Q9WYD1 (TAL_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transaldolase
EC=2.2.1.2

Gene names

Name:	tal
Ordered Locus Names:	TM_0295

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	218 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. HAMAP MF_00494
Catalytic activity	Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. HAMAP MF_00494
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 MF_00494
Subcellular location	Cytoplasm Probable HAMAP MF_00494.
Sequence similarities	Belongs to the transaldolase family. Type 3B subfamily.

Ontologies

Keywords
Biological process	Pentose shunt
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 218

218

Transaldolase HAMAP MF_00494

PRO_0000173687

Sites

Active site

83

1

By similarity

Secondary structure

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218

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

10 – 18

9

Beta strand

24 – 26

3

Helix

42 – 50

9

Beta strand

54 – 57

4

Helix

63 – 74

12

Beta strand

80 – 87

8

Helix

88 – 99

12

Beta strand

104 – 109

6

Helix

112 – 121

10

Beta strand

124 – 129

6

Helix

130 – 135

6

Helix

140 – 154

15

Beta strand

159 – 164

6

Helix

168 – 177

10

Beta strand

180 – 184

5

Helix

186 – 192

7

Helix

196 – 214

19

Sequences

	Sequence		Length	Mass (Da)
	Q9WYD1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 3FF8B0A85CFA6EFA	FASTA	218	24,213
	10 20 30 40 50 60 MKIFLDTANL EEIKKGVEWG IVDGVTTNPT LISKEGAEFK QRVKEICDLV KGPVSAEVVS 70 80 90 100 110 120 LDYEGMVREA RELAQISEYV VIKIPMTPDG IKAVKTLSAE GIKTNVTLVF SPAQAILAAK 130 140 150 160 170 180 AGATYVSPFV GRMDDLSNDG MRMLGEIVEI YNNYGFETEI IAASIRHPMH VVEAALMGVD 190 200 210 IVTMPFAVLE KLFKHPMTDL GIERFMEDWK KYLENLKK

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]	"Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia coli and is related to a novel group of bacterial transaldolases." Schuermann M., Sprenger G.A. J. Biol. Chem. 276:11055-11061(2001) [PubMed: 11120740] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000512 Genomic DNA. Translation: AAD35383.1.

PIR

G72394.

RefSeq

NP_228107.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VPX	X-ray	2.40	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T	1-218	[»]

ProteinModelPortal

Q9WYD1.

SMR

Q9WYD1. Positions 1-215.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

897220.

GenomeReviews

Gene locus TM_0295 in contig AE000512_GR.

KEGG

tma:TM0295.

NMPDR

fig|243274.1.peg.291.

PATRIC

23935469. VBITheMar51294_0300.

TIGR

TM_0295.

Phylogenomic databases

HOGENOM

HBG533000.

OMA

KVNVTLC.

PhylomeDB

Q9WYD1.

ProtClustDB

PRK01362.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_0295-MONOMER.

Family and domain databases

HAMAP

MF_00494. Transaldolase_3b.
[Tree]

InterPro

IPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004731. Transaldolase_3A/3B.
IPR022999. Transaldolase_3B.
IPR018225. Transaldolase_AS.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

KO

K00616.

PANTHER

PTHR10683. Transaldolase. 1 hit.

Pfam

PF00923. Transaldolase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00875. Fsa_talC_mipB. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

TAL_THEMA

Accession

Primary (citable) accession number: Q9WYD1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program