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Protein

Transaldolase NQM1

Gene

NQM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.

Catalytic activityi

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.PROSITE-ProRule annotation1 Publication

Pathwayi: pentose phosphate pathway

This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Transaldolase (TAL1), Transaldolase NQM1 (NQM1)
  3. no protein annotated in this organism
This subpathway is part of the pathway pentose phosphate pathway, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei144 – 1441Schiff-base intermediate with substratePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • cellular response to oxidative stress Source: SGD
  • chronological cell aging Source: SGD
  • pentose-phosphate shunt Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pentose shunt

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciYEAST:YGR043C-MONOMER.
BRENDAi2.2.1.2. 984.
ReactomeiR-SCE-163754. Insulin effects increased synthesis of Xylulose-5-Phosphate.
R-SCE-71336. Pentose phosphate pathway (hexose monophosphate shunt).
UniPathwayiUPA00115; UER00414.

Names & Taxonomyi

Protein namesi
Recommended name:
Transaldolase NQM1 (EC:2.2.1.2)
Alternative name(s):
Non-quiescent mutant protein 1
Gene namesi
Name:NQM1
Ordered Locus Names:YGR043C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR043C.
SGDiS000003275. NQM1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333Transaldolase NQM1PRO_0000173575Add
BLAST

Proteomic databases

MaxQBiP53228.
PeptideAtlasiP53228.
PRIDEiP53228.

PTM databases

iPTMnetiP53228.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi33290. 26 interactions.
MINTiMINT-2491894.

Structurei

Secondary structure

1
333
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 217Combined sources
Beta strandi25 – 295Combined sources
Helixi33 – 353Combined sources
Helixi37 – 393Combined sources
Beta strandi42 – 454Combined sources
Helixi48 – 558Combined sources
Helixi58 – 603Combined sources
Helixi61 – 7414Combined sources
Helixi78 – 9821Combined sources
Beta strandi105 – 1084Combined sources
Helixi111 – 1133Combined sources
Helixi117 – 13317Combined sources
Helixi138 – 1403Combined sources
Beta strandi141 – 1466Combined sources
Helixi149 – 16214Combined sources
Beta strandi166 – 1716Combined sources
Helixi174 – 1829Combined sources
Beta strandi186 – 1927Combined sources
Helixi193 – 2019Combined sources
Turni209 – 2113Combined sources
Helixi213 – 22816Combined sources
Beta strandi233 – 2375Combined sources
Helixi242 – 2487Combined sources
Beta strandi251 – 2577Combined sources
Helixi258 – 2669Combined sources
Helixi277 – 2804Combined sources
Helixi281 – 2833Combined sources
Helixi294 – 30310Combined sources
Helixi305 – 33329Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CQ0X-ray1.90A/B1-333[»]
ProteinModelPortaliP53228.
SMRiP53228. Positions 12-333.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53228.

Family & Domainsi

Sequence similaritiesi

Belongs to the transaldolase family. Type 1 subfamily.Curated

Phylogenomic databases

GeneTreeiENSGT00390000017361.
HOGENOMiHOG000281234.
InParanoidiP53228.
KOiK00616.
OMAiKILIMAN.
OrthoDBiEOG7N905G.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001585. TAL/FSA.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERiPTHR10683. PTHR10683. 1 hit.
PfamiPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00874. talAB. 1 hit.
PROSITEiPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53228-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEPSEKKQK VATSSLEQLK KAGTHVVADS GDFEAISKYE PQDSTTNPSL
60 70 80 90 100
ILAASKLEKY ARFIDAAVEY GRKHGKTDHE KIENAMDKIL VEFGTQILKV
110 120 130 140 150
VPGRVSTEVD ARLSFDKKAT VKKALHIIKL YKDAGVPKER VLIKIASTWE
160 170 180 190 200
GIQAARELEV KHGIHCNMTL LFSFTQAVAC AEANVTLISP FVGRIMDFYK
210 220 230 240 250
ALSGKDYTAE TDPGVLSVKK IYSYYKRHGY ATEVMAASFR NLDELKALAG
260 270 280 290 300
IDNMTLPLNL LEQLYESTDP IENKLNSESA KEEGVEKVSF INDEPHFRYV
310 320 330
LNEDQMATEK LSDGIRKFSA DIEALYKLVE EKM
Length:333
Mass (Da):37,254
Last modified:October 1, 1996 - v1
Checksum:i6492030A7DA3D343
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti290 – 2901F → S in AAS56158 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72828 Genomic DNA. Translation: CAA97042.1.
AY557832 Genomic DNA. Translation: AAS56158.1.
BK006941 Genomic DNA. Translation: DAA08142.1.
PIRiS64337.
RefSeqiNP_011557.1. NM_001181172.1.

Genome annotation databases

EnsemblFungiiYGR043C; YGR043C; YGR043C.
GeneIDi852934.
KEGGisce:YGR043C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72828 Genomic DNA. Translation: CAA97042.1.
AY557832 Genomic DNA. Translation: AAS56158.1.
BK006941 Genomic DNA. Translation: DAA08142.1.
PIRiS64337.
RefSeqiNP_011557.1. NM_001181172.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CQ0X-ray1.90A/B1-333[»]
ProteinModelPortaliP53228.
SMRiP53228. Positions 12-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33290. 26 interactions.
MINTiMINT-2491894.

PTM databases

iPTMnetiP53228.

Proteomic databases

MaxQBiP53228.
PeptideAtlasiP53228.
PRIDEiP53228.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR043C; YGR043C; YGR043C.
GeneIDi852934.
KEGGisce:YGR043C.

Organism-specific databases

EuPathDBiFungiDB:YGR043C.
SGDiS000003275. NQM1.

Phylogenomic databases

GeneTreeiENSGT00390000017361.
HOGENOMiHOG000281234.
InParanoidiP53228.
KOiK00616.
OMAiKILIMAN.
OrthoDBiEOG7N905G.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00414.
BioCyciYEAST:YGR043C-MONOMER.
BRENDAi2.2.1.2. 984.
ReactomeiR-SCE-163754. Insulin effects increased synthesis of Xylulose-5-Phosphate.
R-SCE-71336. Pentose phosphate pathway (hexose monophosphate shunt).

Miscellaneous databases

EvolutionaryTraceiP53228.
PROiP53228.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001585. TAL/FSA.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERiPTHR10683. PTHR10683. 1 hit.
PfamiPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00874. talAB. 1 hit.
PROSITEiPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiTAL2_YEAST
AccessioniPrimary (citable) accession number: P53228
Secondary accession number(s): D6VUI1, Q6Q5P8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1920 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.