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B0C7G7 (F16A2_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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 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:AM1_6321
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesAcaryochloris

Protein attributes

Sequence length331 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 – 331331Fructose-1,6-bisphosphatase class 1 2 HAMAP MF_01855
PRO_0000364442

Regions

Region115 – 1184Substrate binding By similarity

Sites

Metal binding911Magnesium 1 By similarity
Metal binding1121Magnesium 1 By similarity
Metal binding1121Magnesium 2 By similarity
Metal binding1141Magnesium 1; via carbonyl oxygen By similarity
Metal binding1151Magnesium 2 By similarity
Metal binding2741Magnesium 2 By similarity
Binding site2071Substrate By similarity
Binding site2381Substrate By similarity
Binding site2681Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B0C7G7 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 153AB30769EBAC77

FASTA33136,121
        10         20         30         40         50         60 
MSHPTTFNSH LWQQHRLAQQ PIEISILLTQ MGFAAKVLAR EISRAALMGN LGLMGETNAT 

        70         80         90        100        110        120 
GDAQKKLDVF SNQIVIDAFS NIGLVAVIAS EELDQVKLIE CGQQAQYILC TDPLDGSSNT 

       130        140        150        160        170        180 
DTGSAVGTIF GIYRRQTSGY CSTEADVLQP GTELVTAGYV LYGTSTMLVY TTGGRVDGFT 

       190        200        210        220        230        240 
LDPSLGEFLL SHENIRCPET GKTYSANLSY YQEWHPHIQN FADYLSDRKS HTAHTLRYSG 

       250        260        270        280        290        300 
ALVADVHRCL LEGGLYFYPP TADQPEGKLR LLYECAPLAF LVEQAGGKAT SGLARIMDLE 

       310        320        330 
VTSIHQRSPL VIGSQVAVNL YQTFLEQGKA A 

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000828 Genomic DNA. Translation: ABW31251.1.
RefSeqYP_001520570.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0C7G7.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0C7G7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5685098.
GenomeReviewsGene locus AM1_6321 in contig CP000828_GR.
KEGGamr:AM1_6321.
PATRIC20626482. VBIAcaMar40141_5844.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG731261.
OMAYGSATMV.
PhylomeDBB0C7G7.

Enzyme and pathway databases

BioCycAMAR329726:AM1_6321-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 nameF16A2_ACAM1
AccessionPrimary (citable) accession number: B0C7G7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 34 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