P0AB71 (ALF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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-1,6-bisphosphate aldolase
Fructose-bisphosphate aldolase class II

Gene names

Name:	fbaA
Synonyms:	fba, fda
Ordered Locus Names:	b2925, JW2892

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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. Ref.8
Catalytic activity	D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Ref.8
Cofactor	Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution.
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the class II fructose-bisphosphate aldolase family.
Biophysicochemical properties	Kinetic parameters: The catalytic efficiency measured with fructose-1,6-bisphosphate as substrate is 1440-fold higher than that with tagatose-1,6-bisphosphate. KM=0.17 mM for fructose-1,6-bisphosphate Ref.8 KM=0.35 mM for tagatose-1,6-bisphosphate

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	fructose-bisphosphate aldolase activity Inferred from mutant phenotype. Source: EcoliWiki protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from direct assay Ref.7. Source: EcoliWiki
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
dnaK	P0A6Y8	2	EBI-370916,EBI-542092

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2 Ref.5 Ref.6

Chain

2 – 359

358

Fructose-bisphosphate aldolase class 2

PRO_0000178713

Regions

Region

266 – 268

3

Dihydroxyacetone phosphate binding

Region

287 – 290

4

Dihydroxyacetone phosphate binding

Sites

Active site

110

1

Proton donor Ref.12

Metal binding

111

1

Zinc 1; catalytic

Metal binding

145

1

Zinc 2

Metal binding

175

1

Zinc 2

Metal binding

227

1

Zinc 1; catalytic

Metal binding

265

1

Zinc 1; catalytic

Binding site

62

1

Glyceraldehyde 3-phosphate Probable

Binding site

228

1

Dihydroxyacetone phosphate; via amide nitrogen

Amino acid modifications

Modified residue

9

1

N6-acetyllysine Ref.9

Experimental info

Mutagenesis

36

1

N → A: 1.5% of wild-type activity. 5-fold decrease in FBP affinity. Ref.8

Mutagenesis

60

1

Q → A: 81% of wild-type activity. 1.3-fold decrease in FBP affinity. Ref.8

Mutagenesis

62

1

S → A: 8% of wild-type activity. 16-fold decrease in FBP affinity. Ref.8

Mutagenesis

62

1

S → T: 60% of wild-type activity. 2.5-fold decrease in FBP affinity. Ref.8

Mutagenesis

108

1

H → A: Loss of activity. Ref.7

Mutagenesis

111

1

H → A: Loss of activity. Ref.7

Mutagenesis

112

1

C → A: Partial loss of activity. Ref.7

Mutagenesis

326

1

K → A: 6% of wild-type activity. 2.2-fold decrease in FBP affinity. Ref.8

Secondary structure

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359

Helix Strand Turn

Details...

Helix

4 – 6

3

Beta strand

10 – 12

3

Helix

17 – 27

11

Beta strand

32 – 36

5

Helix

40 – 53

14

Beta strand

57 – 61

5

Helix

63 – 70

8

Helix

81 – 101

21

Beta strand

104 – 109

6

Helix

114 – 116

3

Helix

117 – 134

18

Beta strand

140 – 144

5

Helix

151 – 166

16

Turn

167 – 169

3

Beta strand

171 – 177

7

Helix

200 – 210

11

Turn

211 – 213

3

Beta strand

217 – 221

5

Helix

240 – 253

14

Beta strand

262 – 264

3

Helix

272 – 280

9

Beta strand

283 – 288

6

Helix

290 – 306

17

Helix

308 – 310

3

Beta strand

311 – 317

7

Beta strand

320 – 324

5

Helix

326 – 329

4

Helix

331 – 352

22

Sequences

	Sequence		Length	Mass (Da)
	P0AB71 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 7A076D9EA62FBEC4	FASTA	359	39,147
	10 20 30 40 50 60 MSKIFDFVKP GVITGDDVQK VFQVAKENNF ALPAVNCVGT DSINAVLETA AKVKAPVIVQ 70 80 90 100 110 120 FSNGGASFIA GKGVKSDVPQ GAAILGAISG AHHVHQMAEH YGVPVILHTD HCAKKLLPWI 130 140 150 160 170 180 DGLLDAGEKH FAATGKPLFS SHMIDLSEES LQENIEICSK YLERMSKIGM TLEIELGCTG 190 200 210 220 230 240 GEEDGVDNSH MDASALYTQP EDVDYAYTEL SKISPRFTIA ASFGNVHGVY KPGNVVLTPT 250 260 270 280 290 300 ILRDSQEYVS KKHNLPHNSL NFVFHGGSGS TAQEIKDSVS YGVVKMNIDT DTQWATWEGV 310 320 330 340 350 LNYYKANEAY LQGQLGNPKG EDQPNKKYYD PRVWLRAGQT SMIARLEKAF QELNAIDVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli." Alefounder P.R., Perham R.N. Mol. Microbiol. 3:723-732(1989) [PubMed: 2546007] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / CS520.
[2]	"Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli." Alefounder P.R., Baldwin S.A., Perham R.N., Short N.J. Biochem. J. 257:529-534(1989) [PubMed: 2649077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-27.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[6]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed: 9600841] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli." Berry A., Marshall K.E. FEBS Lett. 318:11-16(1993) [PubMed: 8436219] [Abstract] Cited for: MUTAGENESIS OF HIS-108; HIS-111 AND CYS-112.
[8]	"Exploring substrate binding and discrimination in fructose 1,6-bisphosphate and tagatose 1,6-bisphosphate aldolases." Zgiby S.M., Thomson G.J., Qamar S., Berry A. Eur. J. Biochem. 267:1858-1868(2000) [PubMed: 10712619] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, REACTION MECHANISM, MUTAGENESIS OF ASN-36; GLN-60; SER-62 AND LYS-326. Strain: K12 / MG1655 / ATCC 47076.
[9]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[10]	"Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase." Blom N.S., Tetreault S., Coulombe R., Sygusch J. Nat. Struct. Biol. 3:856-862(1996) [PubMed: 8836102] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH ZINC.
[11]	"The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold." Cooper S.J., Leonard G.A., McSweeney S.M., Thompson A.W., Naismith J.H., Qamar S., Plater A., Berry A., Hunter W.N. Structure 4:1303-1315(1996) [PubMed: 8939754] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ZINC.
[12]	"The crystal structure of Escherichia coli class II fructose-1, 6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity." Hall D.R., Leonard G.A., Reed C.D., Watt C.I., Berry A., Hunter W.N. J. Mol. Biol. 287:383-394(1999) [PubMed: 10080900] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC AND TRANSITION STATE ANALOG, ACTIVE SITE.
[13]	"The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase." Hall D.R., Kemp L.E., Leonard G.A., Marshall K., Berry A., Hunter W.N. Acta Crystallogr. D 59:611-614(2003) [PubMed: 12595741] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CADMIUM, METAL BINDING SITES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X14436 Genomic DNA. Translation: CAA32605.1.
U28377 Genomic DNA. Translation: AAA69092.1.
U00096 Genomic DNA. Translation: AAC75962.1.
AP009048 Genomic DNA. Translation: BAE76989.1.

PIR

ADEC2A. S02177.

RefSeq

NP_417400.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B57	X-ray	2.00	A/B	2-359	[»]
1DOS	X-ray	1.67	A/B	2-359	[»]
1GYN	X-ray	2.00	A	2-359	[»]
1ZEN	X-ray	2.50	A	2-359	[»]

ProteinModelPortal

P0AB71.

SMR

P0AB71. Positions 2-359.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31872N.

IntAct

P0AB71. 7 interactions.

2D gel databases

SWISS-2DPAGE

P0AB71.

2DBase-Ecoli

P0AB71.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000005019; EBESCP00000005019; EBESCG00000004096.
EBESCT00000005020; EBESCP00000005020; EBESCG00000004096.
EBESCT00000017979; EBESCP00000017270; EBESCG00000017035.

GeneID

947415.

GenomeReviews

Gene locus JW2892 in contig AP009048_GR.
Gene locus b2925 in contig U00096_GR.

KEGG

ecj:JW2892.
eco:b2925.

PATRIC

32121264. VBIEscCol129921_3020.

Organism-specific databases

EchoBASE

EB0278.

EcoGene

EG10282. fbaA.

Phylogenomic databases

eggNOG

COG0191.

GeneTree

EBGT00050000009021.

HOGENOM

HBG327581.

OMA

RMAKMGM.

PhylomeDB

P0AB71.

ProtClustDB

PRK09197.

Enzyme and pathway databases

BioCyc

EcoCyc:FRUCTBISALD-CLASSII-MONOMER.
MetaCyc:FRUCTBISALD-CLASSII-MONOMER.

Gene expression databases

Genevestigator

P0AB71.

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.

KO

K01624.

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...

Entry information

Entry name

ALF_ECOLI

Accession

Primary (citable) accession number: P0AB71
Secondary accession number(s): P11604, Q2M9R7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program