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Protein

Fructose-bisphosphate aldolase

Gene

fba

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 activityi

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit. One is catalytic and the other provides a structural contribution.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631Glyceraldehyde 3-phosphateBy similarity
Active sitei112 – 1121Proton donorBy similarity
Metal bindingi113 – 1131Zinc 1; catalyticBy similarity
Metal bindingi147 – 1471Zinc 2By similarity
Metal bindingi177 – 1771Zinc 2By similarity
Metal bindingi229 – 2291Zinc 1; catalyticBy similarity
Binding sitei230 – 2301Dihydroxyacetone phosphate; via amide nitrogenBy similarity
Metal bindingi268 – 2681Zinc 1; catalyticBy similarity

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. gluconeogenesis Source: EnsemblFungi
  2. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene namesi
Name:fba
ORF Names:NCU07807
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805 Componenti: Chromosome 2, Linkage Group V

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: EnsemblFungi
  2. mitochondrion Source: EnsemblFungi
  3. nucleus Source: EnsemblFungi
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 362362Fructose-bisphosphate aldolasePRO_0000178759Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi5141.NCU07807.1.

Structurei

3D structure databases

ProteinModelPortaliP53444.
SMRiP53444. Positions 3-362.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni269 – 2713Dihydroxyacetone phosphate bindingBy similarity
Regioni290 – 2934Dihydroxyacetone phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227794.
InParanoidiP53444.
KOiK01624.
OMAiRMSKMGM.
OrthoDBiEOG7HTHSN.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53444-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIFDELNLP AGVLYGDDVL KLFQYAREKQ FAIPACNVTS SSTAVAALEA
60 70 80 90 100
ARDQKAPIIL QTSQGGAAFF AGKGIKDSAE KREASVAGAI AAAHYIRSIA
110 120 130 140 150
PIYGIPVVLH TDHCAKKLLP WLDGMLEEDE KFFKANGVPL FSSHMIDLSE
160 170 180 190 200
EPVEENISTC VKYLKRMAPM KQWLEMEIGI TGGEEDGVDN SEVDNASLYT
210 220 230 240 250
QPEDIWQIEE AFRPISPYFS IAAGFGNVHG VYAPGNVKLH PELLGKHQAY
260 270 280 290 300
VSEKLGGKDK KPVFFVFHGG SGSSKEEYRE AISNGVVKVN VDTDLQWSYL
310 320 330 340 350
VGIRDYILNN IDYLRSQVGN PEGPNKPNKK KYDPRVWIRE GEKTMKARVE
360
EALKDFNAAG TV
Length:362
Mass (Da):39,889
Last modified:March 1, 2004 - v2
Checksum:iC402186EEEBD9368
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 1515MGIFD…AGVLY → MRCPIPEHKQNLTFSLPL in AAB00930 (Ref. 1) CuratedAdd
BLAST
Sequence conflicti58 – 592II → SS in AAB00930 (Ref. 1) Curated
Sequence conflicti66 – 661G → C in AAB00930 (Ref. 1) Curated
Sequence conflicti82 – 843REA → ARD in AAB00930 (Ref. 1) Curated
Sequence conflicti109 – 1091L → RI in AAB00930 (Ref. 1) Curated
Sequence conflicti120 – 1267PWLDGML → FGDGIP in AAB00930 (Ref. 1) Curated
Sequence conflicti211 – 2122AF → DS in AAB00930 (Ref. 1) Curated
Sequence conflicti222 – 2221A → G in AAB00930 (Ref. 1) Curated
Sequence conflicti242 – 2421E → D in AAB00930 (Ref. 1) Curated
Sequence conflicti247 – 2471H → Q in AAB00930 (Ref. 1) Curated
Sequence conflicti252 – 2521S → P in AAB00930 (Ref. 1) Curated
Sequence conflicti263 – 2631V → F in AAB00930 (Ref. 1) Curated
Sequence conflicti352 – 3609ALKDFNAAG → GPQGPSNTTV in AAB00930 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42380 Genomic DNA. Translation: AAB00930.1.
CM002240 Genomic DNA. Translation: ESA42348.1.
CM002240 Genomic DNA. Translation: ESA42349.1.
PIRiT47260.
UniGeneiNcr.25490.

Genome annotation databases

EnsemblFungiiEFNCRT00000008000; EFNCRP00000007989; EFNCRG00000007988.
EFNCRT00000008001; EFNCRP00000007990; EFNCRG00000007988.
KEGGincr:NCU07807.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42380 Genomic DNA. Translation: AAB00930.1.
CM002240 Genomic DNA. Translation: ESA42348.1.
CM002240 Genomic DNA. Translation: ESA42349.1.
PIRiT47260.
UniGeneiNcr.25490.

3D structure databases

ProteinModelPortaliP53444.
SMRiP53444. Positions 3-362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5141.NCU07807.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000008000; EFNCRP00000007989; EFNCRG00000007988.
EFNCRT00000008001; EFNCRP00000007990; EFNCRG00000007988.
KEGGincr:NCU07807.

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227794.
InParanoidiP53444.
KOiK01624.
OMAiRMSKMGM.
OrthoDBiEOG7HTHSN.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiALF_NEUCR
AccessioniPrimary (citable) accession number: P53444
Secondary accession number(s): A7UX41, Q7S1C1, V5IKX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 1, 2004
Last modified: April 29, 2015
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.