ID A0A0F8ULN1_9EURO Unreviewed; 542 AA.
AC A0A0F8ULN1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:KKK20524.1};
GN ORFNames=ARAM_001112 {ECO:0000313|EMBL:KKK20524.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK20524.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK20524.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK20524.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:KKK20524.1}.
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DR EMBL; JZBS01002007; KKK20524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8ULN1; -.
DR STRING; 308745.A0A0F8ULN1; -.
DR OrthoDB; 1891044at2759; -.
DR Proteomes; UP000034291; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd09000; GH43_SXA-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT DOMAIN 327..527
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 15
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 128
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 542 AA; 61410 MW; F3C345FCB9121059 CRC64;
MPPVRNPILP GFNPDPSIIR VGDDYYIATS TFEWYPGVQI HHSRDLANWE LVVRPLNRKS
QLDLRGVPDS CGVWAPCLSY DGDRFWLVYT YMTRKDGSFK DSHNYIVNAP SIQGPWSEPV
YANSSGFDPS LFHDDDGRKW FVNMLWDHRG RSRNFAGIAL QEFDYKAGKL VGPRKNIFQG
TELDLVEGPH LYRRHGWYYL LTAEGGTGYD HACTLARSRD IWGPYEIHPQ KHIVTSKDTP
FTALQRAGHG DIVESPEGKC YLVHLTGRPV GQNRRCVLGR ETAIQEAYWG EDDWLYIQNG
PAPSLHVDLP AARDDTNYWA QQHYTFENSL HKDFQWLRTP ETDRIFVVSE GKLILTGRES
IGSWFEQALI ARRQTHFSFD AETTVEFSPA DERQFAGLVV YYCRYNFFYL TVTAQSDGQR
EINIMSSEAS YPEGKLQMPA PEHISIPNGG RVRLAASIRG GLTLQFFYAL EGQELQKVGP
VFDASIVSDE CGGHQSHGSF TGAFVGVACS DLNGTAIQAK FDSFTYRPVE DAADRYEITT
TH
//
