GenomeNet

Database: UniProt
Entry: BGALB_ASPOR
LinkDB: BGALB_ASPOR
Original site: BGALB_ASPOR 
ID   BGALB_ASPOR             Reviewed;        1022 AA.
AC   Q2U6P1;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   16-JAN-2019, entry version 76.
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=AO090120000158;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G.,
RA   Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K.,
RA   Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W.,
RA   Galagan J.E., Nierman W.C., Yu J., Archer D.B., Bennett J.W.,
RA   Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H.,
RA   Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R.,
RA   Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N.,
RA   Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I.,
RA   Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y.,
RA   Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y.,
RA   Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K.,
RA   Kuhara S., Ogasawara N., Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE62774.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AP007166; BAE62774.1; ALT_SEQ; Genomic_DNA.
DR   ProteinModelPortal; Q2U6P1; -.
DR   SMR; Q2U6P1; -.
DR   Allergome; 1261; Asp o Lactase.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PRIDE; Q2U6P1; -.
DR   HOGENOM; HOG000181922; -.
DR   Proteomes; UP000006564; Chromosome 5.
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   1022       Probable beta-galactosidase B.
FT                                /FTId=PRO_0000395226.
FT   ACT_SITE    196    196       Proton donor. {ECO:0000255}.
FT   ACT_SITE    309    309       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     374    374       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    412    412       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    457    457       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    551    551       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    598    598       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    627    627       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    704    704       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    749    749       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    787    787       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    821    821       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    882    882       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    921    921       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    270    325       {ECO:0000250}.
SQ   SEQUENCE   1022 AA;  112493 MW;  E18455942DAA8A62 CRC64;
     MLISKTVLSG LALGASFVGV SAQQNSTRWP LHDNGLTDTV EWDHYSFLIN GQRHFVFSGE
     FHYWRIPVPE LWRDLLEKIK AAGFTAFSIY NHWGYHSPKP GVLDFENGAH NFTSIMTLAK
     EIGLYMIIRP GPYVNAEANA GGLPLWTTTG AYGKLRDNDP RYLEALTPYW ANISKIIAPH
     LITNDGNVIL YQIENEYAEQ WLDEETHEPN TSGQEYMQYL EDVARENGID APLIHNLPNM
     NGHSWSKDLS NATGNVDVIG VDSYPTCWTC NVSECASTNG EYIPYLKLTY PQISYFKELS
     PTQPSFMPEF QGGSYNPWGG PQGGCPDDLG PDFANLFYRN LISQRVSAIS LYMLYGGTNW
     GWHASTDVAT SYDYSSPISE NRKLIEKYYE TKVLTQFTKI AQDLSKVDRL GNSTKYSSNP
     AVSVAELRNP DTGAAFYVTQ HEYTPSGTVE KFTVKVNTSE GALTIPQYGS QITLNGHQSK
     IIVTDFKFGS KTLLYSTAEV LTYAVIDGKE VLALWVPTGE SGEFTVKGVN SAKFADKGRT
     ANIEIHPGTN NVTVSFMQRS GMSLVELGDG TRIVLLDRSA AHVFWSTPLN NDPAEAGNNT
     VLVHGPYLVR SAKLEGCDLK LTGDIQNSTE VSIFAPKSVC SVNWNGKKTS VKSAKGGVIT
     TTLGGDAKFE LPTISGWKSA DSLPEIAKDY SATSKAWVVA TKTNSSNPTP PAPNNPVLYV
     DENDIHVGNH IYRATFPSTD EPPTDVYLNI TGGRAFGYSV WLNSDFIGSW LGTATTEQND
     QTFSFSNATL STDEDNILVV VMDNSAHDLR DGALNPRGIT NATLIGPGSY SFTEWKLAGN
     AGFEDHLDPV RAPLNEGSLY AERVGIHLPG YEFDEAEEVS SNSTSLTVPG AGIRVFRTVV
     PLSVPQGLDV SISFRLTAPS NVTFTSAEGY TNQLRALLFV NGYQYGRFNP YIGHQIDFPV
     PPGVLDYNGD NTIAVTVWSQ SVDGAEIKVD WNVDYVHETS FDMNFDGAYL RPGWIEERRE
     YA
//
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