ID BGAL_SACS2 Reviewed; 489 AA. AC P22498; Q9V2Z5; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2001, sequence version 2. DT 27-MAR-2024, entry version 166. DE RecName: Full=Beta-galactosidase; DE Short=Lactase; DE EC=3.2.1.23; GN Name=lacS; OrderedLocusNames=SSO3019; OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OS (Sulfolobus solfataricus). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Saccharolobus. OX NCBI_TaxID=273057; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-33. RC STRAIN=DSM 5833 / MT-4; RX PubMed=2121622; DOI=10.1016/0378-1119(90)90472-4; RA Cubellis M.V., Rozzo C., Montecucchi P., Rossi M.; RT "Isolation and sequencing of a new beta-galactosidase-encoding RT archaebacterial gene."; RL Gene 94:89-94(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=98/2; RX PubMed=10383958; DOI=10.1128/jb.181.13.3920-3927.1999; RA Haseltine C., Montalvo-Rodriguez R., Bini E., Carl A., Blum P.; RT "Coordinate transcriptional control in the hyperthermophilic archaeon RT Sulfolobus solfataricus."; RL J. Bacteriol. 181:3920-3927(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; RX PubMed=11427726; DOI=10.1073/pnas.141222098; RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.; RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2."; RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001). RN [4] RP METHYLATION AT LYS-116; LYS-135; LYS-273; LYS-311 AND LYS-332, AND MASS RP SPECTROMETRY. RX PubMed=14660666; DOI=10.1074/jbc.m308520200; RA Febbraio F., Andolfo A., Tanfani F., Briante R., Gentile F., Formisano S., RA Vaccaro C., Scire A., Bertoli E., Pucci P., Nucci R.; RT "Thermal stability and aggregation of Sulfolobus solfataricus beta- RT glycosidase are dependent upon the N-epsilon-methylation of specific lysyl RT residues: critical role of in vivo post-translational modifications."; RL J. Biol. Chem. 279:10185-10194(2004). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RC STRAIN=DSM 5833 / MT-4; RX PubMed=9299327; DOI=10.1006/jmbi.1997.1215; RA Aguilar C.F., Sanderson I., Moracci M., Ciaramella M., Nucci R., Rossi M., RA Pearl L.H.; RT "Crystal structure of the beta-glycosidase from the hyperthermophilic RT archeon Sulfolobus solfataricus: resilience as a key factor in RT thermostability."; RL J. Mol. Biol. 271:789-802(1997). 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 -!- SUBUNIT: Homotetramer. CC -!- MASS SPECTROMETRY: Mass=56754.8; Mass_error=4.9; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:14660666}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}. CC -!- CAUTION: The DNA coding for this protein is not found in the complete CC genome of strain 98/2. Sequence in PubMed:10383958 could have CC originated from another strain. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M34696; AAA72843.1; -; Genomic_DNA. DR EMBL; AF133096; AAD21094.1; -; Genomic_DNA. DR EMBL; AE006641; AAK43121.1; -; Genomic_DNA. DR PIR; B90483; B90483. DR PIR; JQ0767; JQ0767. DR RefSeq; WP_009992676.1; NC_002754.1. DR PDB; 1GOW; X-ray; 2.60 A; A/B=1-489. DR PDB; 1UWI; X-ray; 2.55 A; A/B/C/D=1-489. DR PDB; 1UWQ; X-ray; 2.02 A; A/B=1-489. DR PDB; 1UWR; X-ray; 2.14 A; A/B=1-489. DR PDB; 1UWS; X-ray; 1.95 A; A/B=1-489. DR PDB; 1UWT; X-ray; 1.95 A; A/B=1-489. DR PDB; 1UWU; X-ray; 1.95 A; A/B=1-489. DR PDB; 2CEQ; X-ray; 2.14 A; A/B=1-489. DR PDB; 2CER; X-ray; 2.29 A; A/B=1-489. DR PDB; 4EAM; X-ray; 1.70 A; A/B=1-489. DR PDB; 4EAN; X-ray; 1.75 A; A/B=1-489. DR PDB; 5I3D; X-ray; 2.16 A; A/B/C/D=1-489. DR PDB; 5IXE; X-ray; 1.75 A; A/B=1-489. DR PDB; 7UZ1; X-ray; 1.58 A; A/B=1-489. DR PDB; 7UZ2; X-ray; 1.83 A; A/B=1-489. DR PDBsum; 1GOW; -. DR PDBsum; 1UWI; -. DR PDBsum; 1UWQ; -. DR PDBsum; 1UWR; -. DR PDBsum; 1UWS; -. DR PDBsum; 1UWT; -. DR PDBsum; 1UWU; -. DR PDBsum; 2CEQ; -. DR PDBsum; 2CER; -. DR PDBsum; 4EAM; -. DR PDBsum; 4EAN; -. DR PDBsum; 5I3D; -. DR PDBsum; 5IXE; -. DR PDBsum; 7UZ1; -. DR PDBsum; 7UZ2; -. DR AlphaFoldDB; P22498; -. DR SMR; P22498; -. DR STRING; 273057.SSO3019; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR iPTMnet; P22498; -. DR PaxDb; 273057-SSO3019; -. DR EnsemblBacteria; AAK43121; AAK43121; SSO3019. DR GeneID; 72911572; -. DR KEGG; sso:SSO3019; -. DR PATRIC; fig|273057.12.peg.3113; -. DR eggNOG; arCOG05412; Archaea. DR HOGENOM; CLU_001859_1_3_2; -. DR InParanoid; P22498; -. DR PhylomeDB; P22498; -. DR BRENDA; 3.2.1.23; 6163. DR BRENDA; 3.2.1.55; 6163. DR BRENDA; 3.2.1.B26; 6163. DR BRENDA; 3.2.1.B34; 6163. DR SABIO-RK; P22498; -. DR EvolutionaryTrace; P22498; -. DR PRO; PR:P22498; -. DR Proteomes; UP000001974; Chromosome. DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.80; Glycosidases; 1. 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 NCBIfam; NF041004; Beta_gal_BgaS; 1. DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1. DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1. DR Pfam; PF00232; Glyco_hydro_1; 1. DR PRINTS; PR00131; GLHYDRLASE1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1. DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase; KW Methylation; Reference proteome. FT CHAIN 1..489 FT /note="Beta-galactosidase" FT /id="PRO_0000063867" FT ACT_SITE 206 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 387 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055" FT SITE 76 FT /note="Not N6-methylated" FT SITE 102 FT /note="Not N6-methylated" FT SITE 124 FT /note="Not N6-methylated" FT SITE 138 FT /note="Not N6-methylated" FT MOD_RES 116 FT /note="N6-methyllysine; partial" FT /evidence="ECO:0000269|PubMed:14660666" FT MOD_RES 135 FT /note="N6-methyllysine" FT /evidence="ECO:0000269|PubMed:14660666" FT MOD_RES 273 FT /note="N6-methyllysine; partial" FT /evidence="ECO:0000269|PubMed:14660666" FT MOD_RES 311 FT /note="N6-methyllysine; partial" FT /evidence="ECO:0000269|PubMed:14660666" FT MOD_RES 332 FT /note="N6-methyllysine" FT /evidence="ECO:0000269|PubMed:14660666" FT CONFLICT 235 FT /note="A -> H (in Ref. 1; AAA72843)" FT /evidence="ECO:0000305" FT STRAND 9..13 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 16..19 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 32..38 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 40..44 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 59..72 FT /evidence="ECO:0007829|PDB:4EAM" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 84..87 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 112..121 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 124..139 FT /evidence="ECO:0007829|PDB:4EAM" FT STRAND 143..148 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 160..164 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 177..194 FT /evidence="ECO:0007829|PDB:4EAM" FT TURN 195..197 FT /evidence="ECO:0007829|PDB:4EAM" FT STRAND 199..205 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 207..215 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 218..220 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 229..251 FT /evidence="ECO:0007829|PDB:4EAM" FT STRAND 258..271 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:5IXE" FT HELIX 275..285 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 287..295 FT /evidence="ECO:0007829|PDB:4EAM" FT STRAND 297..299 FT /evidence="ECO:0007829|PDB:1UWT" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:1UWT" FT TURN 308..312 FT /evidence="ECO:0007829|PDB:4EAM" FT STRAND 317..330 FT /evidence="ECO:0007829|PDB:4EAM" FT STRAND 333..336 FT /evidence="ECO:0007829|PDB:4EAM" FT STRAND 338..340 FT /evidence="ECO:0007829|PDB:1GOW" FT STRAND 346..349 FT /evidence="ECO:0007829|PDB:1UWS" FT HELIX 366..379 FT /evidence="ECO:0007829|PDB:4EAM" FT STRAND 383..387 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 398..414 FT /evidence="ECO:0007829|PDB:4EAM" FT STRAND 419..425 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 433..435 FT /evidence="ECO:0007829|PDB:4EAM" FT STRAND 443..446 FT /evidence="ECO:0007829|PDB:4EAM" FT TURN 448..450 FT /evidence="ECO:0007829|PDB:4EAM" FT STRAND 453..455 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 457..468 FT /evidence="ECO:0007829|PDB:4EAM" FT HELIX 473..478 FT /evidence="ECO:0007829|PDB:4EAM" FT STRAND 484..487 FT /evidence="ECO:0007829|PDB:1UWI" SQ SEQUENCE 489 AA; 56692 MW; B56F6CE8EE4A429D CRC64; MYSFPNSFRF GWSQAGFQSE MGTPGSEDPN TDWYKWVHDP ENMAAGLVSG DLPENGPGYW GNYKTFHDNA QKMGLKIARL NVEWSRIFPN PLPRPQNFDE SKQDVTEVEI NENELKRLDE YANKDALNHY REIFKDLKSR GLYFILNMYH WPLPLWLHDP IRVRRGDFTG PSGWLSTRTV YEFARFSAYI AWKFDDLVDE YSTMNEPNVV GGLGYVGVKS GFPPGYLSFE LSRRAMYNII QAHARAYDGI KSVSKKPVGI IYANSSFQPL TDKDMEAVEM AENDNRWWFF DAIIRGEITR GNEKIVRDDL KGRLDWIGVN YYTRTVVKRT EKGYVSLGGY GHGCERNSVS LAGLPTSDFG WEFFPEGLYD VLTKYWNRYH LYMYVTENGI ADDADYQRPY YLVSHVYQVH RAINSGADVR GYLHWSLADN YEWASGFSMR FGLLKVDYNT KRLYWRPSAL VYREIATNGA ITDEIEHLNS VPPVKPLRH //