ID Q8NIU3_NEUCS Unreviewed; 992 AA.
AC Q8NIU3;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Probable beta-galactosidase B {ECO:0000256|ARBA:ARBA00040693};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase B {ECO:0000256|ARBA:ARBA00042633};
GN Name=B13H18.180 {ECO:0000313|EMBL:CAD37064.1};
OS Neurospora crassa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=5141 {ECO:0000313|EMBL:CAD37064.1};
RN [1] {ECO:0000313|EMBL:CAD37064.1}
RP NUCLEOTIDE SEQUENCE.
RA Schulte U., Aign V., Hoheisel J., Brandt P., Fartmann B., Holland R.,
RA Nyakatura G., Mewes H.W., Mannhaupt G.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAD37064.1}
RP NUCLEOTIDE SEQUENCE.
RA German Neurospora genome project;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
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; AL807374; CAD37064.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NIU3; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR VEuPathDB; FungiDB:NCU04623; -.
DR HOGENOM; CLU_005732_2_0_1; -.
DR OMA; GGCPGDI; -.
DR PhylomeDB; Q8NIU3; -.
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:SF64; BETA-GALACTOSIDASE (EUROFUNG)-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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..992
FT /note="Probable beta-galactosidase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004312952"
FT DOMAIN 378..559
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 992 AA; 108896 MW; CB3D112DF489DAD3 CRC64;
MRFANKGFES FAYALLLLSS GRQYVLGASD TPSAWPIQGN DLQDQIQWDH YSIIINGERL
FLFGGEMHPF RLPVPELWQD VLEKVKAMGM RMISIYTHWG FHAPTPDQTD FSTGAHNLTR
FFEMAKEVGL YVLVRPGPYI NGELNAGGLA LWSTTGSYGE LRSNGSAFTE AWTPYQTGIA
KLVKPFQLTD GGTVIMYQLE NEYGEQWKNV DAKIPNPKAV SYMEKLKENA IENGIVVPSV
HNAPNANGRP WSRDYDTVGA GGDVDIYGLD SYLVSPNQPS FMPEFQGGAM SPWLSPAGGC
AERTGPEFVN FYYRDNIAQR ITILNLYMIY GGTNWGWLAA PFLGSSYDYG AAISEDRNIG
SKYYEIKNLG LFTRAADELA YTDRVGTGTN YTNNTNIFTT ELKNPKTGAR FYVLRHATTS
SDSTETFAIN VTTSLGSFYV PRIAPCPKLV GHEGKIFVAD FHFGKHTLFY ATTEVLTYSV
INQKTTLVLW TPIGISGEFY LKGAKKGTLT SSSKGQTAVF DGQDDGVVVG FTQREGATVL
EFDNDVRVVL VDRDTAYKTW VPALTKDPKV PVDKTAIVVG PRLVRSASVQ GNTISVKGDC
NDTTGIEVFT SSHVSTIKWN GKQLRTTQTN YGTLKASLQA PARFSAPKFA SWKSQDSLPE
TAVGYSDDGP AWVIANHTTT YSATKGTVPY LFSDEYGFHT GIRLWRGHFS GEFGATGVYL
TIQGGTAHSW SAFLNGKFLG SYTGNPTVAA SNATLSFANV PIFTNQTNVL LVMHDDTGHD
QLSAALNPRG ILNATLLSSN SSTTPKFNLW KLAGTAGGFD PSRSTLDPLR THYNEGGLSA
ERLGWHLPDF DDSNWSSPLT SPAQGFTGAT IRFYRTSLPL NVPKGVDASF AFKFTPVDTS
NLNYRAFLYV NGYQYGRYYP SIASENVFPV PAGVLNLGGD NVIGLAVWAQ TEKGAKVDVE
LVTRYAVESS FESRFDGTYL QPGWTKERLD YA
//
