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Database: UniProt
Entry: S3EAU9_GLAL2
LinkDB: S3EAU9_GLAL2
Original site: S3EAU9_GLAL2 
ID   S3EAU9_GLAL2            Unreviewed;       986 AA.
AC   S3EAU9;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Probable beta-galactosidase C {ECO:0000256|ARBA:ARBA00040694};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE   AltName: Full=Lactase C {ECO:0000256|ARBA:ARBA00042635};
GN   ORFNames=GLAREA_11152 {ECO:0000313|EMBL:EPE35453.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE35453.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE35453.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   EMBL; KE145354; EPE35453.1; -; Genomic_DNA.
DR   RefSeq; XP_008077532.1; XM_008079341.1.
DR   AlphaFoldDB; S3EAU9; -.
DR   GeneID; 19470194; -.
DR   KEGG; glz:GLAREA_11152; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_005732_2_1_1; -.
DR   OrthoDB; 1032627at2759; -.
DR   Proteomes; UP000016922; 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; 2.60.390.10; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:EPE35453.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..986
FT                   /note="Probable beta-galactosidase C"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004520196"
FT   DOMAIN          378..554
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000259|SMART:SM01029"
SQ   SEQUENCE   986 AA;  108064 MW;  6E78D5E5C67E55C9 CRC64;
     MRLSGLLLTL SALLWGCQST DNGLTTAVTW DNYSLSVNGE RVFIYSGEFH YQRMPVPEMW
     LDIFQKLKAN GFNTVSVYFF WSYHSPSRDV YDFETTGRNV QRMFDYAKEA GIWIIARAGP
     YINAETNGGG LALWGSDGSM GNLRTSDNAY YQAWLPWVLK MGEIIAKNEI MKGGTVIFNQ
     IENELQETSY VATNTLVKYM EQLKAAFLLS GVTVPFSHNE KGMRSISWST DYQNVGGAVN
     LYGLDSYPGG LSCTSVNSGF NVVRTYYQWF ANYSYTQPNH FPEFEGGWFS PWGGTFYDDC
     ASEHEPGFAD VYYKNNIGQR TTIQNIYMTW GGTNWGHSAA PVVYTSYDYS APLRETRQIQ
     DKLYQTKLIG LFSRVSKDLL KTDMIGNGTG YAVSSTGIWT WEIRNPDTNT GFYTVQQAKT
     GSRTSVFFSV NLNTSAGNIT VPNVNLNGRQ SKIFVTDYNF GNHSLLYSTA DVLTYGVFDV
     DVLVLYLMEG QTGQFALKSK SGNAKFTSEG ASKISTAAGN NTITVSYTQG AGQTVLQLDG
     MLIYLLEQKA AWKFWAPPTT NSPDVKPDEQ IFVLGPYLVR SASITNGVVH ISGDNDNATT
     IEVYSGNPAI QTIDWNGIRL NAVKTSYGSV TAKIPGAADR TISLPPLENW RSADSLPEKA
     ATYDDSKWAV CNKSITLSPV APLTKPVLFS SDYGFYTGAK IYRGYFDGQS FTSVDITASG
     GLAFGWTAWL NGALVGGNVG NATLTTTSAV IKLPSASLKA KDNLLTVVVD YHGHDQTSTA
     KGVENPRGIL GASLISSNGT SSSSAFKTWK IQGNAGGSAD IDPARGPMNE GGLYGERLGW
     ALPSFVPSTP QFDRSSPFVG IKTSGVQFYT TTFHLNIDSD LDVPLGIELG APAGTVARVM
     IWVNGYQYGK YVPHIGPQTR FPVPPGVINN RGLNTVALSL WAMTDAGAKM DTVKLITYGQ
     YQTNFKFNRD WSALQPGWDK SRLQYA
//
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