Fructose-bisphosphate aldolase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P14540 (ALF_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 121. History...

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

Documents (4) |

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:	FBA1
Ordered Locus Names:	YKL060C
ORF Names:	YKL320

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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.
Miscellaneous	Present with 1020000 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from mutant phenotype. Source: SGD glycolysis Inferred from mutant phenotype. Source: SGD
Cellular component	cytosol Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	fructose-bisphosphate aldolase activity Inferred from mutant phenotype. Source: SGD 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

Initiator methionine

Removed Ref.6 Ref.8

Chain

2 – 359

358

Fructose-bisphosphate aldolase

PRO_0000178762

Regions

Region

266 – 268

Dihydroxyacetone phosphate binding By similarity

Region

287 – 290

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

265

Zinc 1; catalytic By similarity

Binding site

Glyceraldehyde 3-phosphate By similarity

Binding site

228

Dihydroxyacetone phosphate; via amide nitrogen By similarity

Amino acid modifications

Modified residue

Phosphothreonine Ref.10 Ref.11

Modified residue

Phosphothreonine Ref.11

Modified residue

Phosphoserine Ref.13

Modified residue

Phosphoserine Ref.13

Modified residue

Phosphoserine Ref.13

Modified residue

Phosphothreonine Ref.13

Modified residue

Phosphoserine Ref.13

Modified residue

Phosphoserine Ref.12 Ref.13

Modified residue

Phosphothreonine Ref.13

Modified residue

Phosphoserine Ref.13

Modified residue

Phosphoserine Ref.13

Modified residue

Phosphoserine Ref.13

Modified residue

147

Phosphoserine Ref.11 Ref.13

Modified residue

150

Phosphothreonine Ref.10 Ref.13

Modified residue

156

Phosphoserine Ref.13

Modified residue

157

Phosphothreonine Ref.13

Modified residue

179

Phosphothreonine Ref.11

Modified residue

214

Phosphoserine Ref.13

Modified residue

268

Phosphoserine Ref.11 Ref.13

Modified residue

270

Phosphoserine Ref.11

Modified residue

271

Phosphothreonine Ref.11

Modified residue

277

Phosphothreonine Ref.11

Modified residue

290

Phosphothreonine Ref.13

Modified residue

294

Phosphotyrosine Ref.13

Modified residue

310

Phosphotyrosine Ref.10

Modified residue

313

Phosphoserine Ref.10 Ref.12 Ref.13

Sequences

Sequence

Length

Mass (Da)

Tools

P14540 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C67E61BA5C7E8E4C
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FASTA

359

39,621

        10         20         30         40         50         60 
MGVEQILKRK TGVIVGEDVH NLFTYAKEHK FAIPAINVTS SSTAVAALEA ARDSKSPIIL 

        70         80         90        100        110        120 
QTSNGGAAYF AGKGISNEGQ NASIKGAIAA AHYIRSIAPA YGIPVVLHSD HCAKKLLPWF 

       130        140        150        160        170        180 
DGMLEADEAY FKEHGEPLFS SHMLDLSEET DEENISTCVK YFKRMAAMDQ WLEMEIGITG 

       190        200        210        220        230        240 
GEEDGVNNEN ADKEDLYTKP EQVYNVYKAL HPISPNFSIA AAFGNCHGLY AGDIALRPEI 

       250        260        270        280        290        300 
LAEHQKYTRE QVGCKEEKPL FLVFHGGSGS TVQEFHTGID NGVVKVNLDT DCQYAYLTGI 

       310        320        330        340        350 
RDYVLNKKDY IMSPVGNPEG PEKPNKKFFD PRVWVREGEK TMGAKITKSL ETFRTTNTL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, primary structure and disruption of the structural gene of aldolase from Saccharomyces cerevisiae." Schwelberger H.G., Kohlwein S.D., Paltauf F. Eur. J. Biochem. 180:301-308(1989) [PubMed: 2647491] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and TOA2 genes, an open reading frame (ORF) similar to a translationally controlled tumour protein, one ORF containing motifs also found in plant storage proteins and 13 ORFs with weak or no homology to known proteins." Rasmussen S.W. Yeast 10:S63-S68(1994) [PubMed: 8091862] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Cloning of Saccharomyces cerevisiae promoters using a probe vector based on phleomycin resistance." Gatignol A., Dassain M., Tiraby G. Gene 91:35-41(1990) [PubMed: 1698168] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
[6]	Jack R.S. Thesis (1973), University of Cambridge, United Kingdom Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-40.
[7]	"Protein identifications for a Saccharomyces cerevisiae protein database." Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S. Electrophoresis 15:1466-1486(1994) [PubMed: 7895733] [Abstract] Cited for: PROTEIN SEQUENCE OF 333-339. Strain: ATCC 204508 / S288c.
[8]	"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae." Norbeck J., Blomberg A. FEMS Microbiol. Lett. 137:1-8(1996) [PubMed: 8935650] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21. Strain: ATCC 38531 / Y41.
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; THR-150; TYR-310 AND SER-313, MASS SPECTROMETRY. Strain: ADR376.
[11]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; THR-24; SER-147; THR-179; SER-268; SER-270; THR-271 AND THR-277, MASS SPECTROMETRY.
[12]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-313, MASS SPECTROMETRY.
[13]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-41; SER-42; THR-43; SER-54; SER-56; THR-62; SER-63; SER-76; SER-96; SER-147; THR-150; SER-156; THR-157; SER-214; SER-268; THR-290; TYR-294 AND SER-313, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X15003 Genomic DNA. Translation: CAA33111.1. Z28060 Genomic DNA. Translation: CAA81897.1. X75781 Genomic DNA. Translation: CAA53412.1. M32026 Genomic DNA. No translation available. BK006944 Genomic DNA. Translation: DAA09097.1.
PIR	ADBY2. S07855.
RefSeq	NP_012863.1. NM_001179626.1.
3D structure databases
ProteinModelPortal	P14540.
SMR	P14540. Positions 2-359.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4702N.
IntAct	P14540. 31 interactions.
MINT	MINT-564440.
STRING	P14540.
2D gel databases
SWISS-2DPAGE	P14540.
COMPLUYEAST-2DPAGE	P14540.
UCD-2DPAGE	P14540.
Proteomic databases
PeptideAtlas	P14540.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKL060C; YKL060C; YKL060C.
GeneID	853805.
KEGG	sce:YKL060C.
NMPDR	fig\|4932.3.peg.3848.
Organism-specific databases
SGD	S000001543. FBA1.
Phylogenomic databases
eggNOG	fuNOG05260.
GeneTree	EFGT00050000005775.
HOGENOM	HBG327581.
OMA	SPNFSIA.
OrthoDB	EOG4J14HR.
Gene expression databases
ArrayExpress	P14540.
Genevestigator	P14540.
GermOnline	YKL060C. Saccharomyces cerevisiae.
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.
KO	K01624.
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...
Other
NextBio	974960.

Entry information

Entry name

ALF_YEAST

Accession

Primary (citable) accession number: P14540
Secondary accession number(s): D6VXM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

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

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents