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O51401 (ALF_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 96. 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:fba
Ordered Locus Names:BB_0445
OrganismBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680) [Reference proteome] [HAMAP]
Taxonomic identifier224326 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglycolytic process

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_0000178707

Regions

Region266 – 2683Dihydroxyacetone phosphate binding By similarity
Region287 – 2904Dihydroxyacetone phosphate binding By similarity

Sites

Active site1091Proton donor By similarity
Metal binding1101Zinc 1; catalytic By similarity
Metal binding1441Zinc 2 By similarity
Metal binding1741Zinc 2 By similarity
Metal binding2261Zinc 1; catalytic By similarity
Metal binding2651Zinc 1; catalytic By similarity
Binding site611Glyceraldehyde 3-phosphate By similarity
Binding site2271Dihydroxyacetone phosphate; via amide nitrogen By similarity

Experimental info

Sequence conflict21G → S AA sequence Ref.2
Sequence conflict61K → L AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
O51401 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: FAF4209478692FCB

FASTA35939,981
        10         20         30         40         50         60 
MGVLDKIKPG VVYGKELHFL YEICKKEGFA IPSINCIGTN SINAVLEAAK EINSPIMIQF 

        70         80         90        100        110        120 
SNSGSAFISG KGLKMEKPQG VSIVGAISGA MHVHLMAEHY GVPVVLHTDH CAKNLLPWVE 

       130        140        150        160        170        180 
GLLEYGEKYY SQHKKPLFSS HMLDLSEEPI KENIEISKKF LERMAKIEMF LEIELGITGG 

       190        200        210        220        230        240 
EEDGVDNSDR ALHELFSTPE DIYYGYSELL KVSPNFQIAA AFGNVHGVYK PGNVKLTPKV 

       250        260        270        280        290        300 
LKDGQDYVIS KTGVNMAKPV SYVFHGGSGS TIDEINEALS YGVVKMNIDT DTQWAAWEGV 

       310        320        330        340        350 
LNYYKKNESR LQGQLGDGKD IDIPNKKFYD PRVWLREAEV SMKDRVKIAC KNLNNINRN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000783 Genomic DNA. Translation: AAB91507.1.
PIRD70155.
RefSeqNP_212579.1. NC_001318.1.

3D structure databases

ProteinModelPortalO51401.
SMRO51401. Positions 3-357.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224326.BB0445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB91507; AAB91507; BB_0445.
GeneID1195290.
KEGGbbu:BB_0445.
PATRIC20557506. VBIBorBur75917_0836.

Phylogenomic databases

eggNOGCOG0191.
KOK01624.
OMAHNSLDFV.
OrthoDBEOG69GZPB.

Enzyme and pathway databases

BioCycBBUR224326:G9SO-446-MONOMER.
UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
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.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF_BORBU
AccessionPrimary (citable) accession number: O51401
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: June 11, 2014
This is version 96 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