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P53444 (ALF_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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-1
ORF Names:NCU07807
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora ›

Protein attributes

Sequence length362 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_processglycolysis

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 – 362362Fructose-bisphosphate aldolase
PRO_0000178759

Regions

Region269 – 2713Dihydroxyacetone phosphate binding By similarity
Region290 – 2934Dihydroxyacetone phosphate binding By similarity

Sites

Active site1121Proton donor By similarity
Metal binding1131Zinc 1; catalytic By similarity
Metal binding1471Zinc 2 By similarity
Metal binding1771Zinc 2 By similarity
Metal binding2291Zinc 1; catalytic By similarity
Metal binding2681Zinc 1; catalytic By similarity
Binding site631Glyceraldehyde 3-phosphate By similarity
Binding site2301Dihydroxyacetone phosphate; via amide nitrogen By similarity

Experimental info

Sequence conflict1 – 1515MGIFD…AGVLY → MRCPIPEHKQNLTFSLPL in AAB00930. Ref.1
Sequence conflict58 – 592II → SS in AAB00930. Ref.1
Sequence conflict661G → C in AAB00930. Ref.1
Sequence conflict82 – 843REA → ARD in AAB00930. Ref.1
Sequence conflict1091L → RI in AAB00930. Ref.1
Sequence conflict120 – 1267PWLDGML → FGDGIP in AAB00930. Ref.1
Sequence conflict211 – 2122AF → DS in AAB00930. Ref.1
Sequence conflict2221A → G in AAB00930. Ref.1
Sequence conflict2421E → D in AAB00930. Ref.1
Sequence conflict2471H → Q in AAB00930. Ref.1
Sequence conflict2521S → P in AAB00930. Ref.1
Sequence conflict2631V → F in AAB00930. Ref.1
Sequence conflict352 – 3609ALKDFNAAG → GPQGPSNTTV in AAB00930. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P53444 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: C402186EEEBD9368

FASTA36239,889
        10         20         30         40         50         60 
MGIFDELNLP AGVLYGDDVL KLFQYAREKQ FAIPACNVTS SSTAVAALEA ARDQKAPIIL 

        70         80         90        100        110        120 
QTSQGGAAFF AGKGIKDSAE KREASVAGAI AAAHYIRSIA PIYGIPVVLH TDHCAKKLLP 

       130        140        150        160        170        180 
WLDGMLEEDE KFFKANGVPL FSSHMIDLSE EPVEENISTC VKYLKRMAPM KQWLEMEIGI 

       190        200        210        220        230        240 
TGGEEDGVDN SEVDNASLYT QPEDIWQIEE AFRPISPYFS IAAGFGNVHG VYAPGNVKLH 

       250        260        270        280        290        300 
PELLGKHQAY VSEKLGGKDK KPVFFVFHGG SGSSKEEYRE AISNGVVKVN VDTDLQWSYL 

       310        320        330        340        350        360 
VGIRDYILNN IDYLRSQVGN PEGPNKPNKK KYDPRVWIRE GEKTMKARVE EALKDFNAAG 


TV

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References

« Hide 'large scale' references
[1]"DNA sequence of fructose-1,6-bisphosphate aldolase in N. crassa."
Yamashita R., Stuart W.D.
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 74A.
[2]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42380 Genomic DNA. Translation: AAB00930.1.
AABX02000046 Genomic DNA. Translation: EAA29157.1.
AABX02000046 Genomic DNA. Translation: EDO65002.1.
PIRT47260.
RefSeqXP_001728093.1. XM_001728041.1.
XP_958393.1. XM_953300.2.
UniGeneNcr.25490.

3D structure databases

ProteinModelPortalP53444.
SMRP53444. Positions 3-362.
ModBaseSearch...

Protein-protein interaction databases

STRING5141.NCU07807.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000008001; EFNCRP00000007990; EFNCRG00000007988.
GeneID3874540.
KEGGncr:NCU07807.

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227794.
KOK01624.
OMAREGEKTM.
OrthoDBEOG4J14HR.

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_NEUCR
AccessionPrimary (citable) accession number: P53444
Secondary accession number(s): A7UX41, Q7S1C1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 1, 2004
Last modified: April 3, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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