BGAL_SULAC
ID BGAL_SULAC Reviewed; 491 AA.
AC P14288; Q4J7S6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Beta-galactosidase;
DE Short=Lactase;
DE EC=3.2.1.23;
GN Name=bgaS; OrderedLocusNames=Saci_1849;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2508066; DOI=10.1093/nar/17.19.7980;
RA Little S., Cartwright P., Campbell C., Prenneta A., McChesney J.,
RA Mountain A., Robinson M.;
RT "Nucleotide sequence of a thermostable beta-galactosidase from Sulfolobus
RT solfataricus.";
RL Nucleic Acids Res. 17:7980-7980(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable.;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to originate from S.solfataricus strain
CC P1, but the culture was contaminated with S.acidocaldarius.
CC {ECO:0000305|PubMed:2508066}.
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DR EMBL; X15950; CAA34074.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY81155.1; -; Genomic_DNA.
DR RefSeq; WP_011278657.1; NC_007181.1.
DR AlphaFoldDB; P14288; -.
DR SMR; P14288; -.
DR STRING; 330779.Saci_1849; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR EnsemblBacteria; AAY81155; AAY81155; Saci_1849.
DR GeneID; 3474772; -.
DR KEGG; sai:Saci_1849; -.
DR PATRIC; fig|330779.12.peg.1796; -.
DR eggNOG; arCOG05412; Archaea.
DR HOGENOM; CLU_001859_1_3_2; -.
DR OMA; VEACDRK; -.
DR BRENDA; 3.2.1.B34; 6160.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 2.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..491
FT /note="Beta-galactosidase"
FT /id="PRO_0000063866"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 389
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT CONFLICT 135
FT /note="Q -> H (in Ref. 1; CAA34074)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 57143 MW; A7FF7F4DEEC1C189 CRC64;
MLSFPKGFKF GWSQSGFQSE MGTPGSEDPN SDWHVWVHDR ENIVSQVVSG DLPENGPGYW
GNYKRFHDEA EKIGLNAVRI NVEWSRIFPR PLPKPEMQTG TDKENSPVIS VDLNESKLRE
MDNYANHEAL SHYRQILEDL RNRGFHIVLN MYHWTLPIWL HDPIRVRRGD FTGPTGWLNS
RTVYEFARFS AYVAWKLDDL ASEYATMNEP NVVWGAGYAF PRAGFPPNYL SFRLSEIAKW
NIIQAHARAY DAIKSVSKKS VGIIYANTSY YPLRPQDNEA VEIAERLNRW SFFDSIIKGE
ITSEGQNVRE DLRNRLDWIG VNYYTRTVVT KAESGYLTLP GYGDRCERNS LSLANLPTSD
FGWEFFPEGL YDVLLKYWNR YGLPLYVMEN GIADDADYQR PYYLVSHIYQ VHRALNEGVD
VRGYLHWSLA DNYEWSSGFS MRFGLLKVDY LTKRLYWRPS ALVYREITRS NGIPEELEHL
NRVPPIKPLR H