Reviewed, UniProtKB/Swiss-Prot Q2S1G3 (F16A2_SALRD)

Names and origin

Protein names

Recommended name:
    Fructose-1,6-bisphosphatase class 1 2
      Short name=FBPase class 1 2
    EC=3.1.3.11
Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 2

Gene names

Name:	fbp2
Ordered Locus Names:	SRU_1856

Organism

Salinibacter ruber (strain DSM 13855) [Complete proteome] [HAMAP]

Taxonomic identifier

309807 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Sphingobacteria › Sphingobacteriales › Rhodothermaceae › Salinibacter

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Pathway	Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_01855
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm Potential.
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
Gene Ontology (GO)
Biological process	carbohydrate biosynthetic process 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: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 361	361	Fructose-1,6-bisphosphatase class 1 2 HAMAP MF_01855		PRO_0000364683
Regions
	Region	137 – 140	4	Substrate binding By similarity
Sites
	Metal binding	110	1	Magnesium 1 By similarity
	Metal binding	134	1	Magnesium 1 By similarity
	Metal binding	134	1	Magnesium 2 By similarity
	Metal binding	136	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	137	1	Magnesium 2 By similarity
	Metal binding	300	1	Magnesium 2 By similarity
	Binding site	231	1	Substrate By similarity
	Binding site	264	1	Substrate By similarity
	Binding site	294	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2S1G3-1 [UniParc]. Last modified March 3, 2009. Version 2. Checksum: D8B774698EE09BE5	FASTA	361	39,652
	10 20 30 40 50 60 MTGSHRTSHA GDGAPEDDLG TFQTLEQFIL DRQDSFPHST GAFSRLLRDI SLAAKIVNRD 70 80 90 100 110 120 MRRAGLLDVY GSTGERNVQG EVQQKMDALA HREFVQALRR GGECCLIGSE EHAEAIPLST 130 140 150 160 170 180 VSKEGDGKYI VLLDPLDGSS NIDVNVSVGT IFSIYRLPDG YEEEEPDPAA ALQPGTEQVA 190 200 210 220 230 240 AGYVVYGSST MLVYTTGNGV NGFTLDPSIG EFLLSHPDIQ TPSRGRLSSI NSGYYHSFEE 250 260 270 280 290 300 GLRDYLDWLQ QKDPETNRPA KTRYIGSFVS DFHRNLLKGG IYMYPATESS PAGKLRLMYE 310 320 330 340 350 360 ANPMGFIAEQ AGGAASDGHR RILEKEPDKL HQRTPLFIGS EEMVRRAEAF LQGEPERALS A

References

[1]

"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea." Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F. Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed: 16330755] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000159 Genomic DNA. Translation: ABC44261.1. Different initiation.
RefSeq	YP_445968.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q2S1G3.
Genome annotation databases
GeneID	3851372.
GenomeReviews	Gene locus SRU_1856 in contig CP000159_GR.
KEGG	sru:SRU_1856.
NMPDR	fig|309807.5.peg.1754.
TIGR	SRU_1856.
Phylogenomic databases
HOGENOM	Q2S1G3.
Enzyme and pathway databases
BioCyc	SRUB309807:SRU_1856-MON.
Family and domain databases
HAMAP	MF_01855. [Tree]
InterPro	IPR000146. Fructose_bisphosphatase. IPR020548. Fructose_bisphosphatase_AS. [Graphical view]
PANTHER	PTHR11556. In_FB_phphtase. 1 hit.
Pfam	PF00316. FBPase. 1 hit. [Graphical view]
PRINTS	PR00115. F16BPHPHTASE.
ProDom	PD001491. In_FB_phphtase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00124. FBPASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

F16A2_SALRD

Accession

Primary (citable) accession number: Q2S1G3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 3, 2009
Last sequence update:	March 3, 2009
Last modified:	September 22, 2009
This is version 36 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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