Skip Header

Contribute Send feedback
Read comments (?) or add your own

A4QEF1 (A4QEF1_CORGB) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Transaldolase HAMAP MF_00493
EC=2.2.1.2 HAMAP MF_00493
Gene names
Name:tal HAMAP MF_00493
Ordered Locus Names:cgR_1625
OrganismCorynebacterium glutamicum (strain R) [Complete proteome] [HAMAP]
Taxonomic identifier340322 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway By similarity. HAMAP MF_00493 SAAS SAAS001585

Catalytic activity

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. HAMAP MF_00493 SAAS SAAS001585

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_00493 SAAS SAAS001585

Subcellular location

Cytoplasm By similarity HAMAP MF_00493.

Sequence similarities

Belongs to the transaldolase family. Type 2 subfamily. HAMAP MF_00493

Ontologies

Keywords
   Biological processPentose shunt HAMAP MF_00493 SAAS SAAS001585
   Cellular componentCytoplasm HAMAP MF_00493 SAAS SAAS001585
   Molecular functionTransferase HAMAP MF_00493 SAAS SAAS001585
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpentose-phosphate shunt

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionsedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1391 By similarity HAMAP MF_00493

Sequences

Sequence LengthMass (Da)Tools
A4QEF1 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: B9AD31F246D55422

FASTA36038,314
        10         20         30         40         50         60 
MSHIDDLAQL GTSTWLDDLS RERITSGNLS QVIEEKSVVG VTTNPAIFAA AMSKGDSYDA 

        70         80         90        100        110        120 
QIAELKAAGA SVDQAVYAMS IDDVRNACDL FTGIFESSNG YDGRVSIEVD PRISADRDAT 

       130        140        150        160        170        180 
LAQAKELWAK VDRPNVMIKI PATPGSLPAI TDALAEGISV NVTLIFSVAR YREVIAAFIE 

       190        200        210        220        230        240 
GIKQAAANGH DVSKIHSVAS FFVSRVDVEI DKRLEAIGSD EALALRGKAG VANAQRAYAV 

       250        260        270        280        290        300 
YKELFDAAEL PEGANTQRPL WASTGVKNPA YAATLYVSEL AGPNTVNTMP EGTIDAVLEL 

       310        320        330        340        350        360 
GNLHGDTLSN SAAEADAVFS QLEALGVDLA DVFQVLETEG VDKFVASWSE LLESMEARLK

« Hide

References

[1]"Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R."
Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.
Microbiology 153:1042-1058(2007) [PubMed: 17379713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009044 Genomic DNA. Translation: BAF54617.1.
RefSeqYP_001138519.1. NC_009342.1.

3D structure databases

ProteinModelPortalA4QEF1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4QEF1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4994409.
GenomeReviewsGene locus cgR_1625 in contig AP009044_GR.
KEGGcgt:cgR_1625.
PATRIC21507846. VBICorGlu58097_1674.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0176.
HOGENOMHBG321149.
OMAMPEKTLD.
ProtClustDBPRK03343.

Family and domain databases

HAMAPMF_00493. Transaldolase_2.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004732. Transaldolase_2.
IPR018225. Transaldolase_AS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK00616.
PANTHERPTHR10683. Transaldolase. 1 hit.
PfamPF00923. Transaldolase. 1 hit.
[Graphical view]
PIRSFPIRSF036915. Trnald_Bac_Plnt. 1 hit.
TIGRFAMsTIGR00876. Tal_mycobact. 1 hit.
PROSITEPS01054. TRANSALDOLASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA4QEF1_CORGB
AccessionPrimary (citable) accession number: A4QEF1
Entry history
Integrated into UniProtKB/TrEMBL: May 15, 2007
Last sequence update: May 15, 2007
Last modified: January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info