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 03-AUG-2022, 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=AO090120000158;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
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., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA 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. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE62774.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP007166; BAE62774.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q2U6P1; -.
DR SMR; Q2U6P1; -.
DR STRING; 510516.Q2U6P1; -.
DR Allergome; 1261; Asp o Lactase.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
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; 2.60.390.10; -; 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; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1022
FT /note="Probable beta-galactosidase B"
FT /id="PRO_0000395226"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 309
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 270..325
FT /evidence="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
