Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P58336 (ALF_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. 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-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:RB0192
ORF Names:SMb20199
Encoded onPlasmid pSymB (megaplasmid 2)
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

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.

Ontologies

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

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: UniProtKB-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_0000178729

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

Sequences

Sequence LengthMass (Da)Tools
P58336 [UniParc].

Last modified November 2, 2001. Version 1.
Checksum: 2589C30A0EC28DD3

FASTA35938,909
        10         20         30         40         50         60 
MARITLRQLL DHAAERSYGV PAFNINNMEQ GLAIMEAARA SDAPVILQVS RGARSYANDV 

        70         80         90        100        110        120 
MLAKMMEALE EMYPDIPLCI HQDHGNNVAT CLTAIQHGFT SVMMDGSLKE DAKTPADYDY 

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

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

       250        260        270        280        290        300 
WQDVFNAHGG QMRETYGVPV EEIVRGIRFG VRKVNIDTDL RLAAAAAFRR VADTSRSEFD 

       310        320        330        340        350 
PRKFLKPAMD AMSAVCKARF EAFGTAGNAS RIKVVPMPEM ARRYASGSLK PQSARSEAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591985 Genomic DNA. Translation: CAC48592.1.
PIRH95865.
RefSeqNP_436732.1. NC_003078.1.

3D structure databases

ProteinModelPortalP58336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266834.SM_b20199.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC48592; CAC48592; SM_b20199.
GeneID1236523.
KEGGsme:SM_b20199.
PATRIC23636773. VBISinMel96828_5108.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0191.
KOK01624.
OrthoDBEOG6HXJ7B.

Enzyme and pathway databases

BioCycSMEL266834:GJF6-3625-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_RHIME
AccessionPrimary (citable) accession number: P58336
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: November 2, 2001
Last modified: June 11, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways