GenomeNet

Database: UniProt
Entry: BGALB_ASPFU
LinkDB: BGALB_ASPFU
Original site: BGALB_ASPFU 
ID   BGALB_ASPFU             Reviewed;        1015 AA.
AC   Q4WRD3;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   16-JAN-2019, entry version 86.
DE   RecName: Full=Probable beta-galactosidase B;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase B;
DE   Flags: Precursor;
GN   Name=lacB; ORFNames=AFUA_1G16700;
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.
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.,
RA   Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
RA   Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
RA   Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
RA   Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
RA   Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
RA   Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
RA   Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
RA   Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
RA   Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
RA   Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
RA   Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   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.,
RA   Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
RA   Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
RA   White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
RA   Machida M., Hall N., 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.
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; AAHF01000004; EAL90999.1; -; Genomic_DNA.
DR   RefSeq; XP_753037.1; XM_747944.1.
DR   ProteinModelPortal; Q4WRD3; -.
DR   SMR; Q4WRD3; -.
DR   STRING; 5085.CADAFUBP00001576; -.
DR   EnsemblFungi; EAL90999; EAL90999; AFUA_1G16700.
DR   GeneID; 3510063; -.
DR   KEGG; afm:AFUA_1G16700; -.
DR   EuPathDB; FungiDB:Afu1g16700; -.
DR   HOGENOM; HOG000181922; -.
DR   InParanoid; Q4WRD3; -.
DR   KO; K01190; -.
DR   OMA; GHQSKII; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0005618; C:cell wall; IBA:GO_Central.
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; 2.60.120.260; -; 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; 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.
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     20       {ECO:0000255}.
FT   CHAIN        21   1015       Probable beta-galactosidase B.
FT                                /FTId=PRO_0000395225.
FT   ACT_SITE    196    196       Proton donor. {ECO:0000255}.
FT   ACT_SITE    308    308       Nucleophile. {ECO:0000255}.
FT   BINDING      90     90       Substrate. {ECO:0000250}.
FT   BINDING     135    135       Substrate. {ECO:0000250}.
FT   BINDING     136    136       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     137    137       Substrate. {ECO:0000250}.
FT   BINDING     195    195       Substrate. {ECO:0000250}.
FT   BINDING     265    265       Substrate. {ECO:0000250}.
FT   BINDING     373    373       Substrate. {ECO:0000250}.
FT   CARBOHYD     23     23       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     99     99       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    100    100       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    172    172       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    211    211       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    411    411       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    456    456       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    554    554       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    679    679       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    735    735       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    775    775       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    821    821       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    271    324       {ECO:0000250}.
SQ   SEQUENCE   1015 AA;  111681 MW;  D9EB8677F99A13A8 CRC64;
     MAHIYRLLLL LLSNLWFSTA AQNQSETEWP LHDNGLSKVV QWDHYSFQVN GQRIFIFSGE
     FHYWRIPVPE LWRDILEKVK ATGFTAFAFY SSWAYHAPNN STVDFSTGAR DITPIFELAK
     ELGMYMIVRP GPYVNAEASA GGFPLWLMTG EYGSLRNDDP RYTAAWTPYF ANMSQITSKY
     QVTDGHNTLV YQIENEYGQQ WIGDPKNRNP NKTAVAYMEL LEASARENGI TVPLTSNDPN
     MNSKSWGSDW SNAGGNVDVA GLDSYPSCWT CDVSQCTSTN GEYVPYKVID YYDYFQEVQP
     TLPSFMPEFQ GGSYNPWAGP EGGCPQDTSA EFANLFYRWN IGQRVTAMSL YMLYGGTNWG
     AIAAPVTATS YDYSAPISED RSIGAKYSET KLLALFTRTA KDLTMTEAIG NGTQYTTNTA
     VRAFELRNPQ TNAGFYVTFH TDTTVGGNQA FKLHVNTSVG ALTVPKNEGL IQLNGHQSKI
     IVTDFTLGKR TLLYSTAEVL TYAVFENRPT LVLWVPTGES GEFAIKGAKS GKVENGDGCS
     GIKFKREKDY LVVNFSQAKG LSVLRLDNGV RVVLLDKAAA YRFWAPALTD DPNVQETETV
     LVHGPYLVRS ASISKTTLAL RGDSVEKTTL EIFAPHSVRK ITWNGKEVQT SHTPYGSLKA
     TLAAPPDIKL PALTSWRSND SLPERLPSYD DSGPAWIEAN HMTTSNPSPP ATFPVLYADE
     YGFHNGVRLW RGYFNGSASG VFLNIQGGSA FGWSAWLNGH FLDSHLGTAT TSQANKTLTF
     PSSILNPTEN VLLIVHDDTG HDQTTGALNP RGILEARLLS NDTSSPPPEF THWRLAGTAG
     GESNLDPIRG VFNEDGLFAE RMGWHLPGFD DSAWTSENSA TSASSALSFT GATVRFFRSV
     VPLNIPAGLD VSISFVLSTP TAAPKGYRAQ LFVNGYQYGR YNPHIGNQVV FPVPPGILDY
     QGDNTIGLAV WAQTEEGAGI QVDWKVNYVA DSSLSVAGFG KGLRPGWTEE RLKFA
//
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