ID G4V168_NEUT9 Unreviewed; 994 AA.
AC G4V168;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=NEUTE2DRAFT_95681 {ECO:0000313|EMBL:EGZ67806.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ67806.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ67806.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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; GL891269; EGZ67806.1; -; Genomic_DNA.
DR AlphaFoldDB; G4V168; -.
DR STRING; 510952.G4V168; -.
DR eggNOG; KOG2024; Eukaryota.
DR HOGENOM; CLU_002346_0_2_1; -.
DR Proteomes; UP000008513; 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; -; 2.
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; 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; 2.
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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513}.
FT DOMAIN 737..994
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 994 AA; 113643 MW; 130B2EA8944A8231 CRC64;
MSLVYPSSTP DWNNHQVIHR NTLPPRSHFF LYPDSEKALT RDVSLAKAQL LSGEWKFNLS
KSPLVGPVGF QHFDSFTDPD WKPIHVPGMW QLQGFGKGPH YTNINYPFPV NTPHVPIDEN
ECGRYVTHFQ LAPEDKDHQL RLRFEGVDSA FTVWLNGKNV GYSQGSRNPT EFDITTYVNL
EGDNVLAVEV YQRCDGTYIE DQDQWWLSGI FRDVWIHKFP QKSHFKDVKI LPTLDNEYKD
AKLSVTVELS SPEEFTFRLL RPSGGEVIQG TISGEQSTVM EFNIKDPLKW TAETPNLYTL
VLSMPDCALT ERVGFRRVEL LDGVFSVNGN PVKLRGVNRH EHHPDFGRAV PYEWLKRDLI
LMKQHNINAI RTSHYINDPR LYELADELGL WILDEADLEC HGIFVVGGDG NKMLSDNPEW
KEAYLDRARQ MVMRDYNRPS IIIWSLGNES GYGSNHRAMY DYIKSVDTSR PIHYEGDWNA
HSADIFSRMY TSVDDMERYA REPSWDKPFV MCEFAHAMGN GPGALKEYIE LFYKWPRLMG
GFVWEWANHG LRTKTEEGEE YMAYGGDFGD EPNDSNFVLD GLCFSNHTPT PGLLEYKKAI
EPVQTLKLEN GNQVRIINRY DFVTLDHLKC LYYYSDDETD WVEKREVKIP KGVKPHEQAL
ITISDLLDAE ALQAAGRHDC YVTLEFSLAK ATNWAEPNHI LATGQLPLTP PHNPFANLPA
ATNAHFDLLS PTLLSITVPG SNSTTYEFDL SIGALTSWKR SPSSANILTT PLTLCLYRAQ
TDNDHGCDFG RNWTSSRLNM AKHHLLSTSW DPSASPQTVT IKGRFAPPVL NWALETTTIY
SFLEGGKVKV KMHGKPVGRG PGESYRDKKE SQLMGSWTST IDELWTEYEF PQEGGNRTDV
RSVEFRTEGW EMVLGARFVE PNGENTSFQA SRYTVMDVEA AKHPFELHKK RREDVIVHLD
WMHHGLGTGS CGPETRPEYT LWADREYEVE MVLY
//
