Reviewed, UniProtKB/Swiss-Prot P0A715 (KDSA_ECOLI)

Names and origin

Protein names

Recommended name:
    2-dehydro-3-deoxyphosphooctonate aldolase
    EC=2.5.1.55
Alternative name(s):
    Phospho-2-dehydro-3-deoxyoctonate aldolase
    3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase
    KDO-8-phosphate synthetase
      Short name=KDO 8-P synthase
      Short name=KDOPS

Gene names

Name:	kdsA
Ordered Locus Names:	b1215, JW1206

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	284 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Synthesis of KDO 8-P which is required for lipid A maturation and cellular growth. HAMAP MF_00056
Catalytic activity	Phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate. HAMAP MF_00056
Pathway	Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. HAMAP MF_00056 Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. HAMAP MF_00056
Subunit structure	Homotrimer. HAMAP MF_00056
Subcellular location	Cytoplasm. HAMAP MF_00056
Sequence similarities	Belongs to the kdsA family.
Mass spectrometry	Molecular mass is 30842±17 Da from positions 1 - 284. Determined by ESI. Ref.9

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	keto-3-deoxy-D-manno-octulosonic acid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	3-deoxy-8-phosphooctulonate synthase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 284

284

2-dehydro-3-deoxyphosphooctonate aldolase HAMAP MF_00056

PRO_0000187124

Experimental info

Sequence conflict

22

1

F → L in CAA29067. Ref.1

Secondary structure

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284

Helix Strand Turn

Details...

Beta strand

6 – 8

3

Beta strand

11 – 13

3

Beta strand

20 – 27

8

Helix

31 – 48

18

Beta strand

52 – 58

7

Helix

73 – 88

16

Beta strand

91 – 95

5

Helix

99 – 101

3

Helix

102 – 106

5

Beta strand

110 – 114

5

Helix

116 – 118

3

Helix

122 – 130

9

Beta strand

134 – 138

5

Helix

145 – 147

3

Helix

148 – 157

10

Beta strand

163 – 167

5

Beta strand

173 – 175

3

Helix

183 – 190

8

Beta strand

196 – 199

4

Helix

200 – 203

4

Helix

221 – 231

11

Beta strand

234 – 243

10

Helix

257 – 259

3

Helix

260 – 276

17

Sequences

	Sequence		Length	Mass (Da)
	P0A715-1 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 35E79D692D134535	FASTA	284	30,833
	10 20 30 40 50 60 MKQKVVSIGD INVANDLPFV LFGGMNVLES RDLAMRICEH YVTVTQKLGI PYVFKASFDK 70 80 90 100 110 120 ANRSSIHSYR GPGLEEGMKI FQELKQTFGV KIITDVHEPS QAQPVADVVD VIQLPAFLAR 130 140 150 160 170 180 QTDLVEAMAK TGAVINVKKP QFVSPGQMGN IVDKFKEGGN EKVILCDRGA NFGYDNLVVD 190 200 210 220 230 240 MLGFSIMKKV SGNSPVIFDV THALQCRDPF GAASGGRRAQ VAELARAGMA VGLAGLFIEA 250 260 270 280 HPDPEHAKCD GPSALPLAKL EPFLKQMKAI DDLVKGFEEL DTSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The kdsA gene coding for 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase is part of an operon in Escherichia coli." Woisetschlaeger M., Hoegenauer G. Mol. Gen. Genet. 207:369-373(1987) [PubMed: 3039295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12." Strohmaier H., Remler P., Renner W., Hoegenauer G. J. Bacteriol. 177:4488-4500(1995) [PubMed: 7543480] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"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.
[4]	"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.
[5]	"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.
[6]	"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 1-12. Strain: K12 / EMG2.
[7]	"Overproduction and one-step purification of Escherichia coli 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase and oxygen transfer studies during catalysis using isotopic-shifted heteronuclear NMR." Dotson G.D., Dua R.K., Clemens J.C., Wooten E.W., Woodard R.W. J. Biol. Chem. 270:13698-13705(1995) [PubMed: 7775423] [Abstract] Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 1-10.
[8]	"3-deoxy-D-manno-octulosonate-8-phosphate synthase from Escherichia coli. Model of binding of phosphoenolpyruvate and D-arabinose-5-phosphate." Wagner T., Kretsinger R.H., Bauerle R., Tolbert W.D. J. Mol. Biol. 301:233-238(2000) [PubMed: 10926505] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[9]	"Crystal structures of KDOP synthase in its binary complexes with the substrate phosphoenolpyruvate and with a mechanism-based inhibitor." Asojo O., Friedman J., Adir N., Belakhov V., Shoham Y., Baasov T. Biochemistry 40:6326-6334(2001) [PubMed: 11371194] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X05552 Genomic DNA. Translation: CAA29067.1.
U18555 Genomic DNA. Translation: AAC43441.1.
U00096 Genomic DNA. Translation: AAC74299.1.
AP009048 Genomic DNA. Translation: BAA36073.1.

PIR

SYECOL. I83573.

RefSeq

AP_001840.1.
NP_415733.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D9E	X-ray	2.40	A/B/C/D	1-284	[»]
1G7U	X-ray	2.80	A	1-284	[»]
1G7V	X-ray	2.40	A	1-284	[»]
1GG0	X-ray	3.00	A	1-284	[»]
1PHQ	X-ray	2.70	A	1-284	[»]
1PHW	X-ray	2.36	A	1-284	[»]
1PL9	X-ray	2.90	A	1-284	[»]
1Q3N	X-ray	2.70	A	1-284	[»]
1X6U	X-ray	2.70	A	1-284	[»]
1X8F	X-ray	2.40	A	1-284	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0A715.

2-D gel databases

SWISS-2DPAGE

P0A715.

Genome annotation databases

GeneID

945785.

GenomeReviews

Gene locus JW1206 in contig AP009048_GR.
Gene locus b1215 in contig U00096_GR.

KEGG

ecj:JW1206.
eco:b1215.

Organism-specific databases

EchoBASE

EB0513.

EcoGene

EG10518. kdsA.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A715.

OMA

VHEPHQA.

Enzyme and pathway databases

BioCyc

EcoCyc:KDO-8PSYNTH-MON.
MetaCyc:KDO-8PSYNTH-MON.

Gene expression databases

Genevestigator

P0A715.

Family and domain databases

HAMAP

MF_00056.
[Tree]

InterPro

IPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006269. KDO8P_synthase.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

PANTHER

PTHR21057:SF2. KDO8P_synthase. 1 hit.

Pfam

PF00793. DAHP_synth_1. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01362. KDO8P_synth. 1 hit.

ProtoNet

Search...

Entry information

Entry name

KDSA_ECOLI

Accession

Primary (citable) accession number: P0A715
Secondary accession number(s): P17579

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	November 3, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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