Q1R324 (F16PA_ECOUT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fructose-1,6-bisphosphatase class 1
Short name=FBPase class 1
EC=3.1.3.11

Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1

Gene names

Name:	fbp
Ordered Locus Names:	UTI89_C4836

Organism

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

Taxonomic identifier

364106 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate. HAMAP-Rule MF_01855
Cofactor	Binds 2 magnesium ions per subunit By similarity. HAMAP-Rule MF_01855
Pathway	Carbohydrate biosynthesis; gluconeogenesis. HAMAP-Rule MF_01855
Subunit structure	Homotetramer By similarity. HAMAP-Rule MF_01855
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_01855.
Sequence similarities	Belongs to the FBPase class 1 family.
Sequence caution	The sequence ABE10240.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-UniPathway reductive pentose-phosphate cycle Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	fructose 1,6-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 332	332	Fructose-1,6-bisphosphatase class 1 HAMAP-Rule MF_01855		PRO_0000364548
Regions
	Region	113 – 116	4	Substrate binding By similarity
	Region	257 – 259	3	Substrate binding By similarity
Sites
	Metal binding	89	1	Magnesium 1 By similarity
	Metal binding	110	1	Magnesium 1 By similarity
	Metal binding	110	1	Magnesium 2 By similarity
	Metal binding	112	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	113	1	Magnesium 2 By similarity
	Metal binding	275	1	Magnesium 2 By similarity
	Binding site	206	1	Substrate By similarity
	Binding site	239	1	Substrate By similarity
	Binding site	269	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1R324 [UniParc]. Last modified March 3, 2009. Version 2. Checksum: 4F0FC8109491D78F	FASTA	332	36,834
	10 20 30 40 50 60 MKTLGEFIVE KQHEFSHATG ELTALLSAIK LGAKIIHRDI NKAGLVDILG ASGAENVQGE 70 80 90 100 110 120 VQQKLDLFAN EKLKAALKAR DIVAGIASEE EDEIVVFEGC EHAKYVVLMD PLDGSSNIDV 130 140 150 160 170 180 NVSVGTIFSI YRRVTPVGTP VTEEDFLQPG NKQVAAGYVV YGSSTMLVYT TGCGVHAFTY 190 200 210 220 230 240 DPSLGVFCLC QERMRFPEKG KTYSINEGNY IKFPNGVKKY IKFCQEEDKS TNRPYTSRYI 250 260 270 280 290 300 GSLVADFHRN LLKGGIYLYP STASHPDGKL RLLYECNPMA FLAEQAGGKA SDGKERILDI 310 320 330 IPETLHQRRS FFVGNDHMVE DVERFIREFP DA

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UTI89 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000243 Genomic DNA. Translation: ABE10240.1. Different initiation.
RefSeq	YP_543771.1. NC_007946.1.
3D structure databases
ProteinModelPortal	Q1R324.
SMR	Q1R324. Positions 1-332.
ModBase	Search...
Protein-protein interaction databases
STRING	364106.UTI89_C4836.
Proteomic databases
PRIDE	Q1R324.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABE10240; ABE10240; UTI89_C4836.
GeneID	3992004.
KEGG	eci:UTI89_C4836.
PATRIC	18459075. VBIEscCol42261_4710.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0158.
HOGENOM	HOG000191265.
KO	K03841.
OMA	CQEEDKA.
ProtClustDB	PRK09293.
Enzyme and pathway databases
BioCyc	ECOL364106:GHPQ-4789-MONOMER.
UniPathway	UPA00138.
Family and domain databases
HAMAP	MF_01855. FBPase_class1.
InterPro	IPR000146. FBPase_class-1/SBPase. IPR020548. Fructose_bisphosphatase_AS. [Graphical view]
PANTHER	PTHR11556. PTHR11556. 1 hit.
Pfam	PF00316. FBPase. 1 hit. [Graphical view]
PIRSF	PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTS	PR00115. F16BPHPHTASE.
PROSITE	PS00124. FBPASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

F16PA_ECOUT

Accession

Primary (citable) accession number: Q1R324

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 3, 2009
Last sequence update:	March 3, 2009
Last modified:	May 29, 2013
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program