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Database: UniProt
Entry: A0A1S9DBF7_ASPOZ
LinkDB: A0A1S9DBF7_ASPOZ
Original site: A0A1S9DBF7_ASPOZ 
ID   A0A1S9DBF7_ASPOZ        Unreviewed;       846 AA.
AC   A0A1S9DBF7;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   16-JAN-2019, entry version 11.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {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.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|RuleBase:RU000675,
CC         ECO:0000256|SAAS:SAAS01116863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OOO06413.1}.
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DR   EMBL; MKZY01000008; OOO06413.1; -; Genomic_DNA.
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; -; 1.
DR   Gene3D; 2.60.120.260; -; 3.
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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000190312};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:OOO06413.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190312};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    846       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012661878.
FT   DOMAIN      391    541       BetaGal_dom2. {ECO:0000259|SMART:
FT                                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
//
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