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Q11R22 (F16PA_CYTH3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:CHU_2896
OrganismCytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469) [Complete proteome] [HAMAP]
Taxonomic identifier269798 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Cytophagia › Cytophagales › Cytophagaceae › Cytophaga

Protein attributes

Sequence length346 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 – 346346Fructose-1,6-bisphosphatase class 1 HAMAP MF_01855
PRO_0000364533

Regions

Region122 – 1254Substrate binding By similarity

Sites

Metal binding961Magnesium 1 By similarity
Metal binding1191Magnesium 1 By similarity
Metal binding1191Magnesium 2 By similarity
Metal binding1211Magnesium 1; via carbonyl oxygen By similarity
Metal binding1221Magnesium 2 By similarity
Metal binding2831Magnesium 2 By similarity
Binding site2141Substrate By similarity
Binding site2471Substrate By similarity
Binding site2771Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q11R22 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 46E78FC10CB228CC

FASTA34638,067
        10         20         30         40         50         60 
MERNLSTVKT LVQFITESQK HVFGASGDLS KILNDIAVAA KIINREVNKA GLLDILGMEG 

        70         80         90        100        110        120 
GMNVQNEEVK KLDVYANDQF ISALRSGGQC CAIASEENTD IIPIENNGHS KSNYVVLIDP 

       130        140        150        160        170        180 
LDGSSNIDVN VAIGSIFSIY RRVSESGPGE TVDCMQVGNK QVAAGYIIYG SSTMMVYTTG 

       190        200        210        220        230        240 
DGVNGFTLDP SIGEFCLSHP NLKIPEDGFI YSVNEGNYAD FPREIQEYIY YCKTPDFETS 

       250        260        270        280        290        300 
RPYSSRYIGS MVADFHRNLI KGGIFMYPAT AKYPLGKLRL MYECNPLAFI VEQAGGKAID 

       310        320        330        340 
GEGRILDIEP TNIHQRTGII IGSKNMVEKV EAFIQMNVGL NVYRLK

« Hide

References

[1]"Genome sequence of the cellulolytic gliding bacterium Cytophaga hutchinsonii."
Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B., McBride M.J.
Appl. Environ. Microbiol. 73:3536-3546(2007) [PubMed: 17400776] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33406 / NCIMB 9469.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000383 Genomic DNA. Translation: ABG60142.1.
RefSeqYP_679484.1. NC_008255.1.

3D structure databases

ProteinModelPortalQ11R22.
SMRQ11R22. Positions 8-336.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ11R22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4185068.
GenomeReviewsGene locus CHU_2896 in contig CP000383_GR.
KEGGchu:CHU_2896.
NMPDRfig|269798.12.peg.2776.
PATRIC21596669. VBICytHut34013_2889.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0158.
HOGENOMHBG731261.
OMAHWEAPVQ.

Enzyme and pathway databases

BioCycCHUT269798:CHU_2896-MONOMER.

Family and domain databases

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

Entry information

Entry nameF16PA_CYTH3
AccessionPrimary (citable) accession number: Q11R22
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: August 22, 2006
Last modified: January 25, 2012
This is version 46 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

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