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 27-MAR-2024, entry version 75.
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 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 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. {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=EED49069.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EQ963480; EED49069.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002380970.1; XM_002380929.1.
DR AlphaFoldDB; B8NKI4; -.
DR SMR; B8NKI4; -.
DR STRING; 332952.B8NKI4; -.
DR GlyCosmos; B8NKI4; 17 sites, No reported glycans.
DR VEuPathDB; FungiDB:AFLA_009378; -.
DR eggNOG; KOG0496; Eukaryota.
DR OrthoDB; 1032627at2759; -.
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; Beta-galactosidase, domain 2; 1.
DR Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 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:SF64; BETA-GALACTOSIDASE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF13364; BetaGal_ABD2; 2.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF13363; BetaGal_dom3; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1020
FT /note="Probable beta-galactosidase B"
FT /id="PRO_0000395224"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 307
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 372
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 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 785
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 819
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 919
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 270..323
FT /evidence="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
//
