Fructose-bisphosphate aldolase 1 - Paracoccidioides brasiliensis (strain ATCC MYA-826 / Pb01)

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Reviewed, UniProtKB/Swiss-Prot Q96UH7 (ALF1_PARBA)

Last modified September 22, 2009. Version 36. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Fructose-bisphosphate aldolase 1
      Short name=FBP aldolase 1
      Short name=FBPA 1
    EC=4.1.2.13
Alternative name(s):
    Fructose-1,6-bisphosphate aldolase 1

Gene names

Name:	FBA1
ORF Names:	PAAG_01995

Organism

Paracoccidioides brasiliensis (strain ATCC MYA-826 / Pb01)

Taxonomic identifier

502779 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Onygenales › mitosporic Onygenales › Paracoccidioides

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Protein attributes

Sequence length	360 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.
Induction	Preferentially expressed in yeast cells, the host parasitic phase. Ref.1 Ref.3
Sequence similarities	Belongs to the class II fructose-bisphosphate aldolase family.

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Ontologies

Keywords
Biological process	Glycolysis
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 360

359

Fructose-bisphosphate aldolase 1

PRO_0000377379

Regions

Region

267 – 269

Dihydroxyacetone phosphate binding By similarity

Sites

Active site

110

Proton donor By similarity

Metal binding

111

Zinc 1; catalytic By similarity

Metal binding

145

Zinc 2 By similarity

Metal binding

175

Zinc 2 By similarity

Metal binding

227

Zinc 1; catalytic By similarity

Metal binding

266

Zinc 1; catalytic By similarity

Binding site

Glyceraldehyde 3-phosphate By similarity

Binding site

228

Dihydroxyacetone phosphate; via amide nitrogen By similarity

Experimental info

Sequence conflict

248

Y → H in AAL25625. Ref.1

Sequence conflict

248

Y → H in AAL34519. Ref.1

Sequence conflict

344

S → C in AAL25625. Ref.1

Sequence conflict

344

S → C in AAL34519. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q96UH7-1 [UniParc].

Last modified September 1, 2009. Version 3.
Checksum: 67475F644C58E162
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FASTA

360

39,632

        10         20         30         40         50         60 
MGVKDILSRK TGVIVGDDVL RLFQHAQEKV FAIPAINVTS SSTVVAALEA ARDKNSPIIL 

        70         80         90        100        110        120 
QVSQGGAAFF AGKGVPNGKQ EASVAGAIAA AHYIRSIAPS YGIPVVLHTD HCAKKLLPWL 

       130        140        150        160        170        180 
DGMLDADECY FKLHNEPLFS SHMIDLSEES VEWNIETTAK YLKRAAPMKQ WLEMEIGITG 

       190        200        210        220        230        240 
GEEDGVNNES VDNNSLYTQP EDIYTIYKTL SAISPYFSIA AGFGNVHGVY KPGNVRLHPE 

       250        260        270        280        290        300 
LLSKHQAYVK EKTGSSKNKP VYLVFHGGSG STKAEFKEAI SYGVVKVNLD TDLQYAYLSG 

       310        320        330        340        350        360 
VRDFVLKKKD YLMSAVGNPE GEDKPNKKYF DPRVWIREGE KTMSARVQEA FDDFNTSNQL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Paracoccidioides brasiliensis presents two different cDNAs encoding homologues of the fructose 1,6-biphosphate aldolase: protein isolation, cloning of the cDNAs and genes, structural, phylogenetic, and expression analysis." Carneiro L.C., de Faria F.P., Felipe M.S.S., Pereira M., de Almeida Soares C.M. Fungal Genet. Biol. 42:51-60(2005) [PubMed: 15588996] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 328-339 AND 343-359, INDUCTION.
[2]	"Annotation of Paracoccidioides brasiliensis Pb01." McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Ma L.-J.J., Henn M.R., Champion M., Cuomo C., Jaffe D., Young S., Gnerre S., Berlin A., Heiman D., Hepburn T., Sykes S., Yandava C., Alvarado L., Kodira C.D. Birren B.W. Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Two-dimensional electrophoresis and characterization of antigens from Paracoccidioides brasiliensis." da Fonseca C.A., Jesuino R.S.A., Felipe M.S.S., Cunha D.A., Brito W.A., de Almeida Soares C.M. Microbes Infect. 3:535-542(2001) [PubMed: 11418327] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-37, INDUCTION.

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Cross-references

Sequence databases
	AY057387 Genomic DNA. Translation: AAL25625.2. AY233454 mRNA. Translation: AAL34519.2. DS572814 Genomic DNA. Translation: EEH39806.1.
3D structure databases
HSSP	HSSP built from PDB template 1DOS based on UniProtKB P11604.
ModBase	Search...
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR006411. Fruct_bisP_bact. IPR000771. Ketose_bisP_aldolase_II. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF01116. F_bP_aldolase. 1 hit. [Graphical view]
PIRSF	PIRSF001359. F_bP_aldolase_II. 1 hit.
ProDom	PD002376. K_bP_aldolase. 1 hit. [Graphical view] [Entries sharing at least one domain]
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...

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Entry information

Entry name

ALF1_PARBA

Accession

Primary (citable) accession number: Q96UH7
Secondary accession number(s): C1GU00, Q8X219

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2009
Last sequence update:	September 1, 2009
Last modified:	September 22, 2009
This is version 36 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Family and domain databases

Entry information

Relevant documents