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A7HYA5 (F16PA_PARL1) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 33. 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:Plav_3283
OrganismParvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966) [Complete proteome] [HAMAP]
Taxonomic identifier402881 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Phyllobacteriaceae › Parvibaculum

Protein attributes

Sequence length343 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 – 343343Fructose-1,6-bisphosphatase class 1 HAMAP MF_01855
PRO_0000364620

Regions

Region116 – 1194Substrate binding By similarity

Sites

Metal binding911Magnesium 1 By similarity
Metal binding1131Magnesium 1 By similarity
Metal binding1131Magnesium 2 By similarity
Metal binding1151Magnesium 1; via carbonyl oxygen By similarity
Metal binding1161Magnesium 2 By similarity
Metal binding2821Magnesium 2 By similarity
Binding site2101Substrate By similarity
Binding site2761Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A7HYA5 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 5C74BD12671D485A

FASTA34338,228
        10         20         30         40         50         60 
MSQRTLTQFL IEQQRKEAAL PAQLRLLVEI VARACKTISH CVNKGALGGM LGNLTSENVQ 

        70         80         90        100        110        120 
GEVQKKLDVI ANEKLLEANE WGGHLAAMAS EEMETIHLIP NRYPKGEYLL LFDPIDGSSN 

       130        140        150        160        170        180 
IDVDLSVGTI FSVLTAPEDV SGRAVTEADF LQPGRKQVAA GYAIYGPQTL LILSVGTGVY 

       190        200        210        220        230        240 
EFALDREMGS WVLTNERIRI PSGNREFAIN MSNMRHWAPP VRRYIDECLA GTTGPREANF 

       250        260        270        280        290        300 
NMRWTASMVA DIHRILKRGG IFMYPWDARE PDRAGKLRLM YEANPMGFLI EQAGGMAFDG 

       310        320        330        340 
NHRILDIEPK ALHQRVGVVM GDRDEVKRVV QYHHDANLAK QTA

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References

[1]"Complete genome sequence and annotation of Parvibaculum lavamentivorans DS-1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DS-1 / DSM 13023 / NCIMB 13966.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000774 Genomic DNA. Translation: ABS64888.1.
RefSeqYP_001414545.1. NC_009719.1.

3D structure databases

ProteinModelPortalA7HYA5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7HYA5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5455347.
GenomeReviewsGene locus Plav_3283 in contig CP000774_GR.
KEGGpla:Plav_3283.
PATRIC22868379. VBIParLav90819_3393.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0158.
HOGENOMHBG731261.
OMAHWEAPVQ.

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_PARL1
AccessionPrimary (citable) accession number: A7HYA5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: September 11, 2007
Last modified: December 14, 2011
This is version 33 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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