ID BGALA_ASPFN Reviewed; 1005 AA. AC B8N6V7; DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 77. DE RecName: Full=Probable beta-galactosidase A; DE EC=3.2.1.23; DE AltName: Full=Lactase A; DE Flags: Precursor; GN Name=lacA; ORFNames=AFLA_017100; OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 OS / JCM 12722 / SRRC 167). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=332952; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / RC SRRC 167; 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 -!- 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}. 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; EQ963474; EED54458.1; -; Genomic_DNA. DR RefSeq; XP_002375730.1; XM_002375689.1. DR AlphaFoldDB; B8N6V7; -. DR SMR; B8N6V7; -. DR STRING; 332952.B8N6V7; -. DR GlyCosmos; B8N6V7; 11 sites, No reported glycans. DR EnsemblFungi; EED54458; EED54458; AFLA_017100. DR VEuPathDB; FungiDB:AFLA_002164; -. DR eggNOG; KOG0496; Eukaryota. DR HOGENOM; CLU_005732_2_0_1; -. DR OMA; QTEFPVP; -. DR OrthoDB; 1032627at2759; -. DR Proteomes; UP000001875; Unassembled WGS sequence. 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; Beta-galactosidase, domain 2; 1. DR Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2. 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:SF122; BETA-GALACTOSIDASE A-RELATED; 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 Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase; KW Hydrolase; Polysaccharide degradation; Secreted; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..1005 FT /note="Probable beta-galactosidase A" FT /id="PRO_0000395216" 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 453 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 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 1005 AA; 109870 MW; BAD290D2FA9EB003 CRC64; MKLLSVAAVA LLAAQAAGAS IKHRLNGFTI LEHPDPAKRD LLQDIVTWDD KSLFINGERI MLFSGEVHPF RLPVPSLWLD IFHKIRALGF NCVSFYIDWA LLEGKPGDYR AEGIFALEPF FDAAKEAGIY LIARPGSYIN AEVSGGGFPG WLQRVNGTLR SSDEPFLKAT DNYIANAAAA VAKAQITNGG PVILYQPENE YSGGCCGVKY PDADYMQYVM DQARKADIVV PFISNDASPS GHNAPGSGTG AVDIYGHDSY PLGFDCANPS VWPEGKLPDN FRTLHLEQSP STPYSLLEFQ AGAFDPWGGP GFEKCYALVN HEFSRVFYRN DLSFGVSTFN LYMTFGGTNW GNLGHPGGYT SYDYGSPITE TRNVTREKYS DIKLLANFVK ASPSYLTATP RNLTTGVYTD TSDLAVTPLI GDSPGSFFVV RHTDYSSQES TSYKLKLPTS AGNLTIPQLE GTLSLNGRDS KIHVVDYNVS GTNIIYSTAE VFTWKKFDGN KVLVLYGGPK EHHELAIASK SNVTIIEGSD SGIVSTRKGS SVIIGWDVSS TRRIVQVGDL RVFLLDRNSA YNYWVPELPT EGTSPGFSTS KTTASSIIVK AGYLLRGAHL DGADLHLTAD FNATTPIEVI GAPTGAKNLF VNGEKASHTV DKNGIWSSEV KYAAPEIKLP GLKDLDWKYL DTLPEIKSSY DDSAWVSADL PKTKNTHRPL DTPTSLYSSD YGFHTGYLIY RGHFVANGKE SEFFIRTQGG SAFGSSVWLN ETYLGSWTGA DYAMDGNSTY KLSQLESGKN YVITVVIDNL GLDENWTVGE ETMKNPRGIL SYKLSGQDAS AITWKLTGNL GGEDYQDKVR GPLNEGGLYA ERQGFHQPQP PSESWESGSP LEGLSKPGIG FYTAQFDLDL PKGWDVPLYF NFGNNTQAAR AQLYVNGYQY GKFTGNVGPQ TSFPVPEGIL NYRGTNYVAL SLWALESDGA KLGSFELSYT TPVLTGYGNV ESPEQPKYEQ RKGAY //