Q703I2 (ALF_THECA) 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:

fba

Organism

Thermus caldophilus

Taxonomic identifier

272 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	305 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	Homotetramer. Ref.1
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	3D-structure
Gene Ontology (GO)
Biological_process	fructose 1,6-bisphosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: EC 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 – 305

305

Fructose-bisphosphate aldolase

PRO_0000178752

Regions

Region

209 – 211

3

Dihydroxyacetone phosphate binding By similarity

Region

251 – 254

4

Dihydroxyacetone phosphate binding By similarity

Sites

Active site

80

1

Proton donor By similarity

Metal binding

81

1

Zinc 1; catalytic By similarity UniProtKB P11604

Metal binding

102

1

Zinc 2 By similarity

Metal binding

132

1

Zinc 2 By similarity

Metal binding

178

1

Zinc 1; catalytic By similarity

Metal binding

208

1

Zinc 1; catalytic By similarity

Binding site

49

1

Glyceraldehyde 3-phosphate By similarity

Binding site

179

1

Dihydroxyacetone phosphate; via amide nitrogen By similarity

Secondary structure

1

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305

Helix Strand Turn

Details...

Helix

6 – 14

9

Beta strand

19 – 23

5

Helix

27 – 38

12

Helix

39 – 41

3

Beta strand

44 – 47

4

Helix

50 – 68

19

Beta strand

75 – 78

4

Helix

85 – 93

9

Beta strand

97 – 101

5

Helix

108 – 124

17

Beta strand

128 – 134

7

Helix

146 – 150

5

Helix

155 – 164

10

Beta strand

178 – 181

4

Beta strand

184 – 186

3

Helix

191 – 200

10

Beta strand

205 – 207

3

Helix

215 – 223

9

Helix

236 – 244

9

Beta strand

247 – 252

6

Helix

254 – 270

17

Helix

277 – 299

23

Sequences

	Sequence		Length	Mass (Da)
	Q703I2 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 9FE260186F29B98A	FASTA	305	32,987
	10 20 30 40 50 60 MLVTGLEILR KARAEGYGVG AFNTNNMEFT QAILEAAEEM KSPVILALSE GAMKYGGRAL 70 80 90 100 110 120 TRMVVALAQE ARVPVAVHLD HGSSYESVLK ALREGFTSVM IDKSHEDFET NVRETKRVVE 130 140 150 160 170 180 AAHAVGVTVE AELGRLAGIE EHVAVDEKDA LLTNPEEARI FMERTGADYL AVAIGTSHGA 190 200 210 220 230 240 YKGKGRPFID HPRLARIAKL VPAPLVLHGA SAVPQELVER FRAAGGEIGE ASGIHPEDIK 250 260 270 280 290 300 KAISLGIAKI NTDTDLRLAF TALVRETLGK NPKEFDPRKY LGPAREAVKE VVKSRMELFG SVGRA

References

[1]	"Crystallization and preliminary X-ray analysis of class II fructose-1,6-bisphosphate aldolase from Thermus caldophilus." Lee J.H., Im Y.J., Rho S.-H., Park S.H., Kim M.-K., Cho S.J., Kim T.-Y., Oh J.H., Shin H.-J., Lee D.-S., Eom S.H. Protein Pept. Lett. 10:511-515(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ621816 Genomic DNA. Translation: CAF32659.1.
AY526903 Genomic DNA. Translation: AAS19362.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FJK	X-ray	2.20	A/B/C/D	1-305	[»]

ProteinModelPortal

Q703I2.

SMR

Q703I2. Positions 1-305.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00109; UER00183.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR013785. Aldolase_TIM.
IPR011289. Fruc_bis_ald_class-2.
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.
TIGR01859. fruc_bis_ald_. 1 hit.

PROSITE

PS00602. ALDOLASE_CLASS_II_1. False negative.
PS00806. ALDOLASE_CLASS_II_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q703I2.

Entry information

Entry name

ALF_THECA

Accession

Primary (citable) accession number: Q703I2
Secondary accession number(s): P83739

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program