ID W2S921_9EURO Unreviewed; 1096 AA.
AC W2S921;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=HMPREF1541_10108 {ECO:0000313|EMBL:ETN45231.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN45231.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN45231.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN45231.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) 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 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; KB822713; ETN45231.1; -; Genomic_DNA.
DR RefSeq; XP_008713001.1; XM_008714779.1.
DR AlphaFoldDB; W2S921; -.
DR STRING; 1220924.W2S921; -.
DR GeneID; 19977447; -.
DR VEuPathDB; FungiDB:HMPREF1541_10108; -.
DR eggNOG; KOG2024; Eukaryota.
DR HOGENOM; CLU_002346_0_0_1; -.
DR InParanoid; W2S921; -.
DR OrthoDB; 276651at2759; -.
DR Proteomes; UP000030752; 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:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000030752}.
FT DOMAIN 751..1094
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 984..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 121713 MW; D2ACCC1D153B0CE5 CRC64;
MSGTFPPSTP DWSNIEVIHK GTLAPRSYFF LYDDEAAALK ADISASSSVN LSGTWKFQHS
KSPFTAPHGF EEPNYDTSTW SDIQVPSHWQ LQGWGAPHYT NFNYIIPVDP PHVPYDDNQT
GSYVRKFVVP KDFVDQQIRL RFEGVDSAFH VYVNGREVGY SQGSRNASEF DITAFLDTPG
ENTLAVRVYQ WSDGSYIEDQ DQWRFSGIFR DVLLVAFPHT HIEDFHVQTL LDDEYKDADL
QVKVTTQGTG PIDLKLLDIT GQAVASDTKH AADVSTAFSM KLANPRKWSA EDPNLYKLVL
SFGGRFIAQN VGFRRIEIVN GIYKVNGRRI VFRGANRHEH HPLHGRAVPY DFMKQDLLIM
KKHNINAIRT CHQPSDPRLY SLADELGFWI MDEADLECHG FSVIDQQAMP EEDKIKSAAD
QQNLSYDRAA RWTSDNPEWK DQYVDRAVQL VNRDKNHPCV IMWSLGNEAM YGRNHQAMYD
KIKTLDTSRP VHYEGDREAK SADLFSQMYS SVDSIIDFAK EENFTKPLVL CEFIHAMGNG
PGNIKEYVDA FYKYPRLQGG WVWEWANHGL LSKDRKTGAE FMAYGGDFGD EPNDYNFIMD
GVLFSNHTPT PGLIEYTKAI EPVQVLSHAD GKVTIINRYD TISLNHLKCE AQLVGDGVKK
PLGSISIPSN IDPHTEAILS IPELDVHDLK GDIYLQLDFS LANLTLWAAA GHITSTSQLQ
LQAPFALSAS LPVPTPDAAV PSIVQHASSL TITTASTIFT LSLASGHLTS LIKSGTEHIH
ASLGPHLTLS RALTDNDRPQ DGQDWLRNYL HLARGHMRSI SWSTDSTNRT TTVTVQARLA
PPVLSWSFAA TTTYTFHPSG RLHIHVTGKP QGANLPPTLP RIGLEMGLPL AFSRVDWFGR
GPGESYKDKK LSQQFGNWGF DSVDDLWVDY EFPQEGGNRT DVRWVRFSAP SPTDAALSSV
QHAAQGVVGQ LANAMSNLFS PGAQTAPPAS ALGGSECTVD TTPSAPAPAP TAPSSSLTAH
FGSRPNFSFH ASRYSSADVD SAKHPHELHA LKRDYVILRL DADHHGLGTG SCGPKTLDEY
ALKVEGGGWE FELVLE
//