Fructose-bisphosphate aldolase - Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)

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Q9HGY9 (ALF_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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:	fbaA
ORF Names:	AO090003000725

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

Protein attributes

Sequence length	362 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
Sequence caution	The sequence BAB12232.1 differs from that shown. Reason: Frameshift at positions 85 and 140.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from electronic annotation. Source: EnsemblFungi glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytosol Inferred from electronic annotation. Source: EnsemblFungi mitochondrion Inferred from electronic annotation. Source: EnsemblFungi
Molecular_function	fructose-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 362

362

Fructose-bisphosphate aldolase

PRO_0000178756

Regions

Region

269 – 271

Dihydroxyacetone phosphate binding By similarity

Region

290 – 293

Dihydroxyacetone phosphate binding By similarity

Sites

Active site

112

Proton donor By similarity

Metal binding

113

Zinc 1; catalytic By similarity

Metal binding

147

Zinc 2 By similarity

Metal binding

177

Zinc 2 By similarity

Metal binding

229

Zinc 1; catalytic By similarity

Metal binding

268

Zinc 1; catalytic By similarity

Binding site

Glyceraldehyde 3-phosphate By similarity

Binding site

230

Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9HGY9 [UniParc].

Last modified May 2, 2006. Version 2.
Checksum: 636526911421E17E
Show »

FASTA

362

39,721

        10         20         30         40         50         60 
MGVGVLEKLS RKTGVIVGDD VLRLFEHAQQ NNYAIPAVNV TSSSTVVASL EAARDQNCPI 

        70         80         90        100        110        120 
VLQLSQGGAA YFAGKGVSND GQQASIAGGI AAAHYIRSLA PAYGIPVVLH TDHCAKKLLP 

       130        140        150        160        170        180 
WLDGLLDEDE RYFKLHGEPL FSSHMIDLSE EPVDYNIQTT AAYLKRAAPM KQWLEMEIGI 

       190        200        210        220        230        240 
TGGEEDGVNN EDVDNNSLYT QPEDILAIHK ALSPISPYFS IAAGFGNVHG VYKPGNVKLH 

       250        260        270        280        290        300 
PELLKKHQAY VKEKIGSNKD KPVFFVFHGG SGSSKEEYKE AISYGVVKVN VDTDMQFAYM 

       310        320        330        340        350        360 
SGIRDYILKK KDYLMTAVGN PEGEDKPNKK SFDPRVWVRE GEKTMSQRVK VALEDFNTAG 


QL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of glycolytic gene from Aspergillus oryzae." Nakajima K., Kunihiro S., Sano M., Eto S., Machida M. Submitted (SEP-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. Kikuchi H. Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB032272 mRNA. Translation: BAB12232.1. Frameshift. AP007155 Genomic DNA. Translation: BAE57870.1.
RefSeq	XP_001819872.1. XM_001819820.2.
3D structure databases
ProteinModelPortal	Q9HGY9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00001323; CADAORAP00001304; CADAORAG00001323.
GeneID	5991855.
KEGG	aor:AOR_1_1284154.
Phylogenomic databases
eggNOG	COG0191.
HOGENOM	HOG000227794.
KO	K01624.
OrthoDB	EOG4J14HR.
Enzyme and pathway databases
UniPathway	UPA00109; UER00183.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR006411. Fruct_bisP_bact. IPR000771. Ketose_bisP_aldolase_II. [Graphical view]
Pfam	PF01116. F_bP_aldolase. 1 hit. [Graphical view]
PIRSF	PIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMs	TIGR00167. cbbA. 1 hit. TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITE	PS00602. ALDOLASE_CLASS_II_1. 1 hit. PS00806. ALDOLASE_CLASS_II_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALF_ASPOR

Accession

Primary (citable) accession number: Q9HGY9
Secondary accession number(s): Q2UKP5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	May 2, 2006
Last modified:	May 1, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents