGDLWLF SGSYRLVLDI GDGVLTHDFV LTGTSTRIVQ WPQDPSFLSD SWPRLVAWFC
EPSHILLIPS FTCDSTVIRF PSAGDCPEIY PDRWADGPCK DTGCGAALIL AKPREYKTEG
WDCDEQETML VLLALLSTFL IKIGLAQFNF TFPDCTNGPL RSNVVCDTSK DPATRARTLI
QMFTDEELIL NTDNVSPGVP RLGIPPYQWW SEALHGVAGS PGVTFASSGN FSSATSFPQP
IVLGATFDMD LVKAAAIVTS TEARAFNNAG RAGLDFFTPN INPFKDPRWG RGQETPGEDP
FLVSQYVLNL IDGLQGGIDP RPYYKIAADC KHFAAYDLEN WEGINRSDFD AKVSLQDLSE
YYLPSFQSCV RDAKVASVMC SFNSVNGVPS CASSYLLQDV LRDFWGFNND RWVVADCDAI
ENIFSTHNFT SSLAEAAADA LKAGTDIDCG TTYSTHLPEA LEQSLITRAD LEKALTRQYT
SLMRVGYFDP PESQPYRQLD WSDVNKPDAQ ALAYRAAVEG LVLVKNDGVL PLPAQVKRLA
VIGPYANATT AMQGNYFGAA PVVITPVQGA IAAGFQVQVA HGTDIDGTSD AGFAQAIDIA
KSADTIVFAG GIDHTIEDEA KDRITITWTG NQLELVRQLS ALGKPVIVVQ FGGGQVDDSE
LLANDAVRAL IWAGYPGQSG GTAIFDIITG KVAPAGRLTT TQYPAEYIKQ VNMTDMSLRP
SPTSPGRTYK WYTGKPVVEF GHGLHFTTFQ FSWQKQPLMH YNIQQLIHGS GAEYLDLATL
DTFHILVKNT GKVSSDYVAL LFLSGDGGPS PRPLKSLVSF TRAHDIKAGS SAVVSLKVTL
GSVARADEQG DLWLFSGSYR LMLDLGDDVL THDFVLVGTS TRIVQWPRVP SLFDLNDALL
SSNVSFPPTL DVSNPPLGMK KAVVALLASF VLGAFGAQQQ VAGTLHRRSY FYAGGKYAAQ
GNSSIMEGAM YVERLTPERV TQPFPLLVVH GHAMTGTNFL NTPDGRQGWG DFFLSQGYEV
SIYTQGMPSS ESQVNLKGVY RGPTSPTFDT FTVESRFTAT QRFKLWPQAI LHTQWSGNGS
TGDDTFDSFY ASTVPSLVSD KETSEKMKEA GSALLDKIGP ITKPVILLTH SQSGPLGWVL
GDSRPNLIKT IVALEPMGPP FINVIFPPVA PARPFGVTEI SVAYEPPLSS PDDLKRVVAS
NSSLFTCFRQ AEPPRKLVNL MKIPILVITS EASYHAVYDG CTVDYLKQAG VGVDHINLGN
VGIHGNAHMM FMEKNNIEIA ELIQKWIINN VDN
//