BGALE_ASPFU
ID BGALE_ASPFU Reviewed; 1011 AA.
AC Q4WG05;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable beta-galactosidase E;
DE EC=3.2.1.23;
DE AltName: Full=Lactase E;
DE Flags: Precursor;
GN Name=lacE; ORFNames=AFUA_3G00380;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
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.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR EMBL; AAHF01000010; EAL86322.1; -; Genomic_DNA.
DR RefSeq; XP_748360.1; XM_743267.1.
DR AlphaFoldDB; Q4WG05; -.
DR SMR; Q4WG05; -.
DR STRING; 746128.CADAFUBP00004709; -.
DR EnsemblFungi; EAL86322; EAL86322; AFUA_3G00380.
DR GeneID; 3505787; -.
DR KEGG; afm:AFUA_3G00380; -.
DR VEuPathDB; FungiDB:Afu3g00380; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_005732_2_0_1; -.
DR InParanoid; Q4WG05; -.
DR OMA; IDAYPMR; -.
DR OrthoDB; 179316at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.102.20.10; -; 1.
DR Gene3D; 2.60.390.10; -; 1.
DR InterPro; IPR018954; Betagal_dom2.
DR InterPro; IPR037110; Betagal_dom2_sf.
DR InterPro; IPR025972; BetaGal_dom3.
DR InterPro; IPR036833; BetaGal_dom3_sf.
DR InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421; PTHR23421; 1.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF13363; BetaGal_dom3; 1.
DR Pfam; PF13364; BetaGal_dom4_5; 2.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF117100; SSF117100; 1.
DR SUPFAM; SSF49785; SSF49785; 2.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1011
FT /note="Probable beta-galactosidase E"
FT /id="PRO_0000395243"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 299
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 913
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 267..316
FT /evidence="ECO:0000250"
SQ SEQUENCE 1011 AA; 111734 MW; 6312E4B521800294 CRC64;
MKSLLKRLIA LAAAYSVAAA PSFSHHSSQD AANKRELLQD LVTWDQHSLF VRGERLMIFS
GEFHPFRLPV PGLWFDVFQK IKSLGFNAVS FYTDWGLMEG NPGHVVTDGI WSLDEFFTAA
REAGLYLIAR PGPYINAETS AGGIPGWVLR RKGIIRSNSE DYLRATDTYM ATLGKIIAKA
QITNGGPVIL VQPENEYTTW PNVSESEFPT TMNQEVMAYA EKQLRDAGVV VPTVVNDNKN
LGYFAPGTGL GETDLYGIDA YPMRYDCGNP YVWPTYRFPR DWQHEHRNHS PTTPFAIMEF
QGGSGDGWGG VTEDGCAILV NNEAVRVVYK NNYGFGVRVF NIYMTYGGTN WGNLGYYGGY
TSYDYGAAIT EDRQIWREKY SEEKLQANFL KVSPAYLTST PGNGVNGSYT GNKDITVTPL
FGNGTTTNLY LVRHADFTST GSAQYNLSIS TSVGNVTIPQ LGGSLSLNGR DSKFHITDYD
VGGFNLIYSS AEVFTWAKGD NKKRVLVLYG GAGELHEFAL PKHLPRPTVV EGSYVKIAKQ
GSAWVVQWEV AAQRRVLRAG KLEIHLLWRN DAYQHWVLEL PAKQPIANYS SPSKETVIVK
GGYLLRSAWI TDNDLHLTGD VNVTTPLEVI SAPKRFDGIV FNGQSLKSTR SKIGNLAATV
HYQPPAISLP DLKRLDWKYI DSLPEISTEY NDEGWTPLTN TYTNNTREFT GPTCLYADDY
GYHGGSLIYR GHFTANGDES WVFLNTSGGV GFANSVWLNQ TFLGSWTGSG RNMTYPRNIS
LPHELSPGEP YVFTVVIDHM GQDEEAPGTD AIKFPRGILD YALSGHELSD LRWKMTGNLG
GEQYQDLTRG PLNEGAMYAE RQGYHLPSPP TSSWKSSNPI KEGLTGAGIG FYATSFSLDL
PEGYDIPLSF RFNNSASAAR SGTSYRCQLF VNGYQFGKYV NDLGPQTKFP VPEGILNYNG
VNYVAVSLWA LESQGALIGG LDLVASTPIL SGYRKPAPAP QPGWKPRRGA Y
