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Protein

Beta-galactosidase

Gene

lacS

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei76 – 761Not N6-methylated
Sitei102 – 1021Not N6-methylated
Sitei124 – 1241Not N6-methylated
Sitei138 – 1381Not N6-methylated
Active sitei206 – 2061Proton donorSequence Analysis
Active sitei387 – 3871NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-2809-MONOMER.
BRENDAi3.2.1.23. 6163.
3.2.1.B26. 6163.
3.2.1.B28. 6163.
SABIO-RKP22498.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactosidase (EC:3.2.1.23)
Short name:
Lactase
Gene namesi
Name:lacS
Ordered Locus Names:SSO3019
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001974 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 489489Beta-galactosidasePRO_0000063867Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei116 – 1161N6-methyllysine; partial1 Publication
Modified residuei135 – 1351N6-methyllysine1 Publication
Modified residuei273 – 2731N6-methyllysine; partial1 Publication
Modified residuei311 – 3111N6-methyllysine; partial1 Publication
Modified residuei332 – 3321N6-methyllysine1 Publication

Keywords - PTMi

Methylation

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi273057.SSO3019.

Structurei

Secondary structure

1
489
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 135Combined sources
Helixi16 – 194Combined sources
Helixi32 – 387Combined sources
Helixi40 – 445Combined sources
Helixi53 – 553Combined sources
Helixi59 – 7214Combined sources
Beta strandi77 – 815Combined sources
Helixi84 – 874Combined sources
Helixi112 – 12110Combined sources
Helixi124 – 13916Combined sources
Beta strandi143 – 1486Combined sources
Helixi155 – 1573Combined sources
Helixi160 – 1645Combined sources
Helixi173 – 1753Combined sources
Helixi177 – 19418Combined sources
Turni195 – 1973Combined sources
Beta strandi199 – 2057Combined sources
Helixi207 – 2159Combined sources
Helixi218 – 2203Combined sources
Helixi229 – 25123Combined sources
Beta strandi258 – 27114Combined sources
Helixi272 – 2743Combined sources
Helixi275 – 28511Combined sources
Helixi287 – 2959Combined sources
Beta strandi297 – 2993Combined sources
Beta strandi304 – 3063Combined sources
Turni308 – 3125Combined sources
Beta strandi317 – 33014Combined sources
Beta strandi333 – 3364Combined sources
Beta strandi338 – 3403Combined sources
Beta strandi346 – 3494Combined sources
Helixi366 – 37914Combined sources
Beta strandi383 – 3875Combined sources
Helixi398 – 41417Combined sources
Beta strandi419 – 4257Combined sources
Helixi433 – 4353Combined sources
Beta strandi443 – 4464Combined sources
Turni448 – 4503Combined sources
Beta strandi453 – 4553Combined sources
Helixi457 – 46812Combined sources
Helixi473 – 4786Combined sources
Beta strandi484 – 4874Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GOWX-ray2.60A/B1-489[»]
1UWIX-ray2.55A/B/C/D1-489[»]
1UWQX-ray2.02A/B1-489[»]
1UWRX-ray2.14A/B1-489[»]
1UWSX-ray1.95A/B1-489[»]
1UWTX-ray1.95A/B1-489[»]
1UWUX-ray1.95A/B1-489[»]
2CEQX-ray2.14A/B1-489[»]
2CERX-ray2.29A/B1-489[»]
4EAMX-ray1.70A/B1-489[»]
4EANX-ray1.75A/B1-489[»]
ProteinModelPortaliP22498.
SMRiP22498. Positions 1-489.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22498.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088630.
InParanoidiP22498.
KOiK01190.
OMAiVGIIYAN.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 2 hits.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22498-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYSFPNSFRF GWSQAGFQSE MGTPGSEDPN TDWYKWVHDP ENMAAGLVSG
60 70 80 90 100
DLPENGPGYW GNYKTFHDNA QKMGLKIARL NVEWSRIFPN PLPRPQNFDE
110 120 130 140 150
SKQDVTEVEI NENELKRLDE YANKDALNHY REIFKDLKSR GLYFILNMYH
160 170 180 190 200
WPLPLWLHDP IRVRRGDFTG PSGWLSTRTV YEFARFSAYI AWKFDDLVDE
210 220 230 240 250
YSTMNEPNVV GGLGYVGVKS GFPPGYLSFE LSRRAMYNII QAHARAYDGI
260 270 280 290 300
KSVSKKPVGI IYANSSFQPL TDKDMEAVEM AENDNRWWFF DAIIRGEITR
310 320 330 340 350
GNEKIVRDDL KGRLDWIGVN YYTRTVVKRT EKGYVSLGGY GHGCERNSVS
360 370 380 390 400
LAGLPTSDFG WEFFPEGLYD VLTKYWNRYH LYMYVTENGI ADDADYQRPY
410 420 430 440 450
YLVSHVYQVH RAINSGADVR GYLHWSLADN YEWASGFSMR FGLLKVDYNT
460 470 480
KRLYWRPSAL VYREIATNGA ITDEIEHLNS VPPVKPLRH
Length:489
Mass (Da):56,692
Last modified:June 20, 2001 - v2
Checksum:iB56F6CE8EE4A429D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti235 – 2351A → H in AAA72843 (PubMed:2121622).Curated

Mass spectrometryi

Molecular mass is 56754.8±4.9 Da from positions 1 - 489. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34696 Genomic DNA. Translation: AAA72843.1.
AF133096 Genomic DNA. Translation: AAD21094.1.
AE006641 Genomic DNA. Translation: AAK43121.1.
PIRiB90483.
JQ0767.
RefSeqiNP_344331.1. NC_002754.1.
WP_009992676.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK43121; AAK43121; SSO3019.
GeneIDi1453040.
KEGGisso:SSO3019.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34696 Genomic DNA. Translation: AAA72843.1.
AF133096 Genomic DNA. Translation: AAD21094.1.
AE006641 Genomic DNA. Translation: AAK43121.1.
PIRiB90483.
JQ0767.
RefSeqiNP_344331.1. NC_002754.1.
WP_009992676.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GOWX-ray2.60A/B1-489[»]
1UWIX-ray2.55A/B/C/D1-489[»]
1UWQX-ray2.02A/B1-489[»]
1UWRX-ray2.14A/B1-489[»]
1UWSX-ray1.95A/B1-489[»]
1UWTX-ray1.95A/B1-489[»]
1UWUX-ray1.95A/B1-489[»]
2CEQX-ray2.14A/B1-489[»]
2CERX-ray2.29A/B1-489[»]
4EAMX-ray1.70A/B1-489[»]
4EANX-ray1.75A/B1-489[»]
ProteinModelPortaliP22498.
SMRiP22498. Positions 1-489.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO3019.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK43121; AAK43121; SSO3019.
GeneIDi1453040.
KEGGisso:SSO3019.

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088630.
InParanoidiP22498.
KOiK01190.
OMAiVGIIYAN.

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-2809-MONOMER.
BRENDAi3.2.1.23. 6163.
3.2.1.B26. 6163.
3.2.1.B28. 6163.
SABIO-RKP22498.

Miscellaneous databases

EvolutionaryTraceiP22498.
PROiP22498.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 2 hits.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequencing of a new beta-galactosidase-encoding archaebacterial gene."
    Cubellis M.V., Rozzo C., Montecucchi P., Rossi M.
    Gene 94:89-94(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-33.
    Strain: DSM 5833 / MT-4.
  2. "Coordinate transcriptional control in the hyperthermophilic archaeon Sulfolobus solfataricus."
    Haseltine C., Montalvo-Rodriguez R., Bini E., Carl A., Blum P.
    J. Bacteriol. 181:3920-3927(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 98/2.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  4. "Thermal stability and aggregation of Sulfolobus solfataricus beta-glycosidase are dependent upon the N-epsilon-methylation of specific lysyl residues: critical role of in vivo post-translational modifications."
    Febbraio F., Andolfo A., Tanfani F., Briante R., Gentile F., Formisano S., Vaccaro C., Scire A., Bertoli E., Pucci P., Nucci R.
    J. Biol. Chem. 279:10185-10194(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-116; LYS-135; LYS-273; LYS-311 AND LYS-332, MASS SPECTROMETRY.
  5. "Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability."
    Aguilar C.F., Sanderson I., Moracci M., Ciaramella M., Nucci R., Rossi M., Pearl L.H.
    J. Mol. Biol. 271:789-802(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
    Strain: DSM 5833 / MT-4.

Entry informationi

Entry nameiBGAL_SULSO
AccessioniPrimary (citable) accession number: P22498
Secondary accession number(s): Q9V2Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 20, 2001
Last modified: July 22, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The DNA coding for this protein is not found in the complete genome of strain 98/2. Sequence in PubMed:10383958 could have originated from another strain.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.