Q2S2I3 (F16A1_SALRD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	fbp1
Ordered Locus Names:	SRU_1474

Organism

Salinibacter ruber (strain DSM 13855 / M31)

Taxonomic identifier

309807 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidetes Order II. Incertae sedis › Rhodothermaceae › Salinibacter

Protein attributes

Sequence length	356 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 – 356	356	Fructose-1,6-bisphosphatase class 1 1 HAMAP MF_01855		PRO_0000364682
Regions
	Region	132 – 135	4	Substrate binding By similarity
Sites
	Metal binding	106	1	Magnesium 1 By similarity
	Metal binding	129	1	Magnesium 1 By similarity
	Metal binding	129	1	Magnesium 2 By similarity
	Metal binding	131	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	132	1	Magnesium 2 By similarity
	Metal binding	294	1	Magnesium 2 By similarity
	Binding site	225	1	Substrate By similarity
	Binding site	258	1	Substrate By similarity
	Binding site	288	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2S2I3 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: E8FE7313628FED8C	FASTA	356	38,538
	10 20 30 40 50 60 MSHALSDGPA PSGALESVMT LEQFILDRRG RFPQSTGAFS RLLRDVSVAA KIINHNIRRA 70 80 90 100 110 120 GILDVMGESG TVNVQDEKQK KLDEIADREL ERALRRGGEC CLVGSEEQAD TISLSPRGDF 130 140 150 160 170 180 QERFAVFFDP LDGSSNTDVN ASVGTIFSVY TLPEGADEGD ALDVALRPGA EQVAAGYVAY 190 200 210 220 230 240 GSSTMFVFTT GNGVNGFTLD PGIGEFLLTH PDLQIPQAPA MYSINEADIE DFSPELRAFL 250 260 270 280 290 300 QWLKTKDPDT GHRIRARYIG SFVSDFHRNL LTGGLYMYPA TSDHPDGKLR LMYEANPMAF 310 320 330 340 350 LVEQAGGRAS TGHQRILDLQ PEGLHERTPL FIGSAPLVKA AEAYLQGRGA EAVGGA

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]. Strain: DSM 13855 / M31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000159 Genomic DNA. Translation: ABC45463.1.
RefSeq	YP_445598.1. NC_007677.1.
3D structure databases
HSSP	HSSP built from PDB template 2GQ1 based on UniProtKB P0A993.
ProteinModelPortal	Q2S2I3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2S2I3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3850454.
GenomeReviews	Gene locus SRU_1474 in contig CP000159_GR.
KEGG	sru:SRU_1474.
NMPDR	fig|309807.5.peg.1391.
PATRIC	23425383. VBISalRub86502_1531.
TIGR	SRU_1474.
Phylogenomic databases
eggNOG	COG0158.
HOGENOM	HBG731261.
OMA	NSICTAV.
PhylomeDB	Q2S2I3.
ProtClustDB	CLSK745525.
Enzyme and pathway databases
BioCyc	SRUB309807:SRU_1474-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

F16A1_SALRD

Accession

Primary (citable) accession number: Q2S2I3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 3, 2009
Last sequence update:	January 24, 2006
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program