Reviewed, UniProtKB/Swiss-Prot P0A991 (ALF1_ECOLI)

Names and origin

Protein names

Recommended name:
    Fructose-bisphosphate aldolase class 1
    EC=4.1.2.13
Alternative name(s):
    Fructose-biphosphate aldolase class I
      Short name=FBP aldolase

Gene names

Name:	fbaB
Synonyms:	dhnA
Ordered Locus Names:	b2097, JW5344

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	350 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)

Catalytic activity	D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.
Enzyme regulation	Activated by citrate.
Subunit structure	Homooctamer or homodecamer.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the deoC/fbaB aldolase family. FbaB subfamily.
Caution	Was originally (Ref.1) thought to be a dehydrin.
Mass spectrometry	Molecular mass is 37979.3 Da from positions 2 - 350. Determined by MALDI. Ref.4

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	Schiff base
Molecular function	Lyase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB membrane Inferred from direct assay. Source: UniProtKB
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
	Initiator methionine	1	1	Removed Ref.4
	Chain	2 – 350	349	Fructose-bisphosphate aldolase class 1		PRO_0000138939
Sites
	Active site	237	1	Schiff-base intermediate with dihydroxyacetone-P
Amino acid modifications
	Modified residue	208	1	N6-acetyllysine Ref.5
	Modified residue	262	1	N6-acetyllysine Ref.5
Experimental info
	Mutagenesis	237	1	K → A: Loss of activity.
	Mutagenesis	239	1	K → A: No change in activity.
	Sequence conflict	192	1	L → V in AAB18249. Ref.1
	Sequence conflict	309	1	N → I in AAB18249. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P0A991-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 462341BE2459E587	FASTA	350	38,109
	10 20 30 40 50 60 MTDIAQLLGK DADNLLQHRC MTIPSDQLYL PGHDYVDRVM IDNNRPPAVL RNMQTLYNTG 70 80 90 100 110 120 RLAGTGYLSI LPVDQGVEHS AGASFAANPL YFDPKNIVEL AIEAGCNCVA STYGVLASVS 130 140 150 160 170 180 RRYAHRIPFL VKLNHNETLS YPNTYDQTLY ASVEQAFNMG AVAVGATIYF GSEESRRQIE 190 200 210 220 230 240 EISAAFERAH ELGMVTVLWA YLRNSAFKKD GVDYHVSADL TGQANHLAAT IGADIVKQKM 250 260 270 280 290 300 AENNGGYKAI NYGYTDDRVY SKLTSENPID LVRYQLANCY MGRAGLINSG GAAGGETDLS 310 320 330 340 350 DAVRTAVINK RAGGMGLILG RKAFKKSMAD GVKLINAVQD VYLDSKITIA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Close T.J., Choi D.W. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"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.
[3]	"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.
[4]	"The dhnA gene of Escherichia coli encodes a class I fructose bisphosphate aldolase." Thomson G.J., Howlett G.J., Ashcroft A.E., Berry A. Biochem. J. 331:437-445(1998) [PubMed: 9531482] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-10, CHARACTERIZATION, MASS SPECTROMETRY.
[5]	"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-208 AND LYS-262, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U73760 Genomic DNA. Translation: AAB18249.1. Different initiation. U00096 Genomic DNA. Translation: AAC75158.1. Different initiation. AP009048 Genomic DNA. Translation: BAE76584.1.
RefSeq	AP_002695.1. NP_416600.4.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	946632.
GenomeReviews	Gene locus JW5344 in contig AP009048_GR. Gene locus b2097 in contig U00096_GR.
KEGG	ecj:JW5344. eco:b2097.
Organism-specific databases
EchoBASE	EB3815.
EcoGene	EG14062. fbaB.
CMR	Search...
Phylogenomic databases
HOGENOM	P0A991.
OMA	P0A991. FTIYPGS.
Enzyme and pathway databases
BioCyc	EcoCyc:FRUCBISALD-CLASSI-MON. MetaCyc:FRUCBISALD-CLASSI-MON.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR002915. DeoC/AroFGH_arch. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF01791. DeoC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALF1_ECOLI

Accession

Primary (citable) accession number: P0A991
Secondary accession number(s): P71295, P76416, Q2MAX2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 32 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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