Reviewed, UniProtKB/Swiss-Prot P22780 (F16A2_RHOSH)

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
Synonyms:	fbpB

Organism

Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)

Taxonomic identifier

1063 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	331 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.
Enzyme regulation	Fructose-1,6-bisphosphatase II is not light-activated. HAMAP MF_01855
Pathway	Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_01855
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm Potential.
Miscellaneous	There are two genes for FBPase in R.sphaeroides. 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
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 – 331	331	Fructose-1,6-bisphosphatase class 1 2 HAMAP MF_01855		PRO_0000200488
Regions
	Region	101 – 104	4	Substrate binding By similarity
Sites
	Metal binding	80	1	Magnesium 1 By similarity
	Metal binding	98	1	Magnesium 1 By similarity
	Metal binding	98	1	Magnesium 2 By similarity
	Metal binding	100	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	101	1	Magnesium 2 By similarity
	Metal binding	261	1	Magnesium 2 By similarity
	Binding site	189	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P22780-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 500EB63E9BBECD13	FASTA	331	35,256
	10 20 30 40 50 60 MAIELEDLGL SPDVADVMQR LARVGAGIAR IISRNGLERD LGAGVGTNAG GDGQKALDVI 70 80 90 100 110 120 ADDAFRAALE GSAVAYYASE EQDEVVTLGE GSLALAIDPL DGSSNIDVNV SIGTIFSIFP 130 140 150 160 170 180 AAAGPEASFL RPGTEQIAGG YIIYGPQCAL VCSFGQGVQH WVLDLDAGIF RRMPDIRPLP 190 200 210 220 230 240 AETSEFAINA SNYRHWPQPI RAFVDDLVAG AEGPRGKNFN MRWIASLVAE THRILMRGGV 250 260 270 280 290 300 FLYPGDERKG YERGRLRHVY ECAPIAFLIA NVGGGATDGC ADILTALPDR LHARTPFVFG 310 320 330 CASKVARVAA YHDLACEETS ALFGSRGLFR S

References

[1]	"The form II fructose 1,6-bisphosphatase and phosphoribulokinase genes form part of a large operon in Rhodobacter sphaeroides: primary structure and insertional mutagenesis analysis." Gibson J.L., Chen J.-H., Tower P.A., Tabita F.R. Biochemistry 29:8085-8093(1990) [PubMed: 2175647] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Positive and negative regulation of sequences upstream of the form II cbb CO2 fixation operon of Rhodobacter sphaeroides." Xu H.H., Tabita F.R. J. Bacteriol. 176:7299-7308(1994) [PubMed: 7961502] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42. Strain: HR.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J02922 Genomic DNA. Translation: AAA26105.1. U12430 Genomic DNA. Translation: AAA65078.1.
PIR	A35819.
3D structure databases
HSSP	HSSP built from PDB template 1DBZ based on UniProtKB P46275.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.3.11. 2796.
Family and domain databases
HAMAP	MF_01855. [Tree]
InterPro	IPR000146. Fructose_bisphosphatase. IPR017955. IMPase/FBPase. [Graphical view]
PANTHER	PTHR11556. In_FB_phphtase. 1 hit.
Pfam	PF00316. FBPase. 1 hit. [Graphical view]
PRINTS	PR00115. FBPHPHTASE. PR00377. INFBPHPHTASE.
ProDom	PD001491. In_FB_phphtase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00124. FBPASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

F16A2_RHOSH

Accession

Primary (citable) accession number: P22780
Secondary accession number(s): Q79D81

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 54 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)