Q117I5 (FBSB_TRIEI) 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:

Tery_0948

Organism

Trichodesmium erythraeum (strain IMS101) [Complete proteome] [HAMAP]

Taxonomic identifier

203124 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Oscillatoriales › Trichodesmium

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
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_0000342736
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)
	Q117I5 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: 41A1B770977B73EB	FASTA	345	37,113
	10 20 30 40 50 60 MDNVIGLEII EVVEQAAIAS ARWMGKGEKN TADEVAVEAM RERMNKIHMR GRIVIGEGER 70 80 90 100 110 120 DEAPMLYIGE EVGICTQPDA KKMCEVEQLI EIDIAVDPCE GTNLVAYGQN GSMAVLAISE 130 140 150 160 170 180 KGGLLAAPDV YMKKLAAPAV AKNHVDINKS ATENLKIISE CMDRAVEELV VVVMDRPRHK 190 200 210 220 230 240 QLISEIRQAG ARVRLISDGD VSAAISCAFA GTNIHALMGI GAAPEGVISA AAMRALGGHF 250 260 270 280 290 300 QGQLIYDPAI VKTGLIGESK EDNMKRLKDM GIEDPDKVYN AEELASGETV LFAACGITPG 310 320 330 340 TLMEGVRFFP NGARTQSLVI SSQSKTARFV DTVHMFGETK TLQLK

References

[1]

"Complete sequence of Trichodesmium erythraeum IMS101." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P. , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P. Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IMS101.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000393 Genomic DNA. Translation: ABG50339.1.
RefSeq	YP_720812.1. NC_008312.1.
3D structure databases
ProteinModelPortal	Q117I5.
ModBase	Search...
Protein-protein interaction databases
STRING	Q117I5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4245687.
GenomeReviews	Gene locus Tery_0948 in contig CP000393_GR.
KEGG	ter:Tery_0948.
NMPDR	fig|203124.1.peg.4139.
PATRIC	23985464. VBITriEry99848_1171.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1494.
HOGENOM	HBG284837.
OMA	MYDPSAV.
PhylomeDB	Q117I5.
ProtClustDB	PRK09479.
Enzyme and pathway databases
BioCyc	TERY203124:TERY_0948-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_TRIEI

Accession

Primary (citable) accession number: Q117I5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	August 22, 2006
Last modified:	January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program