Skip Header

Contribute Send feedback
Read comments (?) or add your own

P56888 (ALF_SINMW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. 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
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-bisphosphate aldolase
Short name=FBP aldolase
Short name=FBPA
EC=4.1.2.13
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene names
Name:cbbA
Ordered Locus Names:Smed_3923
Encoded onPlasmid pSMED01
OrganismSinorhizobium medicae (strain WSM419) (Ensifer medicae) [Complete proteome] [HAMAP]
Taxonomic identifier366394 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium ›

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis By similarity.

Catalytic activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Cofactor

Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution By similarity.

Pathway

Carbohydrate biosynthesis; Calvin cycle.

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Sequence caution

The sequence AAF25378.1 differs from that shown. Reason: Frameshift at positions 100 and 120.

Ontologies

Keywords
   Biological processCalvin cycle
Glycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Plasmid
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

reductive pentose-phosphate cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Fructose-bisphosphate aldolase
PRO_0000178730

Regions

Region233 – 2353Dihydroxyacetone phosphate binding By similarity
Region275 – 2784Dihydroxyacetone phosphate binding By similarity

Sites

Active site831Proton donor By similarity
Metal binding841Zinc 1; catalytic By similarity
Metal binding1051Zinc 2 By similarity
Metal binding1421Zinc 2 By similarity
Metal binding1981Zinc 1; catalytic By similarity
Metal binding2321Zinc 1; catalytic By similarity
Binding site501Glyceraldehyde 3-phosphate By similarity
Binding site1991Dihydroxyacetone phosphate; via amide nitrogen By similarity

Experimental info

Sequence conflict89 – 902AT → PN in AAF25378. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P56888 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 00D2342753333700

FASTA35938,925
        10         20         30         40         50         60 
MARITLRQLL DHAAERSYGV PAFNINNMEQ GLAIMEAARA CDAPVILQVS RGARSYANDI 

        70         80         90        100        110        120 
MLAKMMEALE VMYPDIPLCI HQDHGNNVAT CLTAIQHGFT SVMMDGSLKE DAKTPADYAY 

       130        140        150        160        170        180 
NAMITTEVSR LAHMVGASVE GELGCLGSLE TGHGEAEDGH GFEGALDRSQ LLTDPDEAAR 

       190        200        210        220        230        240 
FVAETGVDAL AVAIGTSHGA YKFTRKPTGE VLAMDVIEKI HERLPDTHIV MHGSSSVPQE 

       250        260        270        280        290        300 
WQDVFNAHGG EMRETYGVPV EEIVRGIRFG VRKVNIDTDL RLAAAAAFRR VADTSRTEFD 

       310        320        330        340        350 
PRKFLKPAMD AMSAVCKARF EAFGTAGNAS RIKVVPMAEM ARRYASGSLK PQAKRAEAA

« Hide

References

« Hide 'large scale' references
[1]"Genetic regulation of C1 metabolism in Sinorhizobium meliloti."
Fenner B.J., Tiwari R.P., Dilworth M.J.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WSM419.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF211846 Genomic DNA. Translation: AAF25378.1. Frameshift.
CP000739 Genomic DNA. Translation: ABR62733.1.
RefSeqYP_001312666.1. NC_009620.1.

3D structure databases

ProteinModelPortalP56888.
ModBaseSearch...

Protein-protein interaction databases

STRING366394.Smed_3923.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR62733; ABR62733; Smed_3923.
GeneID5318708.
KEGGsmd:Smed_3923.
PATRIC23613392. VBISinMed134228_0369.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227792.
KOK01624.
OMAIEKIHER.
ProtClustDBPRK09196.

Enzyme and pathway databases

BioCycSMED366394:GJAL-3984-MONOMER.
UniPathwayUPA00109; UER00183.
UPA00116.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR006412. Fruct_bisP_Calv.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsTIGR00167. cbbA. 1 hit.
TIGR01521. FruBisAldo_II_B. 1 hit.
PROSITEPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF_SINMW
AccessionPrimary (citable) accession number: P56888
Secondary accession number(s): A6UGF3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 13, 2007
Last modified: May 1, 2013
This is version 75 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents