P29356 (ALF_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Fructose-bisphosphate aldolase, cytoplasmic isozyme EC=4.1.2.13
Organism	Spinacia oleracea (Spinach)
Taxonomic identifier	3562 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	Schiff base
Molecular function	Lyase
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 357	357	Fructose-bisphosphate aldolase, cytoplasmic isozyme		PRO_0000216925
Sites
	Active site	183	1	Proton acceptor By similarity
	Active site	225	1	Schiff-base intermediate with dihydroxyacetone-P By similarity
	Binding site	53	1	Substrate By similarity
	Binding site	142	1	Substrate By similarity
	Site	357	1	Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P29356 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 33150E3D80B1C6DE	FASTA	357	38,471
	10 20 30 40 50 60 MTAYRGKYAD ELIANASYIA TPGKVILAAD ESTGTIGKRF PSINVENVES NRRALRELLF 70 80 90 100 110 120 TTPGALPYLS GVILFEETLY QKTADGKPFV DAMKDGGVLP GIKVDKGTVE LAGTNGETTT 130 140 150 160 170 180 QGLDGLAQRC AQYYTAGARF AKWRAVLKIG PTEPSPLAIL ENANGLARYG IICQENGLVP 190 200 210 220 230 240 IVEPEILVDG THDIDRCAEV SERVLAACYK ALNDHHVLLE GTSLKPNIVT PGSESKKVTP 250 260 270 280 290 300 EVIAEYTVRT LQRTVPQAVP GVMFLSGGQS EEEATLNLNA MNKLETKKPW TLSFSYGRAL 310 320 330 340 350 QQSTLKAWQG KEENVAKAQE VFLARAKGNS EATLGKYQGG AGGADASESL HVKDYKY

References

[1]	"Plant aldolase: cDNA and deduced amino-acid sequences of the chloroplast and cytosol enzyme from spinach." Pelzer-Reith B., Penger A., Schnarrenberger C. Plant Mol. Biol. 21:331-340(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leaf.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X65742 mRNA. Translation: CAA46649.1.
PIR	ADSPAC. S31091.
3D structure databases
ProteinModelPortal	P29356.
SMR	P29356. Positions 11-357.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
SABIO-RK	P29356.
UniPathway	UPA00109; UER00183.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR000741. Aldolase_I. IPR013785. Aldolase_TIM. [Graphical view]
PANTHER	PTHR11627. PTHR11627. 1 hit.
Pfam	PF00274. Glycolytic. 1 hit. [Graphical view]
PROSITE	PS00158. ALDOLASE_CLASS_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALF_SPIOL

Accession

Primary (citable) accession number: P29356

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	April 3, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program