UniProt Accession

 ALF_ECOLI; P0AB71; P11604; Q2M9R7 

Genbank Protein ID

 X14436; U28377; U00096; AP009048 

Genbank Nucleotide ID

 CAA32605.1; AAA69092.1; AAC75962.1; BAE76989.1 

Protein Name

 Fructose-bisphosphate aldolase class 2 

Protein Synonyms/Alias

 FBP aldolase; FBPA; Fructose-1,6-bisphosphate aldolase; Fructose-bisphosphate aldolase class II 

Gene Name

 fbaA 

Gene Synonyms/Alias

 fba; fda; b2925; JW2892 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
3	*****MSKIFDFVKP	acetylation	[1, 2]
9	SKIFDFVKPGVITGD	acetylation	[1, 2, 3]
20	ITGDDVQKVFQVAKE	acetylation	[1, 2]
26	QKVFQVAKENNFALP	acetylation	[1]
52	AVLETAAKVKAPVIV	acetylation	[2]
54	LETAAKVKAPVIVQF	acetylation	[1, 2]
72	GASFIAGKGVKSDVP	acetylation	[1, 2]
75	FIAGKGVKSDVPQGA	acetylation	[2]
114	LHTDHCAKKLLPWID	acetylation	[1, 2]
115	HTDHCAKKLLPWIDG	acetylation	[1, 2]
129	GLLDAGEKHFAATGK	acetylation	[1, 2]
231	GNVHGVYKPGNVVLT	acetylation	[2]
251	DSQEYVSKKHNLPHN	acetylation	[1, 2]
252	SQEYVSKKHNLPHNS	acetylation	[1, 2]
276	GSTAQEIKDSVSYGV	acetylation	[1, 2]
319	QGQLGNPKGEDQPNK	acetylation	[1, 2]
326	KGEDQPNKKYYDPRV	acetylation	[1, 2]
327	GEDQPNKKYYDPRVW	acetylation	[2]
348	SMIARLEKAFQELNA	acetylation	[1, 2]

Reference

 [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [2] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [3] 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 CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842] 

Functional Description

 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. 

Sequence Annotation

 REGION 266 268 Dihydroxyacetone phosphate binding.
 REGION 287 290 Dihydroxyacetone phosphate binding.
 ACT_SITE 110 110 Proton donor.
 METAL 111 111 Zinc 1; catalytic.
 METAL 145 145 Zinc 2.
 METAL 175 175 Zinc 2.
 METAL 227 227 Zinc 1; catalytic.
 METAL 265 265 Zinc 1; catalytic.
 BINDING 62 62 Glyceraldehyde 3-phosphate (Probable).
 BINDING 228 228 Dihydroxyacetone phosphate; via amide
 MOD_RES 9 9 N6-acetyllysine; alternate.
 MOD_RES 9 9 N6-malonyllysine; alternate.
 MOD_RES 9 9 N6-succinyllysine; alternate.
 MOD_RES 72 72 N6-succinyllysine.
 MOD_RES 115 115 N6-succinyllysine.
 MOD_RES 231 231 N6-succinyllysine.
 MOD_RES 251 251 N6-succinyllysine.
 MOD_RES 319 319 N6-succinyllysine.
 MOD_RES 326 326 N6-succinyllysine.
 MOD_RES 348 348 N6-succinyllysine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 359 AA 

Protein Sequence

Gene Ontology

 GO:0004332; F:fructose-bisphosphate aldolase activity; IMP:EcoliWiki.
 GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
 GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway. 

Interpro

 IPR013785; Aldolase_TIM.
 IPR006411; Fruct_bisP_bact.
 IPR000771; Ketose_bisP_aldolase_II. 

Pfam

 PF01116; F_bP_aldolase 

SMART

  

PROSITE

 PS00602; ALDOLASE_CLASS_II_1
 PS00806; ALDOLASE_CLASS_II_2 

PRINTS