Q1R6K0 (KBAY_ECOUT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
D-tagatose-1,6-bisphosphate aldolase subunit KbaY
Short name=TBPA
Short name=TagBP aldolase
EC=4.1.2.40

Alternative name(s):
D-tagatose-bisphosphate aldolase class II
Ketose 1,6-bisphosphate aldolase class II
Tagatose-bisphosphate aldolase

Gene names

Name:	kbaY
Ordered Locus Names:	UTI89_C3568

Organism

Escherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

364106 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	286 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalytic subunit of the tagatose-1,6-bisphosphate aldolase KbaYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires KbaZ subunit for full activity and stability By similarity. HAMAP MF_01293
Catalytic activity	D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. HAMAP MF_01293
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_01293
Pathway	Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 2/2. HAMAP MF_01293
Subunit structure	Homotetramer. Forms a complex with KbaZ By similarity. HAMAP MF_01293
Sequence similarities	Belongs to the class II fructose-bisphosphate aldolase family. TagBP aldolase KbaY subfamily.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	tagatose-bisphosphate aldolase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 286	286	D-tagatose-1,6-bisphosphate aldolase subunit KbaY HAMAP MF_01293		PRO_0000355324
Regions
	Region	209 – 211	3	Dihydroxyacetone phosphate binding By similarity
	Region	230 – 233	4	Dihydroxyacetone phosphate binding By similarity
Sites
	Active site	82	1	Proton donor By similarity
	Metal binding	83	1	Zinc; catalytic By similarity
	Metal binding	180	1	Zinc; catalytic By similarity
	Metal binding	208	1	Zinc; catalytic By similarity
	Binding site	181	1	Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1R6K0 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: CAA42DF05C2B918B	FASTA	286	31,294
	10 20 30 40 50 60 MSIISTKYLL QDAQANGYAV PAFNIHNAET IQAILEVCSE MRSPVILAGT PGTFKHIALE 70 80 90 100 110 120 EIYALCSAYS TTYNMPLALH LDHHESLDDI RRKVHAGVRS AMIDGSHFPF AENVKLVKSV 130 140 150 160 170 180 VDFCHSQDCS VEAELGRLGG VEDDMSVDAE SAFLTDPQEA KRFVELTGVD SLAVAIGTAH 190 200 210 220 230 240 GLYSKTPKID FQRLAEIREV VDVPLVLHGA SDVPDEFVRR TIELGVTKVN VATELKIAFA 250 260 270 280 GAVKAWFAEN PQGNDPRYYM RVGMDAMKEV VRNKINVCGS ANRISA

References

[1]

"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach." Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UTI89 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000243 Genomic DNA. Translation: ABE09014.1.
RefSeq	YP_542545.1. NC_007946.1.
3D structure databases
ProteinModelPortal	Q1R6K0.
SMR	Q1R6K0. Positions 2-284.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1R6K0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000070656; EBESCP00000068134; EBESCG00000069703.
GeneID	3992479.
GenomeReviews	Gene locus UTI89_C3568 in contig CP000243_GR.
KEGG	eci:UTI89_C3568.
PATRIC	18456638. VBIEscCol42261_3535.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0191.
GeneTree	EBGT00050000009021.
HOGENOM	HBG327581.
OMA	TIELGVC.
ProtClustDB	PRK12738.
Enzyme and pathway databases
BioCyc	ECOL364106:UTI89_C3568-MONOMER.
Family and domain databases
HAMAP	MF_01293. TagBP_aldolase_KbaY. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR000771. Ketose_bisP_aldolase_II. IPR023788. TagBP_ald_KbaY. IPR011288. TagBP_ald_KbaY/GatY. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K08302.
Pfam	PF01116. F_bP_aldolase. 1 hit. [Graphical view]
PIRSF	PIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMs	TIGR00167. CbbA. 1 hit. TIGR01858. Tag_bisphos_ald. 1 hit.
PROSITE	PS00602. ALDOLASE_CLASS_II_1. 1 hit. PS00806. ALDOLASE_CLASS_II_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KBAY_ECOUT

Accession

Primary (citable) accession number: Q1R6K0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	May 16, 2006
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program