Q829U5 (TAL2_STRAW) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transaldolase 2
EC=2.2.1.2

Gene names

Name:	tal2
Ordered Locus Names:	SAV_6314

Organism

Streptomyces avermitilis [Complete proteome] [HAMAP]

Taxonomic identifier

33903 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway By similarity. HAMAP MF_00493
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 By similarity HAMAP MF_00493.
Sequence similarities	Belongs to the transaldolase family. Type 2 subfamily.

Ontologies

Keywords
Biological process	Pentose shunt
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 372	372	Transaldolase 2 HAMAP MF_00493		PRO_0000173640
Sites
	Active site	140	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q829U5 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: FD4345F1E019AEB3	FASTA	372	40,667
	10 20 30 40 50 60 MTDALKRLSK EGVAIWLDDL SRKRITSGNL AELIDQQHVV GVTTNPSIFQ KAISQGDGYD 70 80 90 100 110 120 QQVSDLAARR VTVEEAIRMI TTADVRDAAD ILRPVFDATD GQDGRVSIEV DPRLAHNTKA 130 140 150 160 170 180 TVAEAKQLAW LVDRPNTLIK IPATKAGIPA ITEVIGLGIS VNVTLIFSLE RYRMVMDAYL 190 200 210 220 230 240 AGLEKAKERG LDLSKIHSVA SFFVSRVDTE IDKRIDALGT PEAKAARGKA GLANARLAYE 250 260 270 280 290 300 AYEAVFSTDR WLALDKAQAN KQRPLWASTG VKDPAYKDTM YVEELVAPNT VNTMPEATLE 310 320 330 340 350 360 ATADHGEIRG NTIAGTYEQA RADLDAVEKL GIAYDDVVQL LEEEGVDKFE ASWNDLLKST 370 EAELQRLAPS EG

References

[1]

"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites." Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M. Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

[2]

"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis." Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S. Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000030 Genomic DNA. Translation: BAC74025.1.
RefSeq	NP_827490.1. NC_003155.4.
3D structure databases
ProteinModelPortal	Q829U5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1211459.
GenomeReviews	Gene locus SAV_6314 in contig BA000030_GR.
KEGG	sma:SAV_6314.
NMPDR	fig|227882.1.peg.6316.
PATRIC	23726686. VBIStrAve112782_6695.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG321149.
OMA	EESHAVM.
ProtClustDB	PRK03343.
Enzyme and pathway databases
BioCyc	SAVE227882:SAV6314-MONOMER.
Family and domain databases
HAMAP	MF_00493. Transaldolase_2. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR001585. Transaldolase. IPR004732. Transaldolase_2. 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]
PIRSF	PIRSF036915. Trnald_Bac_Plnt. 1 hit.
TIGRFAMs	TIGR00876. Tal_mycobact. 1 hit.
PROSITE	PS01054. TRANSALDOLASE_1. 1 hit. PS00958. TRANSALDOLASE_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TAL2_STRAW

Accession

Primary (citable) accession number: Q829U5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2005
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program