ID A0A423VQ55_9PEZI Unreviewed; 750 AA.
AC A0A423VQ55;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=VMCG_08688 {ECO:0000313|EMBL:ROV93162.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROV93162.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROV93162.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROV93162.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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 42 family.
CC {ECO:0000256|ARBA:ARBA00005940}.
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:ROV93162.1}.
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DR EMBL; LKEA01000046; ROV93162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423VQ55; -.
DR STRING; 356882.A0A423VQ55; -.
DR Proteomes; UP000283895; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013738; Beta_galactosidase_Trimer.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR003476; Glyco_hydro_42.
DR InterPro; IPR013529; Glyco_hydro_42_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF08532; Glyco_hydro_42M; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000283895};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..750
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019425719"
FT DOMAIN 53..442
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 464..681
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
SQ SEQUENCE 750 AA; 83918 MW; 0E7B5678864F2B40 CRC64;
MRWCSITYLA GLVEGVSALT ARTHNAQSVV RGMSDTAAPS VSRWPSGLHL AVDYYPSQWP
ESTWEPDIVA MRDVNISYVR INEFDWTILE PIEGTYDFSV LDKTLQLLGQ YGLKAIIGTP
TASPPNWLME NYPSVMFVDI TNATYTFGSR RFYSFSSFDY RELSRNITQV LAQRYGDNPN
VVGWQLDNEF GCHNTVRTYD QDAITRFRAW LQQKYGTVEA MNAAQGRVFW SNQYGSFNDV
LPPYLEVYTT NNLYTLDWYT FSSDMVIEFA KEQAEIVRRY APTHVVTTNL QALFTDFDHY
RFAQEVAIDI AVFDLYPLSG PGTFSWLSDQ ELVDTLRTGL PDWQALNHAL YRGIAGVAYG
EVSGPFGVME LEPGVLNWNQ YRVSPWKGMV RLWTLETYAA SGDMVSYFRW RQVPYAQEQT
LSGLHISDGS EDEGFFEVQD VVMNDLPILR EELGTNNTHE PQGDVALVFD YISVWTWSIE
PYSGSWDVKS ATYTNAALTY TDLVYTFYSS LRRLALSIDI VGPGQSLSGY KMVVVPSMPI
ISDRFNTILA SYTDGPVIFG PRSAALTANF SYTPGIQPSQ GALRDHLPFR VTRIETPPDY
ANSGVLYSGS NYTVTSWEEW VSCARQNATS KVSVTSTSKH RLGKPAACCS SEDSPWHYLG
FNPPVDFLVA YLGDVAADAG ISDLTGKTAS KENDLGGSLR LLKRGNLLWA FNYGTEAVAV
PEVGDKAKLL IGKKGSIIAA AHVAVWKLSY
//
