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Database: UniProt
Entry: B8N765_ASPFN
LinkDB: B8N765_ASPFN
Original site: B8N765_ASPFN 
ID   B8N765_ASPFN            Unreviewed;       981 AA.
AC   B8N765;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   16-JAN-2019, entry version 59.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=AFLA_019980 {ECO:0000313|EMBL:EED54746.1};
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM
OS   12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=332952 {ECO:0000313|EMBL:EED54746.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED54746.1, ECO:0000313|Proteomes:UP000001875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167
RC   {ECO:0000313|Proteomes:UP000001875};
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   -!- 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}.
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DR   EMBL; EQ963474; EED54746.1; -; Genomic_DNA.
DR   RefSeq; XP_002376018.1; XM_002375977.1.
DR   ProteinModelPortal; B8N765; -.
DR   EnsemblFungi; EED54746; EED54746; AFLA_019980.
DR   GeneID; 7914956; -.
DR   KEGG; afv:AFLA_019980; -.
DR   EuPathDB; FungiDB:AFLA_019980; -.
DR   HOGENOM; HOG000181922; -.
DR   OMA; IDAYPMR; -.
DR   Proteomes; UP000001875; 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; -; 2.
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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001875};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001875}.
FT   DOMAIN      355    537       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   981 AA;  108805 MW;  E5AE19A1A70365E7 CRC64;
     MINDERIMIF SGEFHPFRLP VPGLWLDVFQ KIKSMGFNGV SFYTDWGLLE GNPENVMVGD
     NGINNDTDIW NLDEFFAAAS EAGIYLIARP GPYINAETSA GGIPGWVLRI KGAIRSMSPD
     YVGAIKNYMS TVGKIIADAQ ITRGGPVIMV QPENEYTTWP GLTEEEFPSQ MNREVMAFMA
     EELRAAGVEV PMAMNDNEVE GYFAPGTGLG EVDIYGIDAY PMRYDCAHPD VWPTYRFPYD
     WNILHEEQSP TTPFTIMEFQ GGSGGGWGGV TEEGCAMLVN QEASRVVYKN NYSFGVKIFN
     IYMTYGGTNW GNLGYHGGYT SYDYGASIAE DRTLTREKYS EQKLQANFFK VSPAYLTATP
     GTGQNGSYTD NPRIAVTPLV GNGTKTNFYV VRHADFTFTG NARYRMTVST SIGNVTLPQL
     HNTTLSLNGR DSKLHVTDYD VGGINMIYSS AEVLTWARAL SSTRVLVLYG GEDEVHEVAF
     SRALSEPVIL DGPTSGIIIE QQQAAWVIQW RVTATPRVIQ IGDLELHLLW RNDAYDYWVM
     EVPAAEPIGN YSSPSKDLII VKAGYLVRSA SIQDNHLVLS GDVNATTTVE VISTPQEVRG
     IVFNNQSLNT ILSSRGKLQG SVPYHPPTIS VPSLYDLEWR YLDSLPEIDP LYDDKAWTVL
     NQSWSNNPRN LTTPTSLYAL DYGYHTGSLL YRGYFIANGQ ESSLFLNISG GAGFGYSIWL
     NDNYLDSWAG SSDSSFYAQN ISLVPTTNNA GLSMGKPYTI SILIDHMGYD EEAPGTDAIK
     FPRGILDYSL SGHEHQSDLR WKMTGNLGGE QYHDLIRGPL NEGAMFAERQ GYHLPQPPSD
     TWETRSPFTK GIEKPGVGFF TTSFPLNLPK GYDIPLRFVF AFNGSTNVVH TRNYRCQLYV
     NGFQFGKFVN NLGPQTDFPV PEGILNYNGN NHIAVTLWGL DGGAVLGPEG LQLVASRPIW
     SGYRKPTAVE WPGYVKRRGA Y
//
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