P19669 (TAL_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transaldolase
EC=2.2.1.2

Alternative name(s):
20 kDa phosphoprotein orfU
CSI9

Gene names

Name:	tal
Synonyms:	ywjH
Ordered Locus Names:	BSU37110

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	212 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. HAMAP MF_00494
Catalytic activity	Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. HAMAP MF_00494
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_00494
Subcellular location	Cytoplasm Probable HAMAP MF_00494.
Sequence similarities	Belongs to the transaldolase family. Type 3B subfamily.
Sequence caution	The sequence CAA89874.1 differs from that shown. Reason: Frameshift at position 182. The sequence M22039 differs from that shown. Reason: Frameshift at position 182.

Ontologies

Keywords
Biological process	Pentose shunt
Cellular component	Cytoplasm
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference 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 – 212	212	Transaldolase HAMAP MF_00494		PRO_0000173658
Sites
	Active site	84	1	By similarity
Amino acid modifications
	Modified residue	39	1	Phosphoserine Ref.9
Experimental info
	Sequence conflict	100	1	D → G in M22039. Ref.1
	Sequence conflict	100	1	D → G in CAA89874. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P19669 [UniParc]. Last modified July 28, 2009. Version 4. Checksum: 59EA1748FB2CBCD6	FASTA	212	22,971
	10 20 30 40 50 60 MLFFVDTANI DEIREANELG ILAGVTTNPS LVAKEANVSF HDRLREITDV VKGSVSAEVI 70 80 90 100 110 120 SLKAEEMIEE GKELAKIAPN ITVKIPMTSD GLKAVRALTD LGIKTNVTLI FNANQALLAA 130 140 150 160 170 180 RAGATYVSPF LGRLDDIGHN GLDLISEVKQ IFDIHGLDTQ IIAASIRHPQ HVTEAALRGA 190 200 210 HIGTMPLKVI HALTKHPLTD KGIEQFLADW NK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence and transcriptional analysis of the spo0F region of the Bacillus subtilis chromosome." Trach K., Chapman J.W., Piggot P.J., Lecoq D., Hoch J.A. J. Bacteriol. 170:4194-4208(1988) [PubMed: 2457578] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / JH642.
[2]	"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)." Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P. Microbiology 143:3313-3328(1997) [PubMed: 9353933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Detecting and analyzing DNA sequencing errors: toward a higher quality of the Bacillus subtilis genome sequence." Medigue C., Rose M., Viari A., Danchin A. Genome Res. 9:1116-1127(1999) [PubMed: 10568751] [Abstract] Cited for: SEQUENCE REVISION.
[5]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 100.
[6]	"Identification of proteins phosphorylated by ATP during sporulation of Bacillus subtilis." Mitchell C., Morris P.W., Vary J.C. J. Bacteriol. 174:2474-2477(1992) [PubMed: 1556067] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-24, PHOSPHORYLATION.
[7]	"Cold shock stress-induced proteins in Bacillus subtilis." Graumann P., Schroeder K., Schmid R., Marahiel M.A. J. Bacteriol. 178:4611-4619(1996) [PubMed: 8755892] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15. Strain: 168 / JH642.
[8]	"Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia coli and is related to a novel group of bacterial transaldolases." Schuermann M., Sprenger G.A. J. Biol. Chem. 276:11055-11061(2001) [PubMed: 11120740] [Abstract] Cited for: CHARACTERIZATION.
[9]	"The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis." Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M. Mol. Cell. Proteomics 6:697-707(2007) [PubMed: 17218307] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, MASS SPECTROMETRY. Strain: 168.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M22039 Unassigned DNA. No translation available. Z49782 Genomic DNA. Translation: CAA89874.1. Frameshift. AL009126 Genomic DNA. Translation: CAB15728.3.
PIR	F32354.
RefSeq	NP_391592.3. NC_000964.3.
3D structure databases
ProteinModelPortal	P19669.
SMR	P19669. Positions 1-212.
ModBase	Search...
PTM databases
PhosSite	P19669.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000003615; EBBACP00000003615; EBBACG00000003608.
GeneID	938462.
GenomeReviews	Gene locus BSU37110 in contig AL009126_GR.
KEGG	bsu:BSU37110.
PATRIC	18979458. VBIBacSub10457_3891.
Organism-specific databases
GenoList	BSU37110. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000001468.
HOGENOM	HBG533000.
PhylomeDB	P19669.
ProtClustDB	PRK01362.
Enzyme and pathway databases
BioCyc	BSUB:BSU37110-MONOMER.
Family and domain databases
HAMAP	MF_00494. Transaldolase_3b. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR001585. Transaldolase. IPR004731. Transaldolase_3A/3B. IPR022999. Transaldolase_3B. 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]
TIGRFAMs	TIGR00875. Fsa_talC_mipB. 1 hit.
PROSITE	PS01054. TRANSALDOLASE_1. 1 hit. PS00958. TRANSALDOLASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TAL_BACSU

Accession

Primary (citable) accession number: P19669

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 28, 2009
Last modified:	January 25, 2012
This is version 103 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program