ID A0A067TMH7_GALM3 Unreviewed; 768 AA.
AC A0A067TMH7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 22-FEB-2023, entry version 26.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
GN ORFNames=GALMADRAFT_649372 {ECO:0000313|EMBL:KDR83517.1};
OS Galerina marginata (strain CBS 339.88).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Galerina.
OX NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR83517.1, ECO:0000313|Proteomes:UP000027222};
RN [1] {ECO:0000313|Proteomes:UP000027222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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; KL142368; KDR83517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067TMH7; -.
DR STRING; 685588.A0A067TMH7; -.
DR HOGENOM; CLU_004542_5_3_1; -.
DR OrthoDB; 366914at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000027222; 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:UP000027222};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..768
FT /note="xylan 1,4-beta-xylosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001649165"
FT DOMAIN 673..743
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 768 AA; 82161 MW; 053F2B2C1410007C CRC64;
MINLQVGAVA LSIVVVHLLQ GAAALTYTFP DCTVAPLKGN GVCDTTKDAT TRARAIVELF
TVEELMANTV NLSPGVSRLG LPSYQWWSEA LHGVAGSPGV TFAASGNFSF ATSFPQPILL
GAAFDDDLIK EVAITVSTEA RAFNNAGRAG LDFFTPNINP FKDPRWGRGQ ETPGEDPFHI
SQYVFNLIQG LQGGIDPKPY FKVIADCKHF AAYDLENWEG NNRMAFNAVV TQQDLSEFYL
PPFQSCVRDA KVASVMCSYN SVNGIPSCAN SFLLQSVLRD YWGFNDDGRW VTSDCDAVDN
IFSTHNFTSD YAHAVADALK AGTDVDCGNA YAAHLPDAFN QSLITRPDLE KALVRQYSSL
VRLGYFDSPK VQPFRQLDWS NVNTPAAQVL AHQAAVEGIV LLKNDGTLPF KKSIKNIAFI
GPWANATTQM QGNYQGVAPF LVSPVQGAVN AGFTATITLG TTISGTSTTG FASALAAAKA
ADAIVFGGGI DESIEREGMD RINITWPGVQ LDLISQLGAL GKPLVVVQFG GGQVDGTALK
NNAQVNSILW AGYPGQSGGT ALAEIISGKA APAGRLTTTQ YPASFTSQVG MTDMTIRPSS
SNPGRTYKWF TGTPVFEFGH GLHFTTFALT WQHQLATVYQ IPRVQTGKGN VDLNVFDTFN
VVVKNTGKVT SDYVALLFLS GSGGPSPLPN KQLVSYTRLH QVKAGGQDVA SLKVTLGSVA
RADARGNLWL YSGSYELTVD TGAQASLTHR FILVGDAVQI SKFPQNSS
//