ID A0A1S9DBF7_ASPOZ Unreviewed; 846 AA.
AC A0A1S9DBF7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN ORFNames=OAory_01020740 {ECO:0000313|EMBL:OOO06413.1};
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO06413.1, ECO:0000313|Proteomes:UP000190312};
RN [1] {ECO:0000313|EMBL:OOO06413.1, ECO:0000313|Proteomes:UP000190312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC7051 {ECO:0000313|EMBL:OOO06413.1,
RC ECO:0000313|Proteomes:UP000190312};
RA Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA Jeennor S., Laoteng K.;
RT "Genome sequencing of Aspergillus oryzae BCC7051.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans.
CC {ECO:0000256|ARBA:ARBA00002691}.
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 Evidence={ECO:0000256|ARBA:ARBA00001412,
CC ECO:0000256|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OOO06413.1}.
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DR EMBL; MKZY01000008; OOO06413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9DBF7; -.
DR VEuPathDB; FungiDB:AO090701000770; -.
DR eggNOG; KOG0496; Eukaryota.
DR Proteomes; UP000190312; Unassembled WGS sequence.
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; Beta-galactosidase, domain 2; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
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; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 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.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Reference proteome {ECO:0000313|Proteomes:UP000190312};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..846
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012661878"
FT DOMAIN 391..541
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 846 AA; 93818 MW; 39D05EA4C78EDA3E CRC64;
MMLPWHLFCM LLLFTRHVFS AEDPEKPLQD IVTWDEYSIL VRGERILFFS GEFHPFRLPS
PGLWLDVFQK IRALGYSGVS FYLMWGLLEG EPGHVRTEGV FSLDGFFNAA SQAGIYLLAR
PGPYINAEVS GGGFPSWVQR IEGSVRTTDP TFLNATKNYI STIGEIISKV QITNGGPVIL
FQLENEYSIC EGAPSHEELN FCLEKDYMAA IEQQFRDAEI VVPFVNNDAV ALGDWAPGTG
QGAIDIYGFD NYPFGWGNGY ASPENWTQIT DPLTQYNFSQ HQSMSPGTPF SIIEFQGGAP
DPWGGTGADV CAEMVSNIFA RVFYKINYDF RITIFNLYMM LGGTNWGNLG YSSGYTSYDV
GAAIIEDRQI TREKYSEIKL EAQFLQVSPA YITSKPHSPC SGCYTNASAL MTTRLQGEST
NFYIIRHSNY IVTQSTSYEW RANTSQGSIT VPQPGGSSTL HGRDSKFHVT DCDLGGINLI
YPTAETFTWR RHGSKSVLVL YGGEDEIHEF AVDSNLGNAT TIEGSNHLDV YLLWRNEAYQ
YWVMDLPAPE PLDLHASPSR TNSSVIVKAG YLLRNASISE NTLHLTGDVN ATSTVELISA
PPGCCSDVLY DGNRLQNISN TNVLYRGHFT AKGEEKSLYL STQGGYAYGH SVWLDSTYLG
SWQGNPAIQN YNQTLQFPQS LQGDEHYVLT ILIDNLGLDL NFELNTNTMK SPRGLLDYDL
SGHNSWKITG NLGGEQYREH SRGPLNKGST FVERQGYHLS GALNSTKAEW QTRTPQEGLS
AAGVGLFATT FSLDYPQGYD IPTSVNNTGP QTEYPIPEGI LNHHGGNYLA HHLLGSGRKW
GKAGRD
//
