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P51778 (TAL_ANAVT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Transaldolase

EC=2.2.1.2
Gene names
Name:tal
Ordered Locus Names:Ava_0493
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length332 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_00492

Catalytic activity

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. HAMAP 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 MF_00492

Subcellular location

Cytoplasm By similarity HAMAP MF_00492.

Sequence similarities

Belongs to the transaldolase family. Type 1 subfamily.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Transaldolase HAMAP MF_00492
PRO_0000173578

Sites

Active site1361 By similarity

Experimental info

Sequence conflict2041D → Y in AAC41527. Ref.1
Sequence conflict3091T → S in AAC41527. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P51778 [UniParc].

Last modified April 4, 2006. Version 2.
Checksum: 3536377CFEA0D692

FASTA33236,165
        10         20         30         40         50         60 
MTKNLLEQLR EMTVVVADTG DIQAIEKFTP RDATTNPSLI TAAAKMPEYQ EIVDQTLLQA 

        70         80         90        100        110        120 
KKDAGAGASK GQIVSLAFDR LAVSFGLKIL QIIPGRVSTE VDARLSYDTE ATITKARELI 

       130        140        150        160        170        180 
AQYKAAGIGP ERVLIKIAST WEGIKAAEIL EKEGIHCNLT LLFGLHQAIA CAEAGITLIS 

       190        200        210        220        230        240 
PFVGRILDWY KKETGRDSYP SAEDPGVISV TTIYNYYKKF GYTTEVMGAS FRNIGEITEL 

       250        260        270        280        290        300 
AGSDLLTISP GLLGELQATI GELPRKLDPA KAATLDIEKI SIDKATFDKM HAADRMAYDK 

       310        320        330 
LDEGIKGFTK ALEELETLLA ERLARLEVVA SH 

« Hide

References

« Hide 'large scale' references
[1]"Transaldolase genes from the cyanobacteria Anabaena variabilis and Synechocystis sp. PCC 6803: comparison with other eubacterial and eukaryotic homologues."
Koehler U., Cerff R., Brinkmann H.
Plant Mol. Biol. 30:213-218(1996) [PubMed: 8616240] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29413 / PCC 7937.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L47327 Genomic DNA. Translation: AAC41527.1.
CP000117 Genomic DNA. Translation: ABA20117.1.
PIRS72517.
RefSeqYP_321012.1. NC_007413.1.

3D structure databases

ProteinModelPortalP51778.
SMRP51778. Positions 3-324.
ModBaseSearch...

Protein-protein interaction databases

STRINGP51778.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3682400.
GenomeReviewsGene locus Ava_0493 in contig CP000117_GR.
KEGGava:Ava_0493.
NMPDRfig|240292.3.peg.1851.
PATRIC35421342. VBIAnaVar43351_1243.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0176.
HOGENOMHBG286747.
OMADWHKAKT.
PhylomeDBP51778.
ProtClustDBPRK05269.

Enzyme and pathway databases

BioCycAVAR240292:AVA_0493-MONOMER.

Family and domain databases

HAMAPMF_00492. Transaldolase_1.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_1.
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]
TIGRFAMsTIGR00874. TalAB. 1 hit.
PROSITEPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTAL_ANAVT
AccessionPrimary (citable) accession number: P51778
Secondary accession number(s): Q3MFW9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 4, 2006
Last modified: January 25, 2012
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families