P53228 (TAL2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transaldolase NQM1
EC=2.2.1.2

Alternative name(s):
Non-quiescent mutant protein 1

Gene names

Name:	NQM1
Ordered Locus Names:	YGR043C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	333 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.
Catalytic activity	Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. Ref.7
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.
Miscellaneous	Present with 1920 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the transaldolase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Pentose shunt
Molecular function	Transferase
PTM	Phosphoprotein
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: InterPro nucleus Inferred from direct assay. Source: SGD
Molecular function	sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity Inferred from direct assay Ref.7. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 333

333

Transaldolase NQM1

PRO_0000173575

Sites

Active site

144

1

By similarity

Amino acid modifications

Modified residue

55

1

Phosphoserine Ref.6

Experimental info

Sequence conflict

290

1

F → S in AAS56158. Ref.3

Secondary structure

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333

Helix Strand Turn

Details...

Helix

15 – 21

7

Beta strand

25 – 29

5

Helix

33 – 35

3

Helix

37 – 39

3

Beta strand

42 – 45

4

Helix

48 – 55

8

Helix

58 – 60

3

Helix

61 – 69

9

Helix

78 – 92

15

Helix

97 – 99

3

Beta strand

105 – 108

4

Helix

111 – 113

3

Helix

117 – 133

17

Helix

138 – 140

3

Beta strand

141 – 146

6

Helix

153 – 161

9

Beta strand

166 – 171

6

Helix

174 – 182

9

Beta strand

186 – 191

6

Helix

195 – 201

7

Turn

209 – 211

3

Helix

216 – 227

12

Beta strand

233 – 237

5

Helix

242 – 248

7

Beta strand

254 – 257

4

Helix

258 – 266

9

Helix

277 – 280

4

Helix

294 – 303

10

Helix

305 – 312

8

Helix

316 – 333

18

Sequences

	Sequence		Length	Mass (Da)
	P53228 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 6492030A7DA3D343	FASTA	333	37,254
	10 20 30 40 50 60 MSEPSEKKQK VATSSLEQLK KAGTHVVADS GDFEAISKYE PQDSTTNPSL ILAASKLEKY 70 80 90 100 110 120 ARFIDAAVEY GRKHGKTDHE KIENAMDKIL VEFGTQILKV VPGRVSTEVD ARLSFDKKAT 130 140 150 160 170 180 VKKALHIIKL YKDAGVPKER VLIKIASTWE GIQAARELEV KHGIHCNMTL LFSFTQAVAC 190 200 210 220 230 240 AEANVTLISP FVGRIMDFYK ALSGKDYTAE TDPGVLSVKK IYSYYKRHGY ATEVMAASFR 250 260 270 280 290 300 NLDELKALAG IDNMTLPLNL LEQLYESTDP IENKLNSESA KEEGVEKVSF INDEPHFRYV 310 320 330 LNEDQMATEK LSDGIRKFSA DIEALYKLVE EKM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII." Rieger M., Brueckner M., Schaefer M., Mueller-Auer S. Yeast 13:1077-1090(1997) [PubMed: 9290212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78. Strain: ATCC 204508 / S288c.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, MASS SPECTROMETRY.
[7]	"The crystal structure and identification of NQM1/YGR043C, a transaldolase from Saccharomyces cerevisiae." Huang H., Rong H., Li X., Tong S., Zhu Z., Niu L., Teng M. Proteins 73:1076-1081(2008) [PubMed: 18831051] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), CATALYTIC ACTIVITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z72828 Genomic DNA. Translation: CAA97042.1.
AY557832 Genomic DNA. Translation: AAS56158.1.
BK006941 Genomic DNA. Translation: DAA08142.1.

PIR

S64337.

RefSeq

NP_011557.1. NM_001181172.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CQ0	X-ray	1.90	A/B	1-333	[»]

ProteinModelPortal

P53228.

SMR

P53228. Positions 12-333.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-2491894.

STRING

P53228.

Proteomic databases

PeptideAtlas

P53228.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGR043C; YGR043C; YGR043C.

GeneID

852934.

KEGG

sce:YGR043C.

NMPDR

fig|4932.3.peg.2673.

Organism-specific databases

CYGD

YGR043c.

SGD

S000003275. YGR043C.

Phylogenomic databases

eggNOG

fuNOG07388.

HOGENOM

HBG286747.

OMA

FINDEPH.

OrthoDB

EOG4XWK6K.

Gene expression databases

ArrayExpress

P53228.

Genevestigator

P53228.

GermOnline

YGR043C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_1.
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

TIGR00874. TalAB. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

NextBio

972666.

Entry information

Entry name

TAL2_YEAST

Accession

Primary (citable) accession number: P53228
Secondary accession number(s): D6VUI1, Q6Q5P8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program