BGAL_ASPNG
ID BGAL_ASPNG Reviewed; 1006 AA.
AC P29853;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Beta-galactosidase;
DE EC=3.2.1.23;
DE AltName: Full=Lactase-N;
DE Short=Lactase;
DE AltName: INN=Tilactase;
DE Flags: Precursor;
GN Name=lacA;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=VTT D-80144;
RX PubMed=1368193; DOI=10.1038/nbt0192-82;
RA Kumar V., Ramakrishnan S., Teeri T.T., Knowles J.K., Hartley B.S.;
RT "Saccharomyces cerevisiae cells secreting an Aspergillus niger beta-
RT galactosidase grow on whey permeate.";
RL Biotechnology (N.Y.) 10:82-85(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PHARMACEUTICAL USE.
RC STRAIN=VTT D-80144;
RA Hartley B.S., Ramakrishnan S., Kumar V.;
RT "DNA construct and modified yeast.";
RL Patent number WO9010703, 20-SEP-1990.
CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans.
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 -!- PHARMACEUTICAL: Capable of effecting hydrolysis of lactose in situ in
CC the gastrointestinal tract of lactase-deficient subjects when given as
CC replacement therapy at mealtime.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L06037; AAA32696.1; -; Genomic_DNA.
DR EMBL; S37150; AAC60538.1; -; mRNA.
DR EMBL; A00968; CAA00105.1; -; Unassigned_DNA.
DR PIR; T31685; T31685.
DR AlphaFoldDB; P29853; -.
DR SMR; P29853; -.
DR STRING; 5061.CADANGAP00001173; -.
DR BindingDB; P29853; -.
DR ChEMBL; CHEMBL4753; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR CLAE; LAC35A_ASPNG; -.
DR VEuPathDB; FungiDB:An01g12150; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1162768; -.
DR VEuPathDB; FungiDB:ATCC64974_13640; -.
DR VEuPathDB; FungiDB:M747DRAFT_325279; -.
DR eggNOG; KOG0496; Eukaryota.
DR BioCyc; MetaCyc:MON-16612; -.
DR BRENDA; 3.2.1.23; 518.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421; PTHR23421; 2.
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.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosidase; Hydrolase; Pharmaceutical; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1006
FT /note="Beta-galactosidase"
FT /id="PRO_0000012192"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 739
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 206
FT /note="S -> C (in Ref. 2; CAA00105)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1006 AA; 109161 MW; 7157B28A83805488 CRC64;
MKLSSACAIA LLAAQAAGAS IKHRINGFTL TEHSDPAKRE LLQKYVTWDD KSLFINGERI
MIFSGEFHPF RLPVKELQLD IFQKVKALGF NCVSFYVDWA LVEGKPGEYR ADGIFDLEPF
FDAASEAGIY LLARPGPYIN AESSGGGFPG WLQRVNGTLR SSDKAYLDAT DNYVSHVAAT
IAKYQITNGG PIILYQPENE YTSGCSGVEF PDPVYMQYVE DQARNAGVVI PLINNDASAS
GNNAPGTGKG AVDIYGHDSY PLGFDCANPT VWPSGDLPTN FRTLHLEQSP TTPYAIVEFQ
GGSYDPWGGP GFAACSELLN NEFERVFYKN DFSFQIAIMN LYMIFGGTNW GNLGYPNGYT
SYDYGSAVTE SRNITREKYS ELKLLGNFAK VSPGYLTASP GNLTTSGYAD TTDLTVTPLL
GNSTGSFFVV RHSDYSSEES TSYKLRLPTS AGSVTIPQLG GTLTLNGRDS KIHVTDHNVS
GTNIIYSTAE VFTWKKFADG KVLVLYGGAG EHHELAISTK SNVTVIEGSE SGISSKQTSS
SVVVGWDVST TRRIIQVGDL KILLLDRNSA YNYWVPQLAT DGTSPGFSTP EKVASSIIVK
AGYLVRTAYL KGSGLYLTAD FNATTSVEVI GVPSTAKNLF INGDKTSHTV DKNGIWSATV
DYNAPDISLP SLKDLDWKYV DTLPEIQSSY DDSLWPAADL KQTKNTLRSL TTPTSLYSSD
YGFHTGYLLY RGHFTATGNE STFAIDTQGG SAFGSSVWLN GTYLGSWTGL YANSDYNATY
NLPQLQAGKT YVITVVIDNM GLEENWTVGE DLMKSPRGIS TSCLPDGQAA PISWKLTGNL
GGEDYEDKVR GPLNEGGLYA ERQGFHQPEP PSQNWKSSSP LEGLSEAGIG FYSASFDLDL
PKDGMSHCSS TSVTALRHPR TACRSTSTDI VCEIHKQHRT SDQLPCPRGN PELSRNELVG
GDPVALDSAG GKLESLELSY TTPVLTALGE VESVDQPKYK KRKGAY
