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P36580 (ALF_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. 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:fba1
ORF Names:SPBC19C2.07
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length358 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.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Fructose-bisphosphate aldolase
PRO_0000178761

Regions

Region265 – 2673Dihydroxyacetone phosphate binding By similarity
Region286 – 2894Dihydroxyacetone phosphate binding By similarity

Sites

Active site1081Proton donor By similarity
Metal binding1091Zinc 1; catalytic By similarity
Metal binding1431Zinc 2 By similarity
Metal binding1731Zinc 2 By similarity
Metal binding2251Zinc 1; catalytic By similarity
Metal binding2641Zinc 1; catalytic By similarity
Binding site611Glyceraldehyde 3-phosphate By similarity
Binding site2261Dihydroxyacetone phosphate; via amide nitrogen By similarity

Amino acid modifications

Modified residue2891Phosphothreonine Ref.3
Modified residue3121Phosphothreonine Ref.3
Modified residue3401Phosphothreonine Ref.3
Modified residue3421Phosphothreonine Ref.3

Experimental info

Sequence conflict131T → A in BAA04237. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P36580 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 50111C1C0E6DD05E

FASTA35839,570
        10         20         30         40         50         60 
MGILDIVPTG VITGDNVLKL FTYAREHGFA IPAINVTSSS TAIAALEAAR EARSPIILQT 

        70         80         90        100        110        120 
SNGGAHFFAG KESSNEGQKA SIAGSIAAAH YIRSIAPFFG VPVVMHSDHC AKKLLPWMDG 

       130        140        150        160        170        180 
MFEADEAYFK IHGEPLFSSH MLDLSEEPKK ENIAQVKEYC KRAVPMKIWI EMEIGITGGE 

       190        200        210        220        230        240 
EDGVDNSHVS HTELYTQPED IWDVYRELSS VTPYFSIAAA FGNVHGVYKP GNVKLQPALL 

       250        260        270        280        290        300 
GQHQAYVKEQ LKTTNDKPVF FVFHGGSGSS VNEFRTGIKC GVVKVNIDTD TQFAYVEGVR 

       310        320        330        340        350 
DYVLKYKDYL MTPVGNPEGA DKPNKKKFDP RVWIHEGEKT MTKRVLTALE DFYTVNTL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and nucleotide sequencing of Schizosaccharomyces pombe homologue of the class II fructose-1,6-bisphosphate aldolase gene."
Mutoh N., Hayashi Y.
Biochim. Biophys. Acta 1183:550-552(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-289; THR-312; THR-340 AND THR-342, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D17415 Genomic DNA. Translation: BAA04237.1.
CU329671 Genomic DNA. Translation: CAB52034.1.
PIRT39798.
T43289.
RefSeqNP_595692.1. NM_001021589.2.

3D structure databases

ProteinModelPortalP36580.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid277287. 14 interactions.
IntActP36580. 3 interactions.
MINTMINT-4688656.
STRING4896.SPBC19C2.07-1.

Proteomic databases

PaxDbP36580.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC19C2.07.1; SPBC19C2.07.1:pep; SPBC19C2.07.
GeneID2540767.
KEGGspo:SPBC19C2.07.

Organism-specific databases

PomBaseSPBC19C2.07.

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227794.
KOK01624.
OMAKKAYDPR.
OrthoDBEOG7HTHSN.
PhylomeDBP36580.

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...

Other

NextBio20801886.
PROP36580.

Entry information

Entry nameALF_SCHPO
AccessionPrimary (citable) accession number: P36580
Secondary accession number(s): Q9UUD3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 11, 2001
Last modified: April 16, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways