ID BGALC_TALMQ Reviewed; 999 AA. AC B6QHA9; DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 24-JAN-2024, entry version 73. DE RecName: Full=Probable beta-galactosidase C; DE EC=3.2.1.23; DE AltName: Full=Lactase C; DE Flags: Precursor; GN Name=lacC; ORFNames=PMAA_093700; OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333) OS (Penicillium marneffei). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces; OC Talaromyces sect. Talaromyces. OX NCBI_TaxID=441960; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333; RX PubMed=25676766; DOI=10.1128/genomea.01559-14; RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.; RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus RT (ATCC10500)."; RL Genome Announc. 3:E0155914-E0155914(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; DS995902; EEA22754.1; -; Genomic_DNA. DR RefSeq; XP_002148921.1; XM_002148885.1. DR AlphaFoldDB; B6QHA9; -. DR SMR; B6QHA9; -. DR STRING; 441960.B6QHA9; -. DR GlyCosmos; B6QHA9; 13 sites, No reported glycans. DR VEuPathDB; FungiDB:PMAA_093700; -. DR HOGENOM; CLU_005732_2_1_1; -. DR OrthoDB; 1032627at2759; -. DR PhylomeDB; B6QHA9; -. DR Proteomes; UP000001294; 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; IPR001944; Glycoside_Hdrlase_35. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR23421:SF125; BETA-GALACTOSIDASE C-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. PE 3: Inferred from homology; KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase; KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..999 FT /note="Probable beta-galactosidase C" FT /id="PRO_0000395240" FT ACT_SITE 186 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 285 FT /note="Nucleophile" FT /evidence="ECO:0000255" FT BINDING 80 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 125 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 127 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 185 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 249 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 351 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CARBOHYD 25 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 195 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 274 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 389 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 441 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 512 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 519 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 600 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 675 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 713 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 757 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 808 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 897 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 255..302 FT /evidence="ECO:0000250" SQ SEQUENCE 999 AA; 110430 MW; CD1A02A994EB2050 CRC64; MFFFRFLTTV LLLFNAKLLV AQSSNTSSPV HWDKYSLSIN GERLFVFAGE FHYIRLPVPE LWLDVFQKLK ANGFNAISVY FYWNHHSASE GVYDFETGGH NVQRLFDYAK QAGVYIIARP GPYANGELSA GGYALWAANG RLGGERTRDS QYYDLWSPWM TKIGKIIAAN QITEGGPVIL VQHENELQET THRANNTLVL YMEQITQILD AAGIVVPSTH NEKGMRSMSW SMDYEDVGGA VNIYGLDSYP GGLSCTNPNA GFNLIRTYYQ WFQNYSYTQP EYLAEFQGGY FTPWGGVFYD DCASMLQPEY ADVFYKNNIG NRVTLQSLYM AYGGTNWGHI AAPVVYTSYD YSAPLRETRE IRDKLKQTKL LGLFTRVSPD LLQTEMEGNG TSYTTGANIF TWALRNPETN AGFYVVAQDD SSSTTDVVFD LEVETSAGSV NITNIGLDGR QSKIITTDYK VGDTTLLYCS ADILTYATLD VDVLALYLNK GQTGTFVLAN AASHLKYTVY GNSTVTSSNS SQGTIYTYTQ GQGISAIKFS NRFLVYLLDK YTAWDFFAPP LQLSDPNVKP NEHIFVIGPY LVREATIKGR TLELTGDNQN TTSIEIYHGN PFITSITWNG KHLSTKRTAY GSLTATIPGA EAITITLPKL TSWKSHDMIP EIDPEYDDSN WVVCNKTTSF NAIAPLSLPV LYSGDYGYHA GPKIYRGRFG STNATGVTVT AQNGNAAGWS AWLNGIYIGG VTGDPSIEAT SAVLKFNSST TLKQEGSENV LTVLVDYTGH DEDNVKPARA QNPRGLLGVI FEGSTSTNFT SWKLQGNAGG EKNIDALRGP MNEGGFYGER LGWHLPGFEP STKSGWDTRA PSDGVDGGSH RFYITEFTLD LGPNSHALDV PIGIHLNASS TSGPAVAYVW LNGYKFAHYL PHIGPQTVFP FQPGVLNIQG SEGHKRKNTL AVSLWALTDQ PAALDVVELV AYGKYTSSFD FARDWSYLQP RWVDRSKYA //