BGALA_ASPPH
ID BGALA_ASPPH Reviewed; 1007 AA.
AC Q4ZHV7;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Probable beta-galactosidase A;
DE EC=3.2.1.23;
DE AltName: Full=Lactase A;
DE Flags: Precursor;
GN Name=lacA;
OS Aspergillus phoenicis (Aspergillus saitoi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=5063;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AS.3.3143;
RA Wang W.K., Dong Z.Y., Mao A.J.;
RT "The cDNA sequence of beta-galactosidase from Aspergillus phoenicis.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; DQ008057; AAY21925.1; -; mRNA.
DR AlphaFoldDB; Q4ZHV7; -.
DR SMR; Q4ZHV7; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
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; IPR019801; Glyco_hydro_35_CS.
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.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1007
FT /note="Probable beta-galactosidase A"
FT /id="PRO_0000395219"
FT REGION 862..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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 CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 205..206
FT /evidence="ECO:0000250"
FT DISULFID 266..315
FT /evidence="ECO:0000250"
SQ SEQUENCE 1007 AA; 109682 MW; D724DF7B1CDE94C3 CRC64;
MKLSSACAIA LLAAQAAGAS IKHRINGFTL TEHSDPAKRE LLQKYVTWDD KSLFINGERI
MIFSGEFHPF RLPVKELQLD IFQKVKALGF NCVSFYVDWA LVEGEPGEYR ADGIFDLEPF
FDAASEAGIY LLARPGPYIN AESSGGGFPG WLQRVNGTLR SSDKAYLDAT DNYVSHVAAT
IAKYQITNGG PIILYQPENE YTSGCCGVEF PDPVYMQYVE DQARNAGVVI PLINNDASAS
GNNAPGTGKG AVDIYGHDSY PLGFDCANPT VWPSGDLPTN FRTLHLEQSP TTPYAIVEFQ
GGSYDPWGGP GFAACSELLN NEFERVSYKN DFSFQIAIMN LYMIFGGTNW GNLGYPNGYT
SYDYGSAVTE SRNITREKYS ELKLLGNFAK VSPGYLTASP GNLTTSGYAD TTDLTVTPLL
GNSTGSFFVV RHSDYSSEES TSYKLRLPTS ASSVTIPQLG GTLTLNGRDS KIHVTDYNVS
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 YVITVVINNM GLEENWTVGE DLMKTPRGIL NFLLAGRPSS AISWKLTGNL
GGEDYEDKVR GPLNEGGLYA ERQGFHQPEP PSQDWKSSSP LEGLSEAGIG FYSASFDLDL
PKGWDVPLFL NIGNSTTPSP YRVQVYVNGY QYAKYISNIG PQTSFPVPEG ILNYRGTNWL
AVTLWALDSA GGKLESLELS YTTPVLTALG EVESVDQPKY KKRKGAY
