ID Q4WL73_ASPFU Unreviewed; 513 AA.
AC Q4WL73;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE SubName: Full=Xylosidase/arabinosidase, putative {ECO:0000313|EMBL:EAL89291.1};
DE EC=3.2.1.- {ECO:0000313|EMBL:EAL89291.1};
GN ORFNames=AFUA_6G14550 {ECO:0000313|EMBL:EAL89291.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL89291.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL89291.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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:EAL89291.1}.
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DR EMBL; AAHF01000006; EAL89291.1; -; Genomic_DNA.
DR RefSeq; XP_751329.1; XM_746236.1.
DR AlphaFoldDB; Q4WL73; -.
DR EnsemblFungi; EAL89291; EAL89291; AFUA_6G14550.
DR GeneID; 3508646; -.
DR KEGG; afm:AFUA_6G14550; -.
DR VEuPathDB; FungiDB:Afu6g14550; -.
DR eggNOG; ENOG502SHCU; Eukaryota.
DR HOGENOM; CLU_016508_0_0_1; -.
DR InParanoid; Q4WL73; -.
DR OMA; GTHEGHM; -.
DR OrthoDB; 1891044at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
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; cd18617; GH43_XynB-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:UP000002530}.
FT DOMAIN 328..504
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 194
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 140
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 513 AA; 57358 MW; 946DC20EB92270FE CRC64;
MSPINPIIPG FAPDPSVVKV GEWFFLINSS FHLFPGLPIY ASQDLVSWRH IGNAINRQSQ
LSLSRSKTEL HPLPTGEVLV ATGGLYAPTI RYHDGTFYVV CTNVVRTVTG DSTQNFIISS
KDIWADSWSD PVYFEFDGID PSLFFDDDGK TYIQGSAAPG PFTTINMFEI DLGSGRKLSE
ERTIWRGTGG IYPEGPHLYK QKGYYYVVIA EGGTHEGHMV TMARSTNIWG PYEGCPDNPV
LTARDTDEYI QYTGHCDVFQ DDRDQWWCTC LGVRKDKNGR YVMGRETFLT QGRWDGDWLS
LDQVKPMPSG LLSRGEGKKL VANPSVDYVY IRDAILSNYT LPSSASDGLT LTASSADLSH
PQKSPSFIGK RQRHLDGCSG VELDIVEATW MATKLRAGMA CYKDEHRFLR IYYDATELAI
VTETINKPKG ICRQERLTLE SLPKSIAFRI QYTEQEYRLF HTVGNAGQAN WKCVSTIDTL
NLTGPDFTGP VIGVFAVAES TDTEVRFRNL TIC
//
