Q63RX4 (F16PA_BURPS) 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:	BPSL2547

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei)

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	338 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 MF_01855
Cofactor	Binds 2 magnesium ions per subunit By similarity. HAMAP MF_01855
Pathway	Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_01855
Subunit structure	Homotetramer By similarity. HAMAP MF_01855
Subcellular location	Cytoplasm Potential HAMAP MF_01855.
Sequence similarities	Belongs to the FBPase class 1 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	fructose 1,6-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: EC metal 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 – 338	338	Fructose-1,6-bisphosphatase class 1 HAMAP MF_01855		PRO_0000364499
Regions
	Region	119 – 122	4	Substrate binding By similarity
Sites
	Metal binding	94	1	Magnesium 1 By similarity
	Metal binding	116	1	Magnesium 1 By similarity
	Metal binding	116	1	Magnesium 2 By similarity
	Metal binding	118	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	119	1	Magnesium 2 By similarity
	Metal binding	282	1	Magnesium 2 By similarity
	Binding site	210	1	Substrate By similarity
	Binding site	276	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63RX4 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: B4964A195E9A89F8	FASTA	338	37,377
	10 20 30 40 50 60 MSITRRTTLS KYLIEQQRET HNLPADLRLL IEVVARACKA ISYNVSKGAL GDALGTAGSE 70 80 90 100 110 120 NVQGEVQKKL DILSNEILLD ANEWGGNLAA MASEEMETFF PIPANYPRGE YLLVFDPLDG 130 140 150 160 170 180 SSNIDVNVSI GTIFSVLRCP DGQQATEQSF LQPGTEQVAA GYAVYGPQTV FVLTTGNGVN 190 200 210 220 230 240 CFTLDREVGS WVLTQSNLRI PEDTREYAIN ASNARHWYEP VKRYIDELNA GAEGPRGENF 250 260 270 280 290 300 NMRWIASMVA DVHRILNRGG IFMYPADKRT PDRPGKLRLM YEANPMSFIV EQAGGAATTG 310 320 330 LKRILDVQPT GLHQRVPVIL GSKNEVERVA RYHEQAQS

References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571965 Genomic DNA. Translation: CAH36554.1.
RefSeq	YP_109143.1. NC_006350.1.
3D structure databases
HSSP	HSSP built from PDB template 1DCU based on UniProtKB P46275.
ProteinModelPortal	Q63RX4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3092110.
GenomeReviews	Gene locus BPSL2547 in contig BX571965_GR.
KEGG	bps:BPSL2547.
PATRIC	19265403. VBIBurPse99623_2904.
Phylogenomic databases
HOGENOM	HBG731261.
OMA	HWEAPVQ.
PhylomeDB	Q63RX4.
ProtClustDB	PRK09293.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSL2547-MONOMER.
Family and domain databases
HAMAP	MF_01855. FBPase_class1. [Tree]
InterPro	IPR000146. FBPase_class-1/SBPase. [Graphical view]
KO	K03841.
PANTHER	PTHR11556. In_FB_phphtase. 1 hit.
Pfam	PF00316. FBPase. 1 hit. [Graphical view]
PIRSF	PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTS	PR00115. F16BPHPHTASE.
PROSITE	PS00124. FBPASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

F16PA_BURPS

Accession

Primary (citable) accession number: Q63RX4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 3, 2009
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program