Reviewed, UniProtKB/Swiss-Prot Q0TCW8 (KBAY_ECOL5)

Names and origin

Protein names

Recommended name:
    D-tagatose-1,6-bisphosphate aldolase subunit kbaY
      Short name=TagBP aldolase
      Short name=TBPA
    EC=4.1.2.40
Alternative name(s):
    Tagatose-bisphosphate aldolase
    D-tagatose-bisphosphate aldolase class II
    Ketose 1,6-bisphosphate aldolase class II

Gene names

Name:	kbaY
Ordered Locus Names:	ECP_3229

Organism

Escherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

362663 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	286 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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.
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	glycolysis Inferred from electronic annotation. Source: InterPro lactose catabolic process via tagatose-6-phosphate Inferred from electronic annotation. Source: InterPro
Molecular function	fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: InterPro tagatose-bisphosphate aldolase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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_0000355327
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)
	Q0TCW8-1 [UniParc]. Last modified September 5, 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]

"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536." Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J. Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000247 Genomic DNA. Translation: ABG71211.1.
RefSeq	YP_671112.1.
3D structure databases
SMR	Q0TCW8. Positions 2-284.
ModBase	Search...
Genome annotation databases
GeneID	4188585.
GenomeReviews	Gene locus ECP_3229 in contig CP000247_GR.
KEGG	ecp:ECP_3229.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0TCW8.
OMA	Q0TCW8. TIELGVC.
Enzyme and pathway databases
BioCyc	ECOL362663:ECP_3229-MON.
Family and domain databases
HAMAP	MF_01293. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR000771. Ketose_bisP_aldolase_II. IPR011288. Tag_bisphos_ald. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF01116. F_bP_aldolase. 1 hit. [Graphical view]
PIRSF	PIRSF001359. F_bP_aldolase_II. 1 hit.
ProDom	PD002376. K_bP_aldolase. 1 hit. [Graphical view] [Entries sharing at least one domain]
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_ECOL5

Accession

Primary (citable) accession number: Q0TCW8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 20 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)