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A2SJK3 (F16A3_METPP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 44. 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 3
Short name=FBPase class 1 3
EC=3.1.3.11
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 3
Gene names
Name:fbp3
Ordered Locus Names:Mpe_A2788
OrganismMethylibium petroleiphilum (strain PM1) [Complete proteome] [HAMAP]
Taxonomic identifier420662 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Methylibium

Protein attributes

Sequence length357 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; Calvin cycle. 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 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: 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 – 357357Fructose-1,6-bisphosphatase class 1 3 HAMAP MF_01855
PRO_0000364598

Regions

Region119 – 1224Substrate binding By similarity

Sites

Metal binding941Magnesium 1 By similarity
Metal binding1161Magnesium 1 By similarity
Metal binding1161Magnesium 2 By similarity
Metal binding1181Magnesium 1; via carbonyl oxygen By similarity
Metal binding1191Magnesium 2 By similarity
Metal binding2831Magnesium 2 By similarity
Binding site2111Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A2SJK3 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 4328E8BE427BBB7E

FASTA35739,078
        10         20         30         40         50         60 
MPTGGKSTLT QFLIEERRKH PAATGELNAL ITDVSLACKA ISRKVAFGGL AGVLGSAGSG 

        70         80         90        100        110        120 
NVQGEEQKTL DVLSNTMFLR ATEWGGHVAG MVSEELEAPY TLPPQYARGK YLLMFDPLDG 

       130        140        150        160        170        180 
SSNIDVNVTV GSIFAIHRAP QPRQDPQPQD YLQPGTTMVC GGYAIYGPST MLVLTLGDGT 

       190        200        210        220        230        240 
HAFTLDPQLG EWVLSHPNLR IPEKTREFAI NASNSRFWEP AVKRYVDECL AGSTGPRGTD 

       250        260        270        280        290        300 
FNMRWIASLV AETHRILMRG GVFLYPRDSK DPNKAGRLRL LYEANPISFL IEQAGGMAST 

       310        320        330        340        350 
GRKRLLEVQP EDIHQRIGFV FGSTEEVARI EAYHRDEPPT PYNSPLFGKR GLFAEAG

« 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].
Strain: PM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000555 Genomic DNA. Translation: ABM95742.1.
RefSeqYP_001021977.1. NC_008825.1.

3D structure databases

ProteinModelPortalA2SJK3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2SJK3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4785038.
GenomeReviewsGene locus Mpe_A2788 in contig CP000555_GR.
KEGGmpt:Mpe_A2788.
NMPDRfig|279263.3.peg.3503.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0158.
HOGENOMHBG731261.
OMAVMVYTTG.
PhylomeDBA2SJK3.
ProtClustDBCLSK2534152.

Enzyme and pathway databases

BioCycMPET420662:MPE_A2788-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 nameF16A3_METPP
AccessionPrimary (citable) accession number: A2SJK3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: March 6, 2007
Last modified: November 16, 2011
This is version 44 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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