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Database: UniProt
Entry: BGALE_NEOFI
LinkDB: BGALE_NEOFI
Original site: BGALE_NEOFI 
ID   BGALE_NEOFI             Reviewed;        1011 AA.
AC   A1DJ58;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JAN-2019, entry version 77.
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=NFIA_000910;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC
OS   A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC       gangliosides, glycoproteins, and glycosaminoglycans.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000305}.
DR   EMBL; DS027697; EAW16747.1; -; Genomic_DNA.
DR   RefSeq; XP_001258644.1; XM_001258643.1.
DR   ProteinModelPortal; A1DJ58; -.
DR   SMR; A1DJ58; -.
DR   STRING; 36630.CADNFIAP00000075; -.
DR   PRIDE; A1DJ58; -.
DR   EnsemblFungi; EAW16747; EAW16747; NFIA_000910.
DR   GeneID; 4585646; -.
DR   KEGG; nfi:NFIA_000910; -.
DR   EuPathDB; FungiDB:NFIA_000910; -.
DR   HOGENOM; HOG000181922; -.
DR   OMA; IDAYPMR; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
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; Complete proteome; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20   1011       Probable beta-galactosidase E.
FT                                /FTId=PRO_0000395244.
FT   ACT_SITE    196    196       Proton donor. {ECO:0000255}.
FT   ACT_SITE    299    299       Nucleophile. {ECO:0000255}.
FT   BINDING      92     92       Substrate. {ECO:0000250}.
FT   BINDING     136    136       Substrate. {ECO:0000250}.
FT   BINDING     137    137       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     138    138       Substrate. {ECO:0000250}.
FT   BINDING     195    195       Substrate. {ECO:0000250}.
FT   BINDING     261    261       Substrate. {ECO:0000250}.
FT   BINDING     365    365       Substrate. {ECO:0000250}.
FT   CARBOHYD    202    202       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    406    406       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    423    423       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    455    455       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    588    588       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    622    622       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    704    704       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    745    745       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    759    759       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    772    772       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    778    778       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    913    913       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    267    316       {ECO:0000250}.
SQ   SEQUENCE   1011 AA;  111421 MW;  2E6518FE3F132FAC CRC64;
     MKFLLRRFIA LAAASSVVAA PSVSHLSLQD AANRRELLQD LVTWDQHSLF VRGERLMIFS
     GEFHPFRLPV PGLWFDVFQK ITSLGFNAVS FYTDWGLMEG NPGHVVTDGI WSLDEFFTAA
     SEAGIYLIAR PGPYINAETS AGGIPGWVLR LKGIIRSNSE DYLRATDTYM ATLGKIIAKA
     QITNGGPVIL VQPENEYTTW PNVSESEFPT TMNKEVMAYA EKQLRDAGVV VPTVVNDNKN
     LGYFAPGTGL GETDLYGIDA YPMRYDCGNP YVWPTYRFPR DWQHTHRNHS PTTPFAIMEF
     QGGSGDGWGG VTEDGCAILV NNEAVRVVYK NNYGFGVGVF NIYMTYGGTN WGNLGYHGGY
     TSYDYGAAIT EDRQIWREKY SEEKLQANFL KVSPAYLTAT PGNGVNGSYT GNKDIAVTPL
     FGNGTTTNFY LVRHADFTST GSVQYQLSVS TSVGNVTIPQ LGGSLSLNGR DSKFHVTDYD
     VGEFNLIYSS AEIFTWAKGD NKKRVLVLYG GAGELHEFAL PKHLPRPTVV DGSDVKMAKK
     GSAWVVQWEV TAQRRVLRAG KLEIHLLWRN DAYQHWVLEL PAKQPIANYS SPSKETVLVK
     GGYLLRSACI TNNKLHLTGD VNATTPLEVI SAPKRFDGIV FNGQSLKSTR SKIGNLAATV
     RYQPPAISLP DLKRLDWKYL DSLPEISPDY SDEGWMSLTN TYTNNTRKFT GPTCLYADDY
     GYHGGSLIYR GHFKANGDES WVFLNTSGGV GFANSVWLNQ TFLGSWTGSG NNMTYPRNIS
     LPHELSPGKP YVFTVVIDHM GQDEEAPGTD AIKFPRGILD YALSGHEVSD LKWKMTGNLG
     GEQYQDSTRG PLNEGAMYAE RRGYHLPNPP TSSWKSSSPI NDGLTGAGIG FYATSFSLDL
     PEGYDIPLSF LFNNSASDAR SGTSYRCQLF VNGYQFGKYV NDLGPQTNFP VPEGILNYNG
     VNYVAVSLWA LEPQGALVGG LELVASTPIL SAYRKPVPAP QPGWKPRRGA Y
//
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