Reviewed, UniProtKB/Swiss-Prot P22498 (BGAL_SULSO)

Names and origin

Protein names

Recommended name:
    Beta-galactosidase
      Short name=Lactase
    EC=3.2.1.23

Gene names

Name:	lacS
Ordered Locus Names:	SSO3019

Organism

Sulfolobus solfataricus [Complete proteome] [HAMAP]

Taxonomic identifier

2287 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

Protein attributes

Sequence length	489 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the glycosyl hydrolase 1 family.
Mass spectrometry	Molecular mass is 56754.8±4.9 Da from positions 1 - 489. Determined by ESI. Ref.4

Ontologies

Keywords
Molecular function	Glycosidase Hydrolase
PTM	Methylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	beta-galactosidase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 489

489

Beta-galactosidase

PRO_0000063867

Sites

Active site

206

1

Proton donor Potential

Active site

387

1

Nucleophile By similarity

Site

76

1

Not N6-methylated

Site

102

1

Not N6-methylated

Site

124

1

Not N6-methylated

Site

138

1

Not N6-methylated

Amino acid modifications

Modified residue

116

1

N6-methyllysine; partial Ref.4

Modified residue

135

1

N6-methyllysine Ref.4

Modified residue

273

1

N6-methyllysine; partial Ref.4

Modified residue

311

1

N6-methyllysine; partial Ref.4

Modified residue

332

1

N6-methyllysine Ref.4

Experimental info

Sequence conflict

235

1

A → H in AAA72843. Ref.1

Secondary structure

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489

Helix Strand Turn

Details...

Beta strand

9 – 13

5

Helix

16 – 19

4

Helix

32 – 38

7

Helix

40 – 44

5

Helix

53 – 55

3

Helix

59 – 72

14

Beta strand

77 – 81

5

Helix

84 – 87

4

Helix

112 – 121

10

Helix

124 – 139

16

Beta strand

143 – 151

9

Turn

155 – 157

3

Helix

160 – 164

5

Helix

173 – 175

3

Helix

177 – 194

18

Turn

195 – 197

3

Beta strand

199 – 205

7

Helix

207 – 215

9

Helix

218 – 220

3

Helix

229 – 251

23

Beta strand

258 – 271

14

Helix

275 – 285

11

Helix

287 – 295

9

Beta strand

297 – 299

3

Beta strand

304 – 306

3

Turn

308 – 312

5

Beta strand

317 – 329

13

Beta strand

331 – 336

6

Helix

366 – 379

14

Beta strand

383 – 387

5

Helix

398 – 414

17

Beta strand

419 – 425

7

Helix

433 – 435

3

Beta strand

443 – 446

4

Turn

448 – 450

3

Beta strand

453 – 455

3

Helix

457 – 468

12

Helix

473 – 478

6

Sequences

	Sequence		Length	Mass (Da)
	P22498-1 [UniParc]. Last modified June 20, 2001. Version 2. Checksum: B56F6CE8EE4A429D	FASTA	489	56,692
	10 20 30 40 50 60 MYSFPNSFRF GWSQAGFQSE MGTPGSEDPN TDWYKWVHDP ENMAAGLVSG DLPENGPGYW 70 80 90 100 110 120 GNYKTFHDNA QKMGLKIARL NVEWSRIFPN PLPRPQNFDE SKQDVTEVEI NENELKRLDE 130 140 150 160 170 180 YANKDALNHY REIFKDLKSR GLYFILNMYH WPLPLWLHDP IRVRRGDFTG PSGWLSTRTV 190 200 210 220 230 240 YEFARFSAYI AWKFDDLVDE YSTMNEPNVV GGLGYVGVKS GFPPGYLSFE LSRRAMYNII 250 260 270 280 290 300 QAHARAYDGI KSVSKKPVGI IYANSSFQPL TDKDMEAVEM AENDNRWWFF DAIIRGEITR 310 320 330 340 350 360 GNEKIVRDDL KGRLDWIGVN YYTRTVVKRT EKGYVSLGGY GHGCERNSVS LAGLPTSDFG 370 380 390 400 410 420 WEFFPEGLYD VLTKYWNRYH LYMYVTENGI ADDADYQRPY YLVSHVYQVH RAINSGADVR 430 440 450 460 470 480 GYLHWSLADN YEWASGFSMR FGLLKVDYNT KRLYWRPSAL VYREIATNGA ITDEIEHLNS VPPVKPLRH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2121622] [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: 10383958] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 98/2.
[3]	"The complete genome of the crenarchaeon Sulfolobus solfataricus P2." She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J. Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed: 11427726] [Abstract] 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: 14660666] [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: 9299327] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). Strain: DSM 5833 / MT-4.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M34696 Genomic DNA. Translation: AAA72843.1.
AF133096 Genomic DNA. Translation: AAD21094.1.
AE006641 Genomic DNA. Translation: AAK43121.1.

PIR

B90483.
JQ0767.

RefSeq

NP_344331.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GOW	X-ray	2.60	A/B	1-489	[»]
1UWI	X-ray	2.55	A/B/C/D	1-489	[»]
1UWQ	X-ray	2.02	A/B	1-489	[»]
1UWR	X-ray	2.14	A/B	1-489	[»]
1UWS	X-ray	1.95	A/B	1-489	[»]
1UWT	X-ray	1.95	A/B	1-489	[»]
1UWU	X-ray	1.95	A/B	1-489	[»]
2CEQ	X-ray	2.14	A/B	1-489	[»]
2CER	X-ray	2.29	A/B	1-489	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH1. Glycoside Hydrolase Family 1.

Genome annotation databases

GeneID

1453040.

GenomeReviews

Gene locus SSO3019 in contig AE006641_GR.

KEGG

sso:SSO3019.

NMPDR

fig|273057.1.peg.2754.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P22498.

OMA

P22498. GFQSEMG.

Enzyme and pathway databases

BioCyc

SSOL273057:SSO3019-MON.

BRENDA

3.2.1.23. 2070.

Family and domain databases

InterPro

IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

PANTHER

PTHR10353. Glyco_hydro_1. 1 hit.

Pfam

PF00232. Glyco_hydro_1. 2 hits.
[Graphical view]

PRINTS

PR00131. GLHYDRLASE1.

PROSITE

PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BGAL_SULSO

Accession

Primary (citable) accession number: P22498
Secondary accession number(s): Q9V2Z5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	June 20, 2001
Last modified:	June 16, 2009
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)