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Reviewed, UniProtKB/Swiss-Prot P48993 (TAL2_ANASP)

Last modified November 3, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Transaldolase 2
    EC=2.2.1.2
Gene names
Name: tal2
Ordered Locus Names: all4020
OrganismAnabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

Catalytic activity

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

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

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the transaldolase family. Type 2 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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontransaldolase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 381381Transaldolase 2 HAMAP MF_00493
PRO_0000173628

Sites

Active site1411 By similarity

Experimental info

Sequence conflict15 – 162SI → MY in AAA98852. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P48993-1 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 1A016AD8B486311A

FASTA38142,023
        10         20         30         40         50         60 
MAINHLLEIK EYGQSIWMDN LSRDIIQSGE LKNLVENQGI CGITSNPAIF EKAIANNVIY 

        70         80         90        100        110        120 
DADIEAGVRA GLPTYKIYES LIFADIRNAC DILRPVYEAS NKLDGYVSIE VPPTIAHDTQ 

       130        140        150        160        170        180 
ATINEARRYY QEIGRENVMI KIPGTEAGLP AVEQVIAEGI NVNVTLLFSV QSYINTIWAY 

       190        200        210        220        230        240 
IRGLEKRLAE GKDISQIASV ASFFLSRIDI NIDGKIDAKL ARGVDDISLE AKLMVVKGKV 

       250        260        270        280        290        300 
AIANAKIAYQ EYKKIIESDQ WQALAAKGAK VQRLLWASTS TKDPNYSDVM YVDELIGPDT 

       310        320        330        340        350        360 
VNTLPPATIT ACADHCEVAN RVETGVAEAY QLIESLKDPD INIDINAVMD ELLIEGINKF 

       370        380 
VQPFQSLMNS LEGKVKLLSP V 

« Hide

References

« Hide 'large scale' references
[1]"A comparison of gene organization in the zwf region of the genomes of the cyanobacteria Synechococcus sp. PCC 7942 and Anabaena sp. PCC 7120."
Newman J., Karakaya H., Scanlan D.J., Mann N.H.
FEMS Microbiol. Lett. 133:187-193(1995) [PubMed: 8566707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

U33282 Genomic DNA. Translation: AAA98852.1.
BA000019 Genomic DNA. Translation: BAB75719.1.
PIRAE2308.
RefSeqNP_488060.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP48993.

Genome annotation databases

GeneID1107618.
GenomeReviewsGene locus all4020 in contig BA000019_GR.
KEGGana:all4020.
NMPDRfig|103690.1.peg.4327.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP48993.
OMAMPEKTLD.

Enzyme and pathway databases

BioCycNSP103690:ALL4020-MON.

Family and domain databases

HAMAPMF_00493.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR004732. Tal_mycobact.
IPR001585. Transaldolase.
IPR018225. Transaldolase_AS.
IPR014634. Transaldolase_Bac/Pln.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
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.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTAL2_ANASP
AccessionPrimary (citable) accession number: P48993
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2002
Last modified: November 3, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents