Reviewed, UniProtKB/Swiss-Prot Q55664 (ALF2_SYNY3)

Names and origin

Protein names

Recommended name:
    Fructose-bisphosphate aldolase class 2
      Short name=FBP aldolase
      Short name=FBPA
    EC=4.1.2.13
Alternative name(s):
    Fructose-bisphosphate aldolase class II
    Fructose-1,6-bisphosphate aldolase

Gene names

Name:	fbaA
Synonyms:	fda
Ordered Locus Names:	sll0018

Organism

Synechocystis sp. (strain PCC 6803) [Complete proteome] [HAMAP]

Taxonomic identifier

1148 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

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.
Sequence similarities	Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 359	358	Fructose-bisphosphate aldolase class 2		PRO_0000178751
Regions
	Region	233 – 235	3	Dihydroxyacetone phosphate binding By similarity
	Region	275 – 278	4	Dihydroxyacetone phosphate binding By similarity
Sites
	Active site	83	1	Proton donor By similarity
	Metal binding	84	1	Zinc 1; catalytic By similarity
	Metal binding	105	1	Zinc 2 By similarity
	Metal binding	142	1	Zinc 2 By similarity
	Metal binding	198	1	Zinc 1; catalytic By similarity
	Metal binding	232	1	Zinc 1; catalytic By similarity
	Binding site	50	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	199	1	Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55664-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 2D005351B70931C3	FASTA	359	38,972
	10 20 30 40 50 60 MALVPMRLLL DHAAENGYGI PAFNVNNMEQ IISIMQAADE TDSPVILQAS RGARSYAGEN 70 80 90 100 110 120 FLRHLVLGAV ETYPHIPIAM HQDHGNSPAT CYSAIRNGFT SVMMDGSLEA DAKTPASFEY 130 140 150 160 170 180 NVNVTAEVVK VAHSVGASVE GELGCLGSLE TGQGEAEDGH GFEGKLDHSQ LLTDPEEAVE 190 200 210 220 230 240 FVNKTQVDAL AVAIGTSHGA YKFTRKPTGE VLAISRIEEI HRLLPNTHLV MHGSSSVPQE 250 260 270 280 290 300 WIDMINEFGG AIPETYGVPV EEIQKGIKSG VRKVNIDTDN RLAITAAFRE AAAKDPKNFD 310 320 330 340 350 PRHFLKPSIK YMKQVCADRY QQFWTAGNAS KIKQLTLDDY AAKYAKGELT ATSRTSVAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome." Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S. DNA Res. 2:153-166(1995) [PubMed: 8590279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Towards a proteome project of cyanobacterium Synechocystis sp. strain PCC6803: linking 130 protein spots with their respective genes." Sazuka T., Ohara O. Electrophoresis 18:1252-1258(1997) [PubMed: 9298645] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000022 Genomic DNA. Translation: BAA10184.1.
PIR	S76332.
RefSeq	NP_442114.1.
3D structure databases
SMR	Q55664. Positions 3-329.
ModBase	Search...
Protein-protein interaction databases
STRING	Q55664.
Genome annotation databases
GeneID	952668.
GenomeReviews	Gene locus sll0018 in contig BA000022_GR.
KEGG	syn:sll0018.
NMPDR	fig|1148.1.peg.2215.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0191.
HOGENOM	HBG327581.
OMA	EWLKIIN.
PhylomeDB	Q55664.
Enzyme and pathway databases
BioCyc	SSP1148:SLL0018-MONOMER.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR006412. Fruct_bisP_Calv. 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.
TIGRFAMs	TIGR00167. cbbA. 1 hit. TIGR01521. FruBisAldo_II_B. 1 hit.
PROSITE	PS00602. ALDOLASE_CLASS_II_1. 1 hit. PS00806. ALDOLASE_CLASS_II_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALF2_SYNY3

Accession

Primary (citable) accession number: Q55664

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 64 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)