P36580 (ALF_SCHPO) Reviewed, UniProtKB/Swiss-Prot

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
ORF Names:	SPBC19C2.07

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
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 By similarity.
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 Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from sequence or structural similarity. Source: PomBase
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase nucleus Inferred from direct assay PubMed 16823372. Source: PomBase
Molecular_function	fructose-bisphosphate aldolase activity Inferred from sequence or structural similarity. Source: PomBase 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 – 358	358	Fructose-bisphosphate aldolase		PRO_0000178761
Regions
	Region	265 – 267	3	Dihydroxyacetone phosphate binding By similarity
	Region	286 – 289	4	Dihydroxyacetone phosphate binding By similarity
Sites
	Active site	108	1	Proton donor By similarity
	Metal binding	109	1	Zinc 1; catalytic By similarity
	Metal binding	143	1	Zinc 2 By similarity
	Metal binding	173	1	Zinc 2 By similarity
	Metal binding	225	1	Zinc 1; catalytic By similarity
	Metal binding	264	1	Zinc 1; catalytic By similarity
	Binding site	61	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	226	1	Dihydroxyacetone phosphate; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	289	1	Phosphothreonine Ref.3
	Modified residue	312	1	Phosphothreonine Ref.3
	Modified residue	340	1	Phosphothreonine Ref.3
	Modified residue	342	1	Phosphothreonine Ref.3
Experimental info
	Sequence conflict	13	1	T → A in BAA04237. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P36580 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: 50111C1C0E6DD05E	FASTA	358	39,570
	10 20 30 40 50 60 MGILDIVPTG VITGDNVLKL FTYAREHGFA IPAINVTSSS TAIAALEAAR EARSPIILQT 70 80 90 100 110 120 SNGGAHFFAG KESSNEGQKA SIAGSIAAAH YIRSIAPFFG VPVVMHSDHC AKKLLPWMDG 130 140 150 160 170 180 MFEADEAYFK IHGEPLFSSH MLDLSEEPKK ENIAQVKEYC KRAVPMKIWI EMEIGITGGE 190 200 210 220 230 240 EDGVDNSHVS HTELYTQPED IWDVYRELSS VTPYFSIAAA FGNVHGVYKP GNVKLQPALL 250 260 270 280 290 300 GQHQAYVKEQ LKTTNDKPVF FVFHGGSGSS VNEFRTGIKC GVVKVNIDTD TQFAYVEGVR 310 320 330 340 350 DYVLKYKDYL MTPVGNPEGA DKPNKKKFDP RVWIHEGEKT MTKRVLTALE DFYTVNTL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and nucleotide sequencing of Schizosaccharomyces pombe homologue of the class II fructose-1,6-bisphosphate aldolase gene." Mutoh N., Hayashi Y. Biochim. Biophys. Acta 1183:550-552(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-289; THR-312; THR-340 AND THR-342, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D17415 Genomic DNA. Translation: BAA04237.1. CU329671 Genomic DNA. Translation: CAB52034.1.
PIR	T39798. T43289.
RefSeq	NP_595692.1. NM_001021589.2.
3D structure databases
ProteinModelPortal	P36580.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4688656.
STRING	4896.SPBC19C2.07-1.
Proteomic databases
PaxDb	P36580.
PRIDE	P36580.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC19C2.07.1; SPBC19C2.07.1:pep; SPBC19C2.07.
GeneID	2540767.
KEGG	spo:SPBC19C2.07.
Organism-specific databases
PomBase	SPBC19C2.07.
Phylogenomic databases
eggNOG	COG0191.
HOGENOM	HOG000227794.
KO	K01624.
OMA	REGEKTM.
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...
Other
NextBio	20801886.

Entry information

Entry name

ALF_SCHPO

Accession

Primary (citable) accession number: P36580
Secondary accession number(s): Q9UUD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 11, 2001
Last modified:	May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program