Reviewed, UniProtKB/Swiss-Prot Q1LN82 (F16A2_RALME)

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
Ordered Locus Names:	Rmet_1511

Organism

Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]

Taxonomic identifier

266264 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	365 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.
Pathway	Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_01855
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm Potential.
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
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 – 365	365	Fructose-1,6-bisphosphatase class 1 2 HAMAP MF_01855		PRO_0000364663
Regions
	Region	125 – 128	4	Substrate binding By similarity
Sites
	Metal binding	100	1	Magnesium 1 By similarity
	Metal binding	122	1	Magnesium 1 By similarity
	Metal binding	122	1	Magnesium 2 By similarity
	Metal binding	124	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	125	1	Magnesium 2 By similarity
	Metal binding	293	1	Magnesium 2 By similarity
	Binding site	221	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1LN82-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 4CFF88F10FCD097A	FASTA	365	39,933
	10 20 30 40 50 60 MPLSHRQTLT RYLIEERRRF PEASGELNAL ILDVALACKA LARVVSFGEL GDALSDGSAA 70 80 90 100 110 120 PTGGGINVQG EVQKPLDVQS NEMFIRMNEW NGQLAGMASE EMEEPYLIPS SYPRGKYLLV 130 140 150 160 170 180 FDPLDGSSNI DVNVSIGSIF SILRAPADVV ASGRDVTEAD FLQPGAAQVA AGYTIYGPTT 190 200 210 220 230 240 QLVLTVGNGV AAFTLDPNLG EFLLTRSDIR VPEQTQEFAI NSSNSRFWEP PVKRYVDECL 250 260 270 280 290 300 AGKTGPRGKD FNMRWVASMV AEAHRILMRG GVFMYPRDTK DPAKPGRLRL LYEANPVAML 310 320 330 340 350 360 MEQAGGRAST GREPILGVSP TALHQRIGLI FGSKDEVERI ERYHQEPASN EAAAPLFAER SLFRD

References

[1]

"Complete sequence of the chromosome of Ralstonia metallidurans CH34." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000352 Genomic DNA. Translation: ABF08394.1.
RefSeq	YP_583663.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q1LN82.
Genome annotation databases
GeneID	4038314.
GenomeReviews	Gene locus Rmet_1511 in contig CP000352_GR.
KEGG	rme:Rmet_1511.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1LN82.
OMA	ATGELTQ.
Enzyme and pathway databases
BioCyc	RMET266264:RMET_1511-MON.
Family and domain databases
HAMAP	MF_01855. [Tree]
InterPro	IPR000146. Fructose_bisphosphatase. IPR020548. Fructose_bisphosphatase_AS. [Graphical view]
PANTHER	PTHR11556. In_FB_phphtase. 1 hit.
Pfam	PF00316. FBPase. 1 hit. [Graphical view]
PRINTS	PR00115. F16BPHPHTASE.
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_RALME

Accession

Primary (citable) accession number: Q1LN82

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 3, 2009
Last sequence update:	May 30, 2006
Last modified:	November 3, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)