P0A870 (TALB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transaldolase B
EC=2.2.1.2

Gene names

Name:	talB
Synonyms:	yaaK
Ordered Locus Names:	b0008, JW0007

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. HAMAP-Rule MF_00492
Catalytic activity	Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. HAMAP-Rule MF_00492
Pathway	Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3. HAMAP-Rule MF_00492
Subunit structure	Homodimer. Ref.9
Subcellular location	Cytoplasm Probable HAMAP-Rule MF_00492.
Sequence similarities	Belongs to the transaldolase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Pentose shunt
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	pentose-phosphate shunt Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6 Ref.7

Chain

2 – 317

316

Transaldolase B HAMAP-Rule MF_00492

PRO_0000173593

Sites

Active site

132

1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

317

Helix Strand Turn

Details...

Helix

4 – 8

5

Turn

9 – 11

3

Beta strand

12 – 19

8

Helix

21 – 27

7

Beta strand

30 – 33

4

Helix

36 – 42

7

Helix

46 – 48

3

Helix

49 – 62

14

Helix

66 – 86

21

Beta strand

93 – 96

4

Helix

99 – 101

3

Helix

105 – 121

17

Helix

126 – 128

3

Beta strand

129 – 134

6

Helix

137 – 148

12

Beta strand

153 – 158

6

Helix

161 – 169

9

Beta strand

173 – 179

7

Helix

180 – 188

9

Beta strand

189 – 191

3

Helix

197 – 199

3

Helix

201 – 215

15

Beta strand

221 – 225

5

Helix

230 – 235

6

Turn

236 – 238

3

Beta strand

239 – 244

6

Helix

246 – 254

9

Beta strand

255 – 257

3

Helix

278 – 286

9

Helix

289 – 314

26

Sequences

	Sequence		Length	Mass (Da)
	P0A870 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 2DF03D741E576C31	FASTA	317	35,219
	10 20 30 40 50 60 MTDKLTSLRQ YTTVVADTGD IAAMKLYQPQ DATTNPSLIL NAAQIPEYRK LIDDAVAWAK 70 80 90 100 110 120 QQSNDRAQQI VDATDKLAVN IGLEILKLVP GRISTEVDAR LSYDTEASIA KAKRLIKLYN 130 140 150 160 170 180 DAGISNDRIL IKLASTWQGI RAAEQLEKEG INCNLTLLFS FAQARACAEA GVFLISPFVG 190 200 210 220 230 240 RILDWYKANT DKKEYAPAED PGVVSVSEIY QYYKEHGYET VVMGASFRNI GEILELAGCD 250 260 270 280 290 300 RLTIAPALLK ELAESEGAIE RKLSYTGEVK ARPARITESE FLWQHNQDPM AVDKLAEGIR 310 KFAIDQEKLE KMIGDLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains." Sprenger G.A., Schorken U., Sprenger G., Sahm H. J. Bacteriol. 177:5930-5936(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Iida A., Teshiba S., Mizobuchi K. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. Submitted (SEP-1994) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[8]	Sprenger G.A. Unpublished observations (JUN-1993) Cited for: PRESENCE OF TWO TRANSALDOLASES IN E.COLI.
[9]	"Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the alpha/beta barrel within the class I aldolase family." Jia J., Huang W., Schoerken U., Sham H., Sprenger G.A., Lindqvist Y., Schneider G. Structure 4:715-724(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS), SUBUNIT.
[10]	"Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: mechanistic implications for class I aldolases." Jia J., Schorken U., Lindqvist Y., Sprenger G.A., Schneider G. Protein Sci. 6:119-124(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[11]	"Identification of catalytically important residues in the active site of Escherichia coli transaldolase." Schorken U., Thorell S., Schurmann M., Jia J., Sprenger G.A., Schneider G. Eur. J. Biochem. 268:2408-2415(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS). Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[12]	"Redesigning the active site of transaldolase TalB from Escherichia coli: new variants with improved affinity towards nonphosphorylated substrates." Schneider S., Gutierrez M., Sandalova T., Schneider G., Clapes P., Sprenger G.A., Samland A.K. ChemBioChem 11:681-690(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Web resources

Wikipedia

Transaldolase B entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D13161 Genomic DNA. Translation: BAA21822.1.
S80045 Genomic DNA. Translation: AAB47022.1.
U00096 Genomic DNA. Translation: AAC73119.1.
AP009048 Genomic DNA. Translation: BAB96586.1.

PIR

S40535.

RefSeq

NP_414549.1. NC_000913.2.
YP_488314.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I2N	X-ray	2.05	A/B	2-317	[»]
1I2O	X-ray	2.05	A/B	2-317	[»]
1I2P	X-ray	2.05	A/B	2-317	[»]
1I2Q	X-ray	2.05	A/B	2-317	[»]
1I2R	X-ray	2.10	A/B	2-317	[»]
1ONR	X-ray	1.87	A/B	2-317	[»]
1UCW	X-ray	2.20	A/B	1-317	[»]
3KOF	X-ray	1.90	A/B	1-317	[»]

ProteinModelPortal

P0A870.

SMR

P0A870. Positions 2-317.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31850N.

IntAct

P0A870. 5 interactions.

STRING

511145.b0008.

PTM databases

PhosSite

P0810439.

2D gel databases

SWISS-2DPAGE

P0A870.

Proteomic databases

PaxDb

P0A870.

PRIDE

P0A870.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73119; AAC73119; b0008.
BAB96586; BAB96586; BAB96586.

GeneID

12932945.
944748.

KEGG

ecj:Y75_p0008.
eco:b0008.

PATRIC

32115111. VBIEscCol129921_0007.

Organism-specific databases

EchoBASE

EB1517.

EcoGene

EG11556. talB.

Phylogenomic databases

eggNOG

COG0176.

HOGENOM

HOG000281234.

KO

K00616.

OMA

EYKPQDA.

ProtClustDB

PRK05269.

Enzyme and pathway databases

BioCyc

ECOL316407:JW0007-MONOMER.

UniPathway

UPA00115; UER00414.

Gene expression databases

Genevestigator

P0A870.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

HAMAP

MF_00492. Transaldolase_1.

InterPro

IPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view]

PANTHER

PTHR10683. PTHR10683. 1 hit.

Pfam

PF00923. Transaldolase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00874. talAB. 1 hit.

PROSITE

PS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A870.

Entry information

Entry name

TALB_ECOLI

Accession

Primary (citable) accession number: P0A870
Secondary accession number(s): P30148

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program