Q1R9X7 (GATY_ECOUT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
D-tagatose-bisphosphate aldolase class II
Tagatose-bisphosphate aldolase

Gene names

Name:	gatY
Ordered Locus Names:	UTI89_C2369

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	284 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalytic subunit of the tagatose-1,6-bisphosphate aldolase GatYZ, 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 GatZ subunit for full activity and stability. Is involved in the catabolism of galactitol By similarity. HAMAP MF_01294
Catalytic activity	D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. HAMAP MF_01294
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_01294
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_01294
Subunit structure	Forms a complex with GatZ By similarity. HAMAP MF_01294
Sequence similarities	Belongs to the class II fructose-bisphosphate aldolase family. TagBP aldolase GatY subfamily.
Sequence caution	The sequence ABE07837.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Galactitol metabolism
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	galactitol catabolic 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 – 284	284	D-tagatose-1,6-bisphosphate aldolase subunit GatY HAMAP MF_01294		PRO_0000355341
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)
	Q1R9X7 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 9C920999A2708E8C	FASTA	284	30,937
	10 20 30 40 50 60 MYVVSTKQML NNARRGGYAV PAFNIHNLET MQVVVETAAS MHAPVIIAGT PGTFTHAGTE 70 80 90 100 110 120 NLMALVSAMA KQYHHPLAIH LDHHTKFDDI AQKVRSGVRS VMIDASHLPF AQNISRVKEV 130 140 150 160 170 180 VDFCHRFDVS VEAELGQLGG QEDDVQVNEA DAFYTNPVQA REFAEATGID SLAVAIGTAH 190 200 210 220 230 240 GMYASAPALD FSRLENIRQW VNLPLVLHGA SGLSTKDIQQ TIKLGICKIN VATELKNAFS 250 260 270 280 QALKNYLTEY PEATDPRDYL QSAKSAMRDV VSKVIADCGC EGRA

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: ABE07837.1. Different initiation.
RefSeq	YP_541368.2. NC_007946.1.
3D structure databases
ProteinModelPortal	Q1R9X7.
SMR	Q1R9X7. Positions 2-284.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1R9X7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000066265; EBESCP00000063743; EBESCG00000065312.
GeneID	3992117.
GenomeReviews	Gene locus UTI89_C2369 in contig CP000243_GR.
KEGG	eci:UTI89_C2369.
PATRIC	18454320. VBIEscCol42261_2398.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0191.
GeneTree	EBGT00050000009021.
HOGENOM	HBG327581.
OMA	KMYVVST.
ProtClustDB	PRK09195.
Enzyme and pathway databases
BioCyc	ECOL364106:UTI89_C2369-MONOMER.
Family and domain databases
HAMAP	MF_01294. TagBP_aldolase_GatY. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR000771. Ketose_bisP_aldolase_II. IPR011288. TagBP_ald_KbaY/GatY. IPR023955. TagBP_aldolase_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

GATY_ECOUT

Accession

Primary (citable) accession number: Q1R9X7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	November 25, 2008
Last modified:	January 25, 2012
This is version 40 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program