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A0M0J2 (F16A1_GRAFK) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 1
Short name=FBPase class 1 1
EC=3.1.3.11
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 1
Gene names
Name:fbp1
Ordered Locus Names:GFO_1163
OrganismGramella forsetii (strain KT0803) [Complete proteome] [HAMAP]
Taxonomic identifier411154 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Gramella

Protein attributes

Sequence length332 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 – 332332Fructose-1,6-bisphosphatase class 1 1 HAMAP MF_01855
PRO_0000364563

Regions

Region118 – 1214Substrate binding By similarity
Region262 – 2643Substrate binding By similarity

Sites

Metal binding921Magnesium 1 By similarity
Metal binding1151Magnesium 1 By similarity
Metal binding1151Magnesium 2 By similarity
Metal binding1171Magnesium 1; via carbonyl oxygen By similarity
Metal binding1181Magnesium 2 By similarity
Metal binding2801Magnesium 2 By similarity
Binding site2111Substrate By similarity
Binding site2441Substrate By similarity
Binding site2741Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A0M0J2 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 38FA85C2820B7D2B

FASTA33236,972
        10         20         30         40         50         60 
MERHTTLGEF IIENQKDFPY AKGELSALLS SIRLAGKVVN QQINKAGLAE ILGKAGKENV 

        70         80         90        100        110        120 
QGESQAKLDV LANEIFVSTL RNRGEICGLA SEELEDYLVF DEEMHKNAEY IVLIDPLDGS 

       130        140        150        160        170        180 
SNIDVDITVG TIFSIYRRIS KKGTPATLED FLQPGINQVA AGYLIYGTST ILVYTTGNGV 

       190        200        210        220        230        240 
NGFTFDPGIG SFFLSHSDIK FPKKGNTYSV NEGNYVHFPQ GIKKYIKWVQ ELNEEENRPF 

       250        260        270        280        290        300 
TSRYTGSLVA DFHRNMLLGG IYLYPQGTTA PKGKLRLLYE CNPMAFLAEQ AGGKATDGSR 

       310        320        330 
RIMELQPQEL HERAPFICGN KEMVEKAEEF MQ

« Hide

References

[1]"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter."
Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O.
Environ. Microbiol. 8:2201-2213(2006) [PubMed: 17107561] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT0803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU207366 Genomic DNA. Translation: CAL66137.1.
RefSeqYP_861204.1. NC_008571.1.

3D structure databases

ProteinModelPortalA0M0J2.
SMRA0M0J2. Positions 6-332.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0M0J2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4652579.
GenomeReviewsGene locus GFO_1163 in contig CU207366_GR.
KEGGgfo:GFO_1163.
NMPDRfig|411154.5.peg.1101.
PATRIC22071143. VBIGraFor5527_1118.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0158.
HOGENOMHBG731261.
OMAELHERAP.
PhylomeDBA0M0J2.
ProtClustDBPRK09293.

Enzyme and pathway databases

BioCycGFOR411154:GFO_1163-MONOMER.

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 nameF16A1_GRAFK
AccessionPrimary (citable) accession number: A0M0J2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 41 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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