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Reviewed, UniProtKB/Swiss-Prot A2SJJ0 (F16A2_METPP)

Last modified November 3, 2009. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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: Mpe_A2775
OrganismMethylibium petroleiphilum (strain PM1) [Complete proteome] [HAMAP]
Taxonomic identifier420662 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Pathway

Carbohydrate biosynthesis; Calvin cycle. HAMAP MF_01855

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the FBPase class 1 family.

Ontologies

Keywords
   Biological processCalvin cycle
Carbohydrate metabolism
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processreductive pentose-phosphate cycle

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: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 336336Fructose-1,6-bisphosphatase class 1 2 HAMAP MF_01855
PRO_0000364597

Regions

Region117 – 1204Substrate binding By similarity

Sites

Metal binding921Magnesium 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 binding2811Magnesium 2 By similarity
Binding site2091Substrate By similarity
Binding site2751Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A2SJJ0-1 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 4BBF9A63C8DD88F3

FASTA33636,989
        10         20         30         40         50         60 
MTRRISLTQY LVEEQRERGR IPAQLRLLLE VVARACKSIA ISVNKGALGG VLGSAGSENV 

        70         80         90        100        110        120 
QGEVQKKLDI IANEVLIEAN EWGGALAAMA SEEMDSIYVV PNRYPQGEYL LLFDPLDGSS 

       130        140        150        160        170        180 
NIDVNVSIGT IFSVLKKQSD TPGVSTQDFL QPGSAQVAAG YCVYGPQTTL VLTVGDGVAM 

       190        200        210        220        230        240 
FTLDREQGSW VLTTDEVRIP EDTREFAVNM SNQRHWAPPM QRYIDECLQG KDGPRGKDFN 

       250        260        270        280        290        300 
MRWVASMVAD VHRILCRGGV FMYPWDKREP AKAGKLRLMY EANPMGFIVE QAGGAATNGK 

       310        320        330 
QRVLDLQPSQ LHERVSVILG SKNEVERASA YHREAG 

« Hide

References

[1]"Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
J. Bacteriol. 189:1931-1945(2007) [PubMed: 17158667] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000555 Genomic DNA. Translation: ABM95729.1.
RefSeqYP_001021964.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA2SJJ0.

Genome annotation databases

GeneID4784672.
GenomeReviewsGene locus Mpe_A2775 in contig CP000555_GR.
KEGGmpt:Mpe_A2775.
NMPDRfig|279263.3.peg.3489.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAQRHWEAP.

Family and domain databases

HAMAPMF_01855.
[Tree]
InterProIPR000146. Fructose_bisphosphatase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PRINTSPR00115. F16BPHPHTASE.
ProDomPD001491. In_FB_phphtase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00124. FBPASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF16A2_METPP
AccessionPrimary (citable) accession number: A2SJJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: March 6, 2007
Last modified: November 3, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents