P78055 (FSAA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fructose-6-phosphate aldolase 1
EC=4.1.2.-

Gene names

Name:	fsaA
Synonyms:	fsa, mipB, ybiZ
Ordered Locus Names:	b0825, JW5109

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-fructose 6-phosphate = glycerone + D-glyceraldehyde 3-phosphate. HAMAP MF_00496
Enzyme regulation	Inhibited by glycerol, inorganic phosphate and arabinose 5-phosphate. HAMAP MF_00496
Subunit structure	Homodecamer or homododecamer.
Subcellular location	Cytoplasm HAMAP MF_00496.
Sequence similarities	Belongs to the transaldolase family. Type 3A subfamily.
Mass spectrometry	Molecular mass is 22998 Da from positions 1 - 220. Determined by ESI. Ref.5

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aldehyde-lyase activity 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 – 220

220

Fructose-6-phosphate aldolase 1 HAMAP MF_00496

PRO_0000173643

Sites

Active site

85

1

Experimental info

Mutagenesis

85

1

K → R: Almost complete loss of activity. Ref.5

Secondary structure

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220

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

10 – 17

8

Beta strand

24 – 26

3

Helix

29 – 35

7

Helix

39 – 49

11

Turn

50 – 52

3

Beta strand

54 – 59

6

Helix

65 – 78

14

Beta strand

83 – 87

5

Helix

90 – 102

13

Beta strand

106 – 111

6

Helix

114 – 123

10

Beta strand

126 – 131

6

Helix

132 – 137

6

Helix

142 – 156

15

Beta strand

161 – 165

5

Helix

170 – 178

9

Beta strand

182 – 186

5

Helix

188 – 193

6

Helix

198 – 215

18

Sequences

	Sequence		Length	Mass (Da)
	P78055 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: 317B9A06CD19C587	FASTA	220	22,997
	10 20 30 40 50 60 MELYLDTSDV VAVKALSRIF PLAGVTTNPS IIAAGKKPLD VVLPQLHEAM GGQGRLFAQV 70 80 90 100 110 120 MATTAEGMVN DALKLRSIIA DIVVKVPVTA EGLAAIKMLK AEGIPTLGTA VYGAAQGLLS 130 140 150 160 170 180 ALAGAEYVAP YVNRIDAQGG SGIQTVTDLH QLLKMHAPQA KVLAASFKTP RQALDCLLAG 190 200 210 220 CESITLPLDV AQQMISYPAV DAAVAKFEQD WQGAFGRTSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Isomura M., Ogino T., Mizuno T. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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]	"Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia coli and is related to a novel group of bacterial transaldolases." Schuermann M., Sprenger G.A. J. Biol. Chem. 276:11055-11061(2001) [PubMed: 11120740] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10, CHARACTERIZATION, MASS SPECTROMETRY, MUTAGENESIS OF LYS-85. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D88188 Genomic DNA. Translation: BAA13552.1.
U00096 Genomic DNA. Translation: AAC73912.2.
AP009048 Genomic DNA. Translation: BAA35513.2.

PIR

A64820.

RefSeq

NP_415346.4. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L6W	X-ray	1.93	A/B/C/D/E/F/G/H/I/J	1-220	[»]

ProteinModelPortal

P78055.

SMR

P78055. Positions 1-220.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10218N.

IntAct

P78055. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003904; EBESCP00000003904; EBESCG00000003192.
EBESCT00000015808; EBESCP00000015099; EBESCG00000014868.

GeneID

945449.

GenomeReviews

Gene locus JW5109 in contig AP009048_GR.
Gene locus b0825 in contig U00096_GR.

KEGG

ecj:JW5109.
eco:b0825.

PATRIC

32116853. VBIEscCol129921_0852.

Organism-specific databases

EchoBASE

EB3244.

EcoGene

EG13471. fsaA.

Phylogenomic databases

eggNOG

COG0176.

GeneTree

EBGT00050000009452.

HOGENOM

HBG533000.

OMA

SIHVQVV.

PhylomeDB

P78055.

ProtClustDB

PRK12653.

Enzyme and pathway databases

BioCyc

EcoCyc:G6428-MONOMER.
MetaCyc:G6428-MONOMER.

Gene expression databases

Genevestigator

P78055.

Family and domain databases

HAMAP

MF_00496. F6P_aldolase.
[Tree]

InterPro

IPR013785. Aldolase_TIM.
IPR023001. F6P_aldolase.
IPR001585. Transaldolase.
IPR004731. Transaldolase_3A/3B.
IPR018225. Transaldolase_AS.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

KO

K08313.

PANTHER

PTHR10683. Transaldolase. 1 hit.

Pfam

PF00923. Transaldolase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00875. Fsa_talC_mipB. 1 hit.

PROSITE

PS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FSAA_ECOLI

Accession

Primary (citable) accession number: P78055
Secondary accession number(s): P77855, Q9R3X3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	January 25, 2012
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program