Reviewed, UniProtKB/Swiss-Prot Q9X108 (BGLT_THEMA)

Names and origin

Protein names

Recommended name:
    6-phospho-beta-glucosidase bglT
    EC=3.2.1.86

Gene names

Name:	bglT
Ordered Locus Names:	TM_1281

Organism

Thermotoga maritima [Complete proteome] [HAMAP]

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	415 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes cellobiose 6'-phosphate into glucose 6-phosphate (Glc6P) and glucose.
Catalytic activity	6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate.
Cofactor	Binds 1 NAD per subunit. Binds 1 manganese ion per subunit.
Subunit structure	Homodimer or homotetramer. Exists in a homodimer/homotetramer equilibrium state in solution.
Miscellaneous	Is a retaining glucosidase as it hydrolyzes glycosidic bond with retention of anomeric configuration. Reaction mechanism includes redox steps involving NAD and stabilization of intermediates by Mn2+.
Sequence similarities	Belongs to the glycosyl hydrolase 4 family.
biophysicochemical properties	Kinetic parameters: KM=41 µM for p-nitrophenyl-beta-D-glucopyranoside 6-phosphate pH dependence: Optimum pH is 8.0. Active from pH 6.5 to 10.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	Manganese Metal-binding NAD
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	6-phospho-beta-glucosidase activity Inferred from electronic annotation. Source: EC manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 415

415

6-phospho-beta-glucosidase bglT

PRO_0000169857

Regions

Nucleotide binding

1 – 64

64

NAD

Sites

Active site

241

1

Proton acceptor

Metal binding

162

1

Manganese

Metal binding

192

1

Manganese

Binding site

87

1

Substrate

Binding site

140

1

Substrate

Binding site

163

1

Substrate

Binding site

261

1

Substrate

Site

103

1

Increases basicity of active site Tyr By similarity

Secondary structure

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415

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Helix

13 – 23

11

Turn

24 – 26

3

Beta strand

31 – 35

5

Helix

39 – 53

15

Beta strand

56 – 61

6

Helix

65 – 69

5

Beta strand

73 – 77

5

Helix

83 – 92

10

Helix

93 – 97

5

Beta strand

103 – 105

3

Helix

107 – 129

23

Beta strand

134 – 137

4

Beta strand

139 – 141

3

Helix

142 – 151

10

Beta strand

156 – 160

5

Helix

164 – 175

12

Helix

180 – 182

3

Beta strand

183 – 190

8

Beta strand

193 – 201

9

Helix

207 – 214

8

Helix

228 – 234

7

Beta strand

236 – 238

3

Helix

240 – 242

3

Helix

243 – 246

4

Helix

248 – 256

9

Helix

261 – 276

16

Helix

284 – 288

5

Turn

290 – 293

4

Helix

294 – 306

13

Beta strand

307 – 309

3

Beta strand

311 – 318

8

Beta strand

331 – 339

9

Beta strand

342 – 346

5

Helix

353 – 374

22

Helix

378 – 387

10

Helix

394 – 407

14

Turn

408 – 411

4

Sequences

	Sequence		Length	Mass (Da)
	Q9X108-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: FB4E3B358245BFEE	FASTA	415	47,627
	10 20 30 40 50 60 MRIAVIGGGS SYTPELVKGL LDISEDVRID EVIFYDIDEE KQKIVVDFVK RLVKDRFKVL 70 80 90 100 110 120 ISDTFEGAVV DAKYVIFQFR PGGLKGREND EGIPLKYGLI GQETTGVGGF SAALRAFPIV 130 140 150 160 170 180 EEYVDTVRKT SNATIVNFTN PSGHITEFVR NYLEYEKFIG LCNVPINFIR EIAEMFSARL 190 200 210 220 230 240 EDVFLKYYGL NHLSFIEKVF VKGEDVTEKV FENLKLKLSN IPDEDFPTWF YDSVRLIVNP 250 260 270 280 290 300 YLRYYLMEKK MFKKISTHEL RAREVMKIEK ELFEKYRTAV EIPEELTKRG GSMYSTAAAH 310 320 330 340 350 360 LIRDLETDEG KIHIVNTRNN GSIENLPDDY VLEIPCYVRS GRVHTLSQGK GDHFALSFIH 370 380 390 400 410 AVKMYERLTI EAYLKRSKKL ALKALLSHPL GPDVEDAKDL LEEILEANRE YVKLG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 beta-glycosidase from Thermotoga maritima." Yip V.L.Y., Varrot A., Davies G.J., Rajan S.S., Yang X., Thompson J., Anderson W.F., Withers S.G. J. Am. Chem. Soc. 126:8354-8355(2004) [PubMed: 15237973] [Abstract] Cited for: CHARACTERIZATION, REACTION MECHANISM. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]	"NAD(+) and metal-ion dependent hydrolysis by family 4 glycosidases: structural insight into specificity for phospho-beta-D-glucosides." Varrot A., Yip V.L.Y., Li Y., Rajan S.S., Yang X., Anderson W.F., Thompson J., Withers S.G., Davies G.J. J. Mol. Biol. 346:423-435(2005) [PubMed: 15670594] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH NAD(+) AND GLUCOSE-6-PHOSPHATE.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE000512 Genomic DNA. Translation: AAD36356.1.

PIR

E72273.

RefSeq

NP_229086.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UP4	X-ray	2.85	A/B/C/D/E/F/G/H	1-415	[»]
1UP6	X-ray	2.55	A/B/C/D/E/F/G/H	1-415	[»]
1UP7	X-ray	2.40	A/B/C/D/E/F/G/H	1-415	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH4. Glycoside Hydrolase Family 4.

Genome annotation databases

GeneID

898202.

GenomeReviews

Gene locus TM_1281 in contig AE000512_GR.

KEGG

tma:TM1281.

NMPDR

fig|243274.1.peg.1270.

TIGR

TM_1281.

Phylogenomic databases

HOGENOM

Q9X108.

OMA

Q9X108. AKLDIIF.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_1281-MON.

BRENDA

3.2.1.86. 16699.

Family and domain databases

InterPro

IPR019802. GlycHydrolase_4_CS.
IPR001088. Glyco_hydro_4.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
[Graphical view]

Gene3D

G3DSA:3.90.110.10. lact_mal_DH. 1 hit.

Pfam

PF02056. Glyco_hydro_4. 1 hit.
[Graphical view]

PRINTS

PR00732. GLHYDRLASE4.

ProDom

PD006892. Glyco_hydro_4. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS01324. GLYCOSYL_HYDROL_F4. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BGLT_THEMA

Accession

Primary (citable) accession number: Q9X108

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	November 1, 1999
Last modified:	June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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