BGAL_SACS2
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 25-MAY-2022, entry version 158.
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; Crenarchaeota; 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}.
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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 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 AlphaFoldDB; P22498; -.
DR SMR; P22498; -.
DR STRING; 273057.SSO3019; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR iPTMnet; P22498; -.
DR PRIDE; P22498; -.
DR EnsemblBacteria; AAK43121; AAK43121; SSO3019.
DR GeneID; 44128742; -.
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 OMA; VEACDRK; -.
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 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; 1.
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 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
