ID S8BXG2_DACHA Unreviewed; 1017 AA.
AC S8BXG2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, 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=H072_1885 {ECO:0000313|EMBL:EPS44203.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS44203.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS44203.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS44203.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-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}.
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:EPS44203.1}.
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DR EMBL; AQGS01000057; EPS44203.1; -; Genomic_DNA.
DR RefSeq; XP_011107876.1; XM_011109574.1.
DR AlphaFoldDB; S8BXG2; -.
DR STRING; 1284197.S8BXG2; -.
DR eggNOG; KOG2024; Eukaryota.
DR HOGENOM; CLU_002346_0_2_1; -.
DR OMA; WCDHGIL; -.
DR OrthoDB; 276651at2759; -.
DR Proteomes; UP000015100; 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:UP000015100}.
FT DOMAIN 736..1017
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1017 AA; 116107 MW; DE31261F9DC874BC CRC64;
MRVTASNYRW PSHKPDWSNL SVLHKNTLPP RSTFYIYDNE KDALYRDTAQ SKTLCLSGKW
KFRLDKVPIE QPSFPPFDLN MEKWGDIEVP GMWQLQGYGK GPQYTNVDYP WPVDPPNIPY
DDNETGHYHR EFLIPESFRD HQLRLRFEGV DSGFHVWINS KEVGYSQGAR CPSEFDITDF
VHLDKKNYIT VVVYQRCDGT YLEDQDQWWL SGMFRDVNIM AFPKIHIQDF KIETILDDQY
RDATLSIKIE LNESTNVEAK LYDPSMSIVD TITQSSSSTT MNMEIPVQDP YKWTAESPYL
YTLILSLGAG HVICQRVGFR TSEIKDGNLL VNGKPIIIRG VNRHEHHPTR GRAVPYEFMR
NDLLLMKTHN INAIRTSHYM NDPRLYDVAD ELGLWILDEA DLECHGMGEL GGDSASWTSD
NPDWEEAYVD RARQLVMRDK NHPCVIIWSL GNESFYGRNH RAMYDWIKAF DKTRPVHYEA
DYNAHSADLY SRMYASVGDI INFATRDATW DKPLILCEYV HAMGNGPGGI KEYIDAFYKY
PRLQGGFVWE WANHGLLTKT ENGDEYYGYG GDFGDDPHDG HFVMDGLLHS NHTPTPGLTE
YKKAIEPVQV LENSTAGRVL IINRYDHVTL DHLKCEWCVV GDDYKGPKKE ISIPAGVKPG
ATAAIDIQGV DLPPGSYLEV SFSLRNDELW AKAGHEVAFG QIASNTARDP LSLAGLTLKS
SKQAPIINII SPSRLEVVGQ KTTWEFDTAH GFLCLWKTSD GGKALVNRIL GLDFYRAVTD
NERFNHGSDW KSQRLHQTKT HLQSFETSEN AEDGTVTVKA KYRVAPPIYQ WSVDTEITYV
MSDHGTKLYV KGNPRGLRLP RTFARIGLTL TLDSDYTHCT WFGRGPGESY SDSKMAQRFG
NWSAPVEDLY TPYEFPQDCG NRTDVRSVSF ACDEAGKGKI TARFGDQDGC SFSAMHYTTQ
DLDECEHPYE LEKRKKEEVY VRLDWAHQGL GSGSCGPQVD PRYELLSKPF EFELMLE
//
