P73922 (FBSB_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase
Short name=FBPase class 2/SBPase
EC=3.1.3.11
EC=3.1.3.37

Gene names

Ordered Locus Names:

slr2094

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa)

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the hydrolysis of fructose 1,6-bisphosphate (Fru 1,6-P2) and sedoheptulose 1,7-bisphosphate (Sed 1,7-P2) to fructose 6-phosphate and sedoheptulose 7-phosphate, respectively By similarity.
Catalytic activity	D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate. Sedoheptulose 1,7-bisphosphate + H2O = sedoheptulose 7-phosphate + phosphate.
Cofactor	Manganese By similarity.
Pathway	Carbohydrate biosynthesis; Calvin cycle.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the FBPase class 2 family.

Ontologies

Keywords
Biological process	Calvin cycle Carbohydrate metabolism
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glycerol metabolic process Inferred from electronic annotation. Source: InterPro reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
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 sedoheptulose-bisphosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 345	345	D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase		PRO_0000342735
Regions
	Region	100 – 102	3	Substrate binding By similarity
	Region	176 – 178	3	Substrate binding By similarity
	Region	198 – 200	3	Substrate binding By similarity
Sites
	Metal binding	33	1	Manganese 1 By similarity
	Metal binding	57	1	Manganese 1 By similarity
	Metal binding	97	1	Manganese 2 By similarity
	Metal binding	100	1	Manganese 2 By similarity
	Metal binding	225	1	Manganese 2 By similarity
	Binding site	131	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P73922 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: A6DA0D2E16724179	FASTA	345	37,075
	10 20 30 40 50 60 MDSTLGLEII EVVEQAAIAS AKWMGKGEKN TADQVAVEAM RERMNKIHMR GRIVIGEGER 70 80 90 100 110 120 DDAPMLYIGE EVGICTREDA KSFCNPDELV EIDIAVDPCE GTNLVAYGQN GSMAVLAISE 130 140 150 160 170 180 KGGLFAAPDF YMKKLAAPPA AKGHVDIDKS ATENLKILSD CLNRSIEELV VVVMDRPRHK 190 200 210 220 230 240 ELIQEIRNAG ARVRLISDGD VSAAISCAFS GTNIHALMGI GAAPEGVISA AAMRCLGGHF 250 260 270 280 290 300 QGQLIYDPEV VKTGLIGESR EGNLERLASM GIKNPDQVYN CEELACGETV LFAACGITPG 310 320 330 340 TLMEGVRFFH GGVRTQSLVI SSQSSTARFV DTVHMKESPK VIQLH

References

[1]

"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27184 / PCC 6803 / N-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000022 Genomic DNA. Translation: BAA17988.1.
PIR	S75126.
RefSeq	NP_441308.1. NC_000911.1.
3D structure databases
HSSP	HSSP built from PDB template 1NI9 based on UniProtKB P0A9C9.
ProteinModelPortal	P73922.
ModBase	Search...
Protein-protein interaction databases
IntAct	P73922. 1 interaction.
STRING	P73922.
Proteomic databases
PRIDE	P73922.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	954653.
GenomeReviews	Gene locus slr2094 in contig BA000022_GR.
KEGG	syn:slr2094.
NMPDR	fig|1148.1.peg.1409.
PATRIC	23839982. VBISynSp132158_1551.
Phylogenomic databases
eggNOG	COG1494.
HOGENOM	HBG284837.
OMA	MYDPSAV.
PhylomeDB	P73922.
ProtClustDB	PRK09479.
Enzyme and pathway databases
BioCyc	MetaCyc:FBPSBP-MONOMER. SSP1148:SLR2094-MONOMER.
Family and domain databases
InterPro	IPR004464. FBPase_class-2/SBPase. [Graphical view]
KO	K11532.
Pfam	PF03320. FBPase_glpX. 1 hit. [Graphical view]
PIRSF	PIRSF004532. GlpX. 1 hit.
TIGRFAMs	TIGR00330. GlpX. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FBSB_SYNY3

Accession

Primary (citable) accession number: P73922

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	February 1, 1997
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program