Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fructose-bisphosphate aldolase

Gene

fbaA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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 sitei65 – 651Glyceraldehyde 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:fbaA
ORF Names:AO090003000725
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564 Componenti: Chromosome 2

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_0000178756Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9HGY9.
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.
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.

Q9HGY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVGVLEKLS RKTGVIVGDD VLRLFEHAQQ NNYAIPAVNV TSSSTVVASL
60 70 80 90 100
EAARDQNCPI VLQLSQGGAA YFAGKGVSND GQQASIAGGI AAAHYIRSLA
110 120 130 140 150
PAYGIPVVLH TDHCAKKLLP WLDGLLDEDE RYFKLHGEPL FSSHMIDLSE
160 170 180 190 200
EPVDYNIQTT AAYLKRAAPM KQWLEMEIGI TGGEEDGVNN EDVDNNSLYT
210 220 230 240 250
QPEDILAIHK ALSPISPYFS IAAGFGNVHG VYKPGNVKLH PELLKKHQAY
260 270 280 290 300
VKEKIGSNKD KPVFFVFHGG SGSSKEEYKE AISYGVVKVN VDTDMQFAYM
310 320 330 340 350
SGIRDYILKK KDYLMTAVGN PEGEDKPNKK SFDPRVWVRE GEKTMSQRVK
360
VALEDFNTAG QL
Length:362
Mass (Da):39,721
Last modified:May 2, 2006 - v2
Checksum:i636526911421E17E
GO

Sequence cautioni

The sequence BAB12232.1 differs from that shown. Reason: Frameshift at positions 85 and 140. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032272 mRNA. Translation: BAB12232.1. Frameshift.
AP007155 Genomic DNA. Translation: BAE57870.1.
RefSeqiXP_001819872.1. XM_001819820.2.

Genome annotation databases

EnsemblFungiiCADAORAT00001323; CADAORAP00001304; CADAORAG00001323.
GeneIDi5991855.
KEGGiaor:AOR_1_1284154.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032272 mRNA. Translation: BAB12232.1. Frameshift.
AP007155 Genomic DNA. Translation: BAE57870.1.
RefSeqiXP_001819872.1. XM_001819820.2.

3D structure databases

ProteinModelPortaliQ9HGY9.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00001323; CADAORAP00001304; CADAORAG00001323.
GeneIDi5991855.
KEGGiaor:AOR_1_1284154.

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227794.
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. "Molecular cloning and characterization of glycolytic gene from Aspergillus oryzae."
    Nakajima K., Kunihiro S., Sano M., Eto S., Machida M.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ATCC 42149 / RIB 40.
  2. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiALF_ASPOR
AccessioniPrimary (citable) accession number: Q9HGY9
Secondary accession number(s): Q2UKP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: May 2, 2006
Last modified: April 1, 2015
This is version 81 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.