ID A0A2W1HUY6_9PLEO Unreviewed; 1009 AA.
AC A0A2W1HUY6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 ORFNames=Ptr86124_006959 {ECO:0000313|EMBL:KAI1514329.1}, PtrM4_06389
GN {ECO:0000313|EMBL:PWO13338.1}, PtrM4_107760
GN {ECO:0000313|EMBL:KAF7570774.1};
OS Pyrenophora tritici-repentis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=45151 {ECO:0000313|EMBL:KAI1514329.1, ECO:0000313|Proteomes:UP000249757};
RN [1] {ECO:0000313|EMBL:KAF7570774.1, ECO:0000313|Proteomes:UP000245464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M4 {ECO:0000313|EMBL:KAF7570774.1,
RC ECO:0000313|Proteomes:UP000245464};
RX PubMed=29685100; DOI=10.1186/s12864-018-4680-3;
RA Moolhuijzen P., See P.T., Hane J.K., Shi G., Liu Z., Oliver R.P.,
RA Moffat C.S.;
RT "Comparative genomics of the wheat fungal pathogen Pyrenophora tritici-
RT repentis reveals chromosomal variations and genome plasticity.";
RL BMC Genomics 19:279-279(2018).
RN [2] {ECO:0000313|EMBL:KAI1514329.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1514329.1};
RA Moolhuijzen P.M., Moffat C.S.;
RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAI1514329.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1514329.1};
RA Moolhuijzen P., See P.T., Shi G., Powell H.R., Cockram J., Jorgensen L.N.,
RA Benslimane H., Strelkov S.E., Turner J., Liu Z., Moffat C.S.;
RT "A global pangenome for the wheat fungal pathogen Pyrenophora tritici-
RT repentis and prediction of effector protein structural homology.";
RL bioRxiv 0:0-0(2022).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAI1514329.1}.
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DR EMBL; NQIK02000005; KAF7570774.1; -; Genomic_DNA.
DR EMBL; NRDI02000008; KAI1514329.1; -; Genomic_DNA.
DR EMBL; NQIK01000004; PWO13338.1; -; Genomic_DNA.
DR OMA; GGCPGDI; -.
DR Proteomes; UP000245464; Unassembled WGS sequence.
DR Proteomes; UP000249757; 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: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..1009
FT /note="Probable beta-galactosidase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041069239"
FT DOMAIN 408..589
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1009 AA; 109564 MW; 572EAEC64D06F663 CRC64;
MKTIAGLSWI SALSSLASLP NGLGVSAQNN TPSTWPLHDN GLSDVVQWDH YSFKVNGKRL
FVFSGEIHYW RIPVYEVWED LLEKIKAAGF TAFAFYGNWA YHSANNKTLD FESGAHDFSK
LFEIAHRVGL YVITRPGPYV NAEANAGGFP LWLTTGAYGK LRDDDPRYLQ ALDPYFSKFS
ELTSKHLVTN GGNALVYQIE NEYGEQWKDR TKKIPNDAAG RYMQALEDSA RANGIEIPLI
HNDPNMNTKS WSKDYAPGAV GNVDVAGLDS YPSCWSCNLA ECTGTNGKYV AYQVVNYYDH
FKEVSPTQPS FFPEFQGGSY NPWGGPEGGC PGDIGADFAN LFYRNLISQR VTAVSLYMMF
GGTNWGAIAA PVTATSYDYS SPISENREIG AKFYETKNLA MFTRVADDLT VTDRLGSSSS
YTTNPAVTAS ELRNPITKAA FYVTIHSVSS SSTTESFKLH ISTSVGNLTI PQHSGSIVLN
GHQSKIISTD FAMGNKTLTY STAEILTYAL IDSSPVVVLS TDVGGSVEFH VKGATKGSLA
SSGFTSNATF RAEAGGVTTN IERVTGMGVY QFNNGVKVVL ADKPTAYLFW APNLSNDPFA
PVDQSVLIQG PYLVRGAALD GDVVALKGDV KNSTTIEVFA HETALTLSWN GKKLETSRTP
YGSLKAQISA FNGTIPLPSL NDWKVNEGLP EKMPEYDDNG AAWVVANHTT TPNPTKPDTL
PVLYVDEYGF HNSFHLFRGY FEGSATGAQL SVQGGLAFGW SAWLNGDLVG SWLGNTTLGV
GNMTLSFANA TVHANGTNVL LIAQDNTGHD LRGGATDPRG ILRATLDGAD FTSWKIAGEA
GGENIQLDPV RGPLAEGGLT AERLGWHLSG FSDCDWASAS PSTGFSGADI KFYRTTFPLD
IPEDVDASFA FILNATGPKT VRVQLFVNGY QYARFNPYVG NEVKFPIPPG ILNYAGDNVI
GLSVWAQGND GAKVDVEFVQ EYAVESSWSS RFDSEYLRPE WTEERLAYA
//
