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B2V6E2 (F16PA_SULSY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-1,6-bisphosphatase class 1

Short name=FBPase class 1
EC=3.1.3.11
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1
Gene names
Name:fbp
Ordered Locus Names:SYO3AOP1_0023
OrganismSulfurihydrogenibium sp. (strain YO3AOP1) [Complete proteome] [HAMAP]
Taxonomic identifier436114 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesHydrogenothermaceaeSulfurihydrogenibium

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP MF_01855

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_01855

Subunit structure

Homotetramer By similarity. HAMAP MF_01855

Subcellular location

Cytoplasm Potential HAMAP MF_01855.

Sequence similarities

Belongs to the FBPase class 1 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionfructose 1,6-bisphosphate 1-phosphatase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Fructose-1,6-bisphosphatase class 1 HAMAP MF_01855
PRO_0000364725

Regions

Region117 – 1204Substrate binding By similarity

Sites

Metal binding931Magnesium 1 By similarity
Metal binding1141Magnesium 1 By similarity
Metal binding1141Magnesium 2 By similarity
Metal binding1161Magnesium 1; via carbonyl oxygen By similarity
Metal binding1171Magnesium 2 By similarity
Metal binding2691Magnesium 2 By similarity
Binding site2051Substrate By similarity
Binding site2331Substrate By similarity
Binding site2631Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B2V6E2 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: B23649344993CC1A

FASTA32335,375
        10         20         30         40         50         60 
MAKIGMDLNS FILEQERLYP NATGSLSRAL VAIESATKVI ASHVRMAGLA DILGMAGKKN 

        70         80         90        100        110        120 
IQGEEVQKLD ELSNNLLIQY LSQSGEFFAL ASEELDEPIF PEEGKDAKYV IAFDPLDGSS 

       130        140        150        160        170        180 
NIDVNISIGT IFSIHRRVNS DVSDFLQEGY KQVAAGYVIY GSSTMLVLST GNGVNGFTLD 

       190        200        210        220        230        240 
PAVGMYLLSH PNMKIPEKGK IYSINESNDK KWIDAGLKEY IESLKDEGYT SRYIGSMVAD 

       250        260        270        280        290        300 
VHRTLIKGGI FAYPADVKNK NGKLRLLYEA SPMAFLTVQA GGIATTGKED ILNIKPTDIH 

       310        320 
QRVPVFLGGK YEMEKLKSML KNG 

« Hide

References

[1]"Complete and draft genome sequences of six members of the Aquificales."
Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.
J. Bacteriol. 191:1992-1993(2009) [PubMed: 19136599] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YO3AOP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001080 Genomic DNA. Translation: ACD65674.1.
RefSeqYP_001930228.1. NC_010730.1.

3D structure databases

ProteinModelPortalB2V6E2.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2V6E2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6331634.
GenomeReviewsGene locus SYO3AOP1_0023 in contig CP001080_GR.
KEGGsul:SYO3AOP1_0023.
PATRIC23764703. VBISulSp94719_0022.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG731261.
OMAHWEAPVQ.
ProtClustDBCLSK2479282.

Family and domain databases

HAMAPMF_01855. FBPase_class1.
[Tree]
InterProIPR000146. FBPase_class-1/SBPase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
KOK03841.
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFPIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSPR00115. F16BPHPHTASE.
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF16PA_SULSY
AccessionPrimary (citable) accession number: B2V6E2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: July 1, 2008
Last modified: January 25, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families