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Database: UniProt
Entry: BGALB_NEOFI
LinkDB: BGALB_NEOFI
Original site: BGALB_NEOFI 
ID   BGALB_NEOFI             Reviewed;        1015 AA.
AC   A1D199;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   20-JUN-2018, entry version 71.
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=NFIA_008690;
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: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000305}.
DR   EMBL; DS027688; EAW22192.1; -; Genomic_DNA.
DR   RefSeq; XP_001264089.1; XM_001264088.1.
DR   ProteinModelPortal; A1D199; -.
DR   SMR; A1D199; -.
DR   STRING; 36630.CADNFIAP00001723; -.
DR   EnsemblFungi; EAW22192; EAW22192; NFIA_008690.
DR   GeneID; 4591479; -.
DR   KEGG; nfi:NFIA_008690; -.
DR   EuPathDB; FungiDB:NFIA_008690; -.
DR   HOGENOM; HOG000181922; -.
DR   OMA; DSYPSCW; -.
DR   OrthoDB; EOG092C0SLI; -.
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; -; 3.
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     21       {ECO:0000255}.
FT   CHAIN        22   1015       Probable beta-galactosidase B.
FT                                /FTId=PRO_0000395230.
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    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    441    441       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   CARBOHYD    878    878       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    271    324       {ECO:0000250}.
SQ   SEQUENCE   1015 AA;  111471 MW;  7BDC616E2D3A2DFF CRC64;
     MAHIYRLLLL LLSNLWFSAA AQNQSETEWP LHDNGLSKVV QWDHYSFQVN GQRIFIFSGE
     FHYWRIPVPE LWRDILEKVK ATGFTAFAFY SSWAYHAPNN RTVDFSTGAR DITPIFELAK
     ELGMYMIVRP GPYVNAEASA GGFPLWLTTG EYGSLRNDDP RYTAAWTPYF ANMSQITSKY
     QVTDGHNTLV YQIENEYGQQ WIGDPKDRNP NKTAVAYMEL LEASALENGI TVPLTSNDPN
     MNSKSWGSDW SNAGGNVDVA GLDSYPSCWT CDVSQCTSTN GEYVPYKVID YYDYFQEVQP
     TLPSFMPEFQ GGSYNPWAGP EGGCPQDTGA EFANLFYRWN IGQRVTAMSL YMLYGGTNWG
     AIAAPVTATS YDYSAPISED RSIGAKYSET KLLALFTRTA KDLTMTEAIG NGTQYTTNTA
     VRAFELRNPQ TNAGFYVTFH NDTTVGGNQA FKLHVNTSVG ALTVPKNEGV IQLNGHQSKI
     IVTDFTLGKR TLLYSTAEVL TYAVFENRPT LVLWVPTGES GEFAIKGTKS GKVENGDGCS
     GINFKREKDY LVVNFSQAKG LSVLRLDNGV RVVLLDKAAA YRFWAPALTD DPIVQETETV
     LVHGPYLVRS ASVSKSTLAL RGDSVEKTTL EIFAPHSVRK ITWNGKEVKT SQTPYGSLKA
     TLAAPPTIKL PALTSWRSND SLPERLPSYD DSGPAWIEAN HMTTSNPSPP ATLPVLYADE
     YGFHNGVRLW RGYFNGSASG VFLNIQGGSA FGWSAWLNGH FLDSHLGTAT TSQANKTLTF
     SSSILNPTEN VLLIVHDDTG HDQTTGALNP RGIIEARLLS NDTSSPAPGF TQWRIAGTAG
     GESNLDPIRG VFNEDGLFAE RMGWHLPGFD DSAWTPENST TSASSALSFT GATVRFFRTV
     VPLDIPAGLD VSISFVLSTP SAAPKGYRAQ LFVNGYQYGR YNPHIGNQVV FPVPPGILDY
     QGDNTIGLAV WAQTEEGAGI QVDWKVNYVA DSSLSVAGFG KGLRPGWTEE RLKFA
//
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