Reviewed, UniProtKB/Swiss-Prot P14540 (ALF_YEAST)

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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [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.8
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
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 Ref.1 Inferred from direct assay. Source: SGD zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5 Ref.7
	Chain	2 – 359	358	Fructose-bisphosphate aldolase		PRO_0000178762
Regions
	Region	266 – 268	3	Dihydroxyacetone phosphate binding By similarity
	Region	287 – 290	4	Dihydroxyacetone phosphate binding By similarity
Sites
	Active site	110	1	Proton donor By similarity
	Metal binding	111	1	Zinc 1; catalytic By similarity
	Metal binding	145	1	Zinc 2 By similarity
	Metal binding	175	1	Zinc 2 By similarity
	Metal binding	227	1	Zinc 1; catalytic By similarity
	Metal binding	265	1	Zinc 1; catalytic By similarity
	Binding site	63	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	228	1	Dihydroxyacetone phosphate; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	11	1	Phosphothreonine Ref.9 Ref.10
	Modified residue	24	1	Phosphothreonine Ref.10
	Modified residue	40	1	Phosphoserine Ref.12
	Modified residue	41	1	Phosphoserine Ref.12
	Modified residue	42	1	Phosphoserine Ref.12
	Modified residue	43	1	Phosphothreonine Ref.12
	Modified residue	54	1	Phosphoserine Ref.12
	Modified residue	56	1	Phosphoserine Ref.12 Ref.11
	Modified residue	62	1	Phosphothreonine Ref.12
	Modified residue	63	1	Phosphoserine Ref.12
	Modified residue	76	1	Phosphoserine Ref.12
	Modified residue	96	1	Phosphoserine Ref.12
	Modified residue	147	1	Phosphoserine Ref.10 Ref.12
	Modified residue	150	1	Phosphothreonine Ref.9 Ref.12
	Modified residue	156	1	Phosphoserine Ref.12
	Modified residue	157	1	Phosphothreonine Ref.12
	Modified residue	179	1	Phosphothreonine Ref.10
	Modified residue	214	1	Phosphoserine Ref.12
	Modified residue	268	1	Phosphoserine Ref.10 Ref.12
	Modified residue	270	1	Phosphoserine Ref.10
	Modified residue	271	1	Phosphothreonine Ref.10
	Modified residue	277	1	Phosphothreonine Ref.10
	Modified residue	290	1	Phosphothreonine Ref.12
	Modified residue	294	1	Phosphotyrosine Ref.12
	Modified residue	310	1	Phosphotyrosine Ref.9
	Modified residue	313	1	Phosphoserine Ref.9 Ref.12 Ref.11

Sequences

	Sequence		Length	Mass (Da)
	P14540-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C67E61BA5C7E8E4C	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

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. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"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.
[4]	"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.
[5]	Jack R.S. Thesis (1973), University of Cambridge, United Kingdom Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-40.
[6]	"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.
[7]	"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.
[8]	"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].
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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
EMBLGenBankDDBJ	X15003 Genomic DNA. Translation: CAA33111.1. Z28060 Genomic DNA. Translation: CAA81897.1. X75781 Genomic DNA. Translation: CAA53412.1. M32026 Genomic DNA. No translation available.
PIR	ADBY2. S07855.
RefSeq	NP_012863.1.
3D structure databases
HSSP	HSSP built from PDB template 1GYN based on UniProtKB P11604.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4702N.
IntAct	P14540. 76 interactions.
2-D gel databases
SWISS-2DPAGE	P14540.
COMPLUYEAST-2DPAGE	P14540.
Proteomic databases
PeptideAtlas	P14540.
PRIDE	P14540.
Genome annotation databases
Ensembl	YKL060C. Saccharomyces cerevisiae. [Contig view]
GeneID	853805.
GenomeReviews	Gene locus YKL060C in contig Y13137_GR.
KEGG	sce:YKL060C.
NMPDR	fig|4932.3.peg.3848.
Organism-specific databases
CYGD	YKL060c.
SGD	S000001543. FBA1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P14540.
OMA	P14540. DLNCVDV.
Enzyme and pathway databases
BRENDA	4.1.2.13. 250.
Gene expression databases
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.
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...
Other Resources
NextBio	974960.

Entry information

Entry name

ALF_YEAST

Accession

Primary (citable) accession number: P14540

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)