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

P44429 (ALF_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:HI_0524
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

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 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 processGlycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
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_0000178716

Regions

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

Sites

Active site1101Proton donor By similarity
Metal binding1111Zinc 1; catalytic By similarity
Metal binding1451Zinc 2 By similarity
Metal binding1751Zinc 2 By similarity
Metal binding2271Zinc 1; catalytic By similarity
Metal binding2651Zinc 1; catalytic By similarity
Binding site621Glyceraldehyde 3-phosphate By similarity
Binding site2281Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P44429 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 1EDDFCDD0B69E32C

FASTA35939,340
        10         20         30         40         50         60 
MAKLLDIVKP GVVTGEDVQK VFAYAKEHNF AIPAVNCVGS DSVNAVLETA ARVKAPVIIQ 

        70         80         90        100        110        120 
FSNGGAAFYA GKGIKPTSGT RPDVLGAIAG AKQVHTLAKE YGVPVILHTD HAAKKLLPWI 

       130        140        150        160        170        180 
DGLLDAGEKH FAETGRPLFS SHMIDLSEES MEENMAICRE YLARMDKMGM TLEIEIGITG 

       190        200        210        220        230        240 
GEEDGVDNSD VDESRLYTQP SDVLYVYDQL HPVSPNFTVA AAFGNVHGVY KPGNVKLKPS 

       250        260        270        280        290        300 
ILGESQEFVS KERNLPAKPI NFVFHGGSGS SREEIREAIG YGAIKMNIDT DTQWASWNGI 

       310        320        330        340        350 
LNFYKANEAY LQGQLGNPEG PDAPNKKYYD PRVWLRKMEE SMSKRLEQSF EDLNCVDVL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC22182.1.
PIRC64074.
RefSeqNP_438682.1. NC_000907.1.

3D structure databases

ProteinModelPortalP44429.
SMRP44429. Positions 2-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI0524.

Proteomic databases

PRIDEP44429.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC22182; AAC22182; HI_0524.
GeneID949539.
KEGGhin:HI0524.
PATRIC20189601. VBIHaeInf48452_0543.

Phylogenomic databases

eggNOGCOG0191.
KOK01624.
OMAHNSLDFV.
OrthoDBEOG69GZPB.
PhylomeDBP44429.

Enzyme and pathway databases

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_HAEIN
AccessionPrimary (citable) accession number: P44429
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 92 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

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names