ID A0A094HZH2_9PEZI Unreviewed; 1304 AA.
AC A0A094HZH2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN ORFNames=V501_00242 {ECO:0000313|EMBL:KFZ20257.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ20257.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ20257.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
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:KFZ20257.1}.
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DR EMBL; JPKD01000085; KFZ20257.1; -; Genomic_DNA.
DR STRING; 1420914.A0A094HZH2; -.
DR HOGENOM; CLU_261230_0_0_1; -.
DR Proteomes; UP000029315; 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; IPR045518; 2EXR.
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; PF20150; 2EXR; 1.
DR Pfam; PF21317; BetaGal_ABD_1; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF01301; Glyco_hydro_35; 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:UP000029315};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1304
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001899683"
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 DOMAIN 643..746
FT /note="2EXR"
FT /evidence="ECO:0000259|Pfam:PF20150"
SQ SEQUENCE 1304 AA; 144091 MW; 25A4797F0F167DC7 CRC64;
MRSFWLLTSL AAILGPAACA DTVPFTYNRT DFLLHGKPYQ MIGGQMDPQR IPNEYWRDRL
SMARAMGLNT IFSYIFWNDI EPSPGTWDFT GQNDIKKYFQ IAQEEGLNIV LRPGPYICGE
REWGGFPAWL SEVPGMAVRT NNKPFLDASK AYLEHLAEEV APLQVTKGGP ILMVQVENEY
GSFGNDHIYV AALRDMLKSQ YEVPLYTNDG GGESYLAGGQ ITGVLAETDG DPKTGFEARD
KFVTDPTSLG PQLDGEYYVT WIDTWGSNST HNTNDGNAAA LKSIQDDVAW VLTNKSSISI
YMFHGGTNMG FQNAGLWIDN ALSPVTSSYD YGAPLDESGH PTDAYHAIRE TIIAHLGDNS
TVPDIPVKSP MIEIPTFQLK PSVALFDALP KPAHQQNPTN MEALGQSYGF IMYRHKVKTA
IKGSLKPGDV PRDRVLVYVN GERVGVIDRI YTVPATVTLD LKAGDVLELL VENMGRIDYG
PALVEQRKGV VGNVTIGDNV LLDWMAYPLS LEQPPAPQAK YRGPAPSSTS TPIFYTGSFD
VETVGDTFLE LPGWVKGNVW VNGVNLGRYW IIGPQQSLYL PGCYLKNKGN QITVLALEPL
AEATSADLGG GGTFEFGELP APASSLGSMT TTNATRQEPA QSFTLFPQLP VELQRRIWEL
CLPARIVELD RPITENVTTP CSMYNMSHFN SRIPIAIQIC KESRSVALLA GFKEIYDGNF
VDSDAPGWKA MNNIKDLWIT PSIDVLHLNY GNCYNVGRDH PSDNPLQFLL WLRRRLGHST
RISIVAPLVL AFNDYQGAEF MTTYEDKNLD LLTEAGGSYL TTLCVVSLHL SLDAALRKEG
GMLFGRLGEE RVKLVRAGDK TALKAYYKLW AAGPRKALEP VMFFELALVR HESEWLPRVA
QWKQRLVTKW VTHNLRKAEA KNNCADIQDP EGIFRTRRED EWRTVLQGDS GPFSDNMRPP
RGWAFLNNAT DVTNTEHPWV AKVLRDMPCF EPMVMFRLCA DKCFAQKPPR PQHIIGGQGT
VSGREKSGAN DPLKNQHATN LVYYYYCYGG SVFVTLLLSE YPPPPTFSAT KSPQPFHLRT
PVRPIAQAHI ASLIISPIPL TTSIRLLLRL HLTITRRPSR RKEARTNIIV RPTDAAIRPS
LVLAVATRRL PDVQAERACR AREAAEDACT AGPFDRMCDG DFERGASFYS ARRFGAGDSG
KERGKVGGHV RVEGVEGMGV GGFDQLGGYL LVRFSGGRVN AGEPRLGFRA VADVAGVNIK
SGQVALSIRE VVRGYMGDDD AVGSGWHGSN YEVLGKAEEY GDDG
//
