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Database: UniProt
Entry: A0A093Y8D0_9PEZI
LinkDB: A0A093Y8D0_9PEZI
Original site: A0A093Y8D0_9PEZI 
ID   A0A093Y8D0_9PEZI        Unreviewed;       623 AA.
AC   A0A093Y8D0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=V490_01998 {ECO:0000313|EMBL:KFX98977.1};
OS   Pseudogymnoascus sp. VKM F-3557.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX98977.1, ECO:0000313|Proteomes:UP000029320};
RN   [1] {ECO:0000313|EMBL:KFX98977.1, ECO:0000313|Proteomes:UP000029320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX98977.1,
RC   ECO:0000313|Proteomes:UP000029320};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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|RuleBase:RU000675};
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:KFX98977.1}.
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DR   EMBL; JPJS01000557; KFX98977.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093Y8D0; -.
DR   STRING; 1437433.A0A093Y8D0; -.
DR   HOGENOM; CLU_007853_7_2_1; -.
DR   Proteomes; UP000029320; 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; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR048912; BetaGal1-like_ABD1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21317; BetaGal_ABD_1; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029320};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..623
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001889409"
FT   DOMAIN          32..352
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          398..509
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          532..590
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        179
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        256
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   623 AA;  68570 MW;  B289EC0FE8CDDE78 CRC64;
     MRPFWLLSSV AAILGQAAST DTEPFTYNRT DFLLHGKPYQ MIGGQMDPQR IPHEYWRDRL
     SMARAMGLNT IFSYIFWNDI EPSPGAWDFT GNNDIKKYFQ IAQEEGLNIV LRPGPYICGE
     REWGGFPAWL SEVPGMAVRT NNKPFLDASK AYLEHLAEEV APLQVTNGGP ILMVQVENEY
     GSFGNDHIYV AALRDMLKAQ YNVPLYTNDG GGESYLAGGQ ITGVLAETDG DPKTGFEARD
     KYVTDPSSLG PQLDGEYYVT WIDTWGSNST HNTNDGNAAA LKAIQDDVAW VLTNRSSISI
     YMFHGGTNKG FQNAGLWIDN ALAAVTTSYD YGAPLDESGR PTDAYHAIRE TIIAHLGDNS
     TVPDIPVKSP MIDVPTFQLK PSVALFDVLP KPAHQQNPTN MEALGQSYGF IMYRHKVKTA
     LKGSIKPGDV PRDRVLVYVN GERVGVIDRI YMVPATVTLD LKAGDVLELL VENMGRIDYG
     PTLVEQRKGI VGNVTVGDSV LLDWTTYPLS LEQPPAPQSK YRGPAPSTTS TPIFYSGSFD
     VETIGDTFLE LPGWVKGIVW VNGVNLGRYW IIGPQQSLYL PGCYLKNKDN EITVLALEPL
     ADATSAVGHS KRTWGNNPDP DAP
//
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