O06812 (TAL_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transaldolase
EC=2.2.1.2

Gene names

Name:	tal
Ordered Locus Names:	Rv1448c, MT1495
ORF Names:	MTCY493.06

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	373 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 Reference proteome
Gene Ontology (GO)
Biological process	growth Inferred from mutant phenotype. Source: MTBBASE pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: MTBBASE extracellular region Inferred from direct assay. Source: MTBBASE
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 – 373	373	Transaldolase HAMAP MF_00493		PRO_0000173636
Sites
	Active site	143	1	By similarity
Experimental info
	Sequence conflict	244	1	T → A in AAK45758. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O06812 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 8CBA28D2654CF1FA	FASTA	373	40,721
	10 20 30 40 50 60 MTAQNPNLAA LSAAGVSVWL DDLSRDRLRS GNLQELIDTK SVVGVTTNPS IFQKALSEGH 70 80 90 100 110 120 TYDAQIAELA ARGADVDATI RTVTTDDVRS ACDVLVPQWE DSDGVDGRVS IEVDPRLAHE 130 140 150 160 170 180 TEKTIQQAIE LWKIVDRPNL FIKIPATKAG LPAISAVLAE GISVNVTLIF SVQRYREVMD 190 200 210 220 230 240 AYLTGMEKAR QAGHSLSKIH SVASFFVSRV DTEIDKRLDR IGSRQALELR GQAGVANARL 250 260 270 280 290 300 AYATYREVFE DSDRYRSLKV DGARVQRPLW ASTGVKNPDY SDTLYVTELV APHTVNTMPE 310 320 330 340 350 360 KTIDAVADHG VIQGDTVTGT ASDAQAVFDQ LGAIGIDLTD VFAVLEEEGV RKFEASWNEL 370 LQETRAHLDT AAQ

References

[1]

"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.

[2]

"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842576 Genomic DNA. Translation: CAB09258.1. AE000516 Genomic DNA. Translation: AAK45758.1.
PIR	C70917.
RefSeq	NP_215964.1. NC_000962.2. NP_335944.1. NC_002755.2.
3D structure databases
ProteinModelPortal	O06812.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000001561; EBMYCP00000001561; EBMYCG00000001561. EBMYCT00000070908; EBMYCP00000068967; EBMYCG00000070903.
GeneID	886606. 924475.
GenomeReviews	Gene locus MT1495 in contig AE000516_GR. Gene locus Rv1448c in contig AL123456_GR.
KEGG	mtc:MT1495. mtu:Rv1448c.
PATRIC	18125052. VBIMycTub22151_1641.
TIGR	MT1495.
Organism-specific databases
TubercuList	Rv1448c.
Phylogenomic databases
GeneTree	EBGT00050000017406.
HOGENOM	HBG321149.
OMA	MPEKTLD.
PhylomeDB	O06812.
ProtClustDB	PRK03343.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TAL_MYCTU

Accession

Primary (citable) accession number: O06812

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	July 1, 1997
Last modified:	January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program