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
//