Q7V1T8 (FBSB_PROMP) 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:

PMM0767

Organism

Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]

Taxonomic identifier

59919 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	333 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 – 333	333	D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase		PRO_0000342723
Regions
	Region	88 – 90	3	Substrate binding By similarity
	Region	164 – 166	3	Substrate binding By similarity
	Region	186 – 188	3	Substrate binding By similarity
Sites
	Metal binding	33	1	Manganese 1 By similarity
	Metal binding	57	1	Manganese 1 By similarity
	Metal binding	85	1	Manganese 2 By similarity
	Metal binding	88	1	Manganese 2 By similarity
	Metal binding	213	1	Manganese 2 By similarity
	Binding site	119	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7V1T8 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 1D6CA247CABCE8F2	FASTA	333	35,150
	10 20 30 40 50 60 MNQTLIQEIL EVVEQAAIAS AKLTGLGQKD EADAAAVEAM RLRMGKIEMK GKIVIGEGER 70 80 90 100 110 120 DEAPMLYIGE EVGSGNGPGV DFAVDPCEGT NLCANNQRGS MAVLAASDTG GLFNAPDFYM 130 140 150 160 170 180 NKLAAPPAAK GKVDIRNSAT ENLKILSNCL DLAIDELTVV VMDRARHKGL IKEIRECGAK 190 200 210 220 230 240 IQPISDGDVQ AAIACGFAGT GTHCLMGIGA APEGVISAAA MRALGGHFQG QLVYDPAIAQ 250 260 270 280 290 300 TSEWADYTKE GNIKRLNEMG ITDIDKIYEA NELASGENVI FAGSGITDGL LFDGVKFEKD 310 320 330 CTRTSSLVIS TLDSTCRFTN TIHMKDGAKS ISL

References

[1]

"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation." Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W. Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CCMP1986 / MED4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX548174 Genomic DNA. Translation: CAE19226.1.
RefSeq	NP_892885.1. NC_005072.1.
3D structure databases
HSSP	HSSP built from PDB template 1NI9 based on UniProtKB P0A9C9.
ProteinModelPortal	Q7V1T8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7V1T8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1726391.
GenomeReviews	Gene locus PMM0767 in contig BX548174_GR.
KEGG	pmm:PMM0767.
NMPDR	fig|59919.1.peg.764.
PATRIC	23032390. VBIProMar68066_0863.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1494.
HOGENOM	HBG284837.
OMA	TSEWADM.
PhylomeDB	Q7V1T8.
ProtClustDB	PRK09479.
Enzyme and pathway databases
BioCyc	PMAR167540:PMM0767-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_PROMP

Accession

Primary (citable) accession number: Q7V1T8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program