GenomeNet

Database: UniProt
Entry: BGALB_ASPFN
LinkDB: BGALB_ASPFN
Original site: BGALB_ASPFN 
ID   BGALB_ASPFN             Reviewed;        1020 AA.
AC   B8NKI4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   16-JAN-2019, entry version 56.
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=AFLA_091500;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM
OS   12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167;
RX   PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EED49069.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; EQ963480; EED49069.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002380970.1; XM_002380929.1.
DR   ProteinModelPortal; B8NKI4; -.
DR   SMR; B8NKI4; -.
DR   GeneID; 7920299; -.
DR   KEGG; afv:AFLA_091500; -.
DR   EuPathDB; FungiDB:AFLA_091500; -.
DR   HOGENOM; HOG000181922; -.
DR   Proteomes; UP000001875; 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; 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     22       {ECO:0000255}.
FT   CHAIN        23   1020       Probable beta-galactosidase B.
FT                                /FTId=PRO_0000395224.
FT   ACT_SITE    196    196       Proton donor. {ECO:0000255}.
FT   ACT_SITE    307    307       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     264    264       Substrate. {ECO:0000250}.
FT   BINDING     372    372       Substrate. {ECO:0000250}.
FT   CARBOHYD     25     25       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    111    111       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    172    172       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    210    210       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    251    251       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    271    271       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    410    410       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    455    455       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    549    549       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    596    596       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    625    625       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    702    702       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    747    747       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    785    785       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    819    819       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    880    880       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    919    919       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    270    323       {ECO:0000250}.
SQ   SEQUENCE   1020 AA;  112288 MW;  353EB4A96CBFBF8C CRC64;
     MLISKTVLSG LALGASFVGV SAQQNSTRWP LHDNGLTDTV EWDHYSFLIN GQRHFVFSGE
     FHYWRIPVPE LWRDLLEKIK AAGFTAFSIY NHWGYHSPKP GVLDFENGAH NFTSIMTLAK
     EIGLYMIIRP GPYVNAEANA GGLPLWTTTG AYGKLRDNDP RYLEALTPYW ANISKIIAPH
     LITNGGNVIL YQIENEYAEQ WLDEETHEPN TSGQEYMQYL EDVARENGID APLIHNLPNM
     NGHSWSKDLS NATGNVDVIG VDSYPTCWTC NVSECASTNG EYIPYKTLIY YDYFKELSPT
     QPSFMPEFQG GSYNPWGGPQ GGCPDDLGPD FANLFYRNLI SQRVSAISLY MLYGGTNWGW
     HASTDVATSY DYSSPISENR KLIEKYYETK VLTQFTKIAQ DLSKVDRLGN STKYSSNPAV
     SVAELRNPDT GAAFYVTQHE YTPSGTVEKF TVKVNTSEGA LTIPQYGSQI TLNGHQSKII
     VTDFKFGSKT LLYSTAEVLT YAVIDGKEVL ALWVPTGESG EFTVKGVNSA KFADKGRTAN
     IEIHPGANNV TVSFMQRSGM SLVELGDGTR IVLLDRSAAH VFWSTPLNND PAEAGNNTVL
     VHGPYLVRSA KLEGCDLKLT GDIQNSTEVS IFAPKSVCSV NWNGKKTSVK SAKGGVITTT
     LGGDAKFELP TISGWKSADS LPEIAKDYSA TSKAWVVATK TNSSNPTPPA PNNPVLYVDE
     NDIHVGNHIY RATFPSTDEP PTDVYLNITG GRAFSYSVWL NSDFIGSWLG TATTEQNDQT
     FSFSNATLST DEDNILVVVM DNSAHDLRDG ALNPRGITNA TLIGPGSYSF TEWKLAGNAG
     FEDHLDPVRA PLNEGSLYAE RVGIHLPGYE FDEAEEVSSN STSLTVPGAG IRVFRTVVPL
     SVPQGLDVSI SFRLTAPSNV TFTSAEGYTN QLRALLFVNG YQYGRFNPYI GHQIDFPVPP
     GVLDYNGDNT IAVTVWSQSV DGAEIKVDWN VDYVHETSFD MNFDGAYLRP GWIEERREYA
//
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