O66496 (KDSA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-dehydro-3-deoxyphosphooctonate aldolase
EC=2.5.1.55

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

Gene names

Name:	kdsA
Ordered Locus Names:	aq_085

Organism

Aquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Aquificae › Aquificae › Aquificales › Aquificaceae › Aquifex › Aquifex aeolicus

Protein attributes

Sequence length	267 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate. HAMAP-Rule 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-Rule MF_00056 Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. HAMAP-Rule MF_00056
Subunit structure	Oligomer.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the KdsA family.

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	keto-3-deoxy-D-manno-octulosonic acid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 267

267

2-dehydro-3-deoxyphosphooctonate aldolase HAMAP-Rule MF_00056

PRO_0000187099

Secondary structure

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267

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Helix

16 – 32

17

Beta strand

36 – 41

6

Helix

60 – 74

15

Beta strand

77 – 81

5

Helix

85 – 87

3

Helix

88 – 92

5

Beta strand

96 – 100

5

Helix

102 – 104

3

Helix

108 – 115

8

Turn

116 – 118

3

Beta strand

119 – 124

6

Helix

131 – 134

4

Helix

135 – 143

9

Beta strand

147 – 153

7

Beta strand

159 – 161

3

Helix

169 – 173

5

Turn

174 – 176

3

Beta strand

177 – 182

6

Helix

185 – 187

3

Turn

190 – 193

4

Beta strand

194 – 196

3

Helix

201 – 203

3

Helix

204 – 214

11

Beta strand

217 – 225

9

Helix

227 – 229

3

Beta strand

231 – 233

3

Turn

234 – 236

3

Beta strand

237 – 239

3

Helix

240 – 242

3

Helix

243 – 258

16

Sequences

	Sequence		Length	Mass (Da)
	O66496 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 0A3CFEA3337F1964	FASTA	267	29,734
	10 20 30 40 50 60 MEKFLVIAGP CAIESEELLL KVGEEIKRLS EKFKEVEFVF KSSFDKANRS SIHSFRGHGL 70 80 90 100 110 120 EYGVKALRKV KEEFGLKITT DIHESWQAEP VAEVADIIQI PAFLCRQTDL LLAAAKTGRA 130 140 150 160 170 180 VNVKKGQFLA PWDTKNVVEK LKFGGAKEIY LTERGTTFGY NNLVVDFRSL PIMKQWAKVI 190 200 210 220 230 240 YDATHSVQLP GGLGDKSGGM REFIFPLIRA AVAVGCDGVF METHPEPEKA LSDASTQLPL 250 260 SQLEGIIEAI LEIREVASKY YETIPVK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
[2]	"Functional and biochemical characterization of a recombinant 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase from the hyperthermophilic bacterium Aquifex aeolicus." Duewel H.S., Sheflyan G.Y., Woodard R.W. Biochem. Biophys. Res. Commun. 263:346-351(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[3]	"Function of His185 in Aquifex aeolicus 3-deoxy-D-manno-octulosonate 8-phosphate synthase." Wang J., Duewel H.S., Stuckey J.A., Woodard R.W., Gatti D.L. J. Mol. Biol. 324:205-214(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000657 Genomic DNA. Translation: AAC06457.1.

PIR

E70308.

RefSeq

NP_213056.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FWN	X-ray	1.94	A/B	1-267	[»]
1FWS	X-ray	1.90	A/B	1-267	[»]
1FWT	X-ray	1.90	A/B	1-267	[»]
1FWW	X-ray	1.85	A/B	1-267	[»]
1FX6	X-ray	2.06	A/B	1-267	[»]
1FXP	X-ray	1.80	A/B	1-267	[»]
1FXQ	X-ray	1.80	A/B	1-267	[»]
1FY6	X-ray	1.89	A/B	1-267	[»]
1JCX	X-ray	1.80	A/B	1-267	[»]
1JCY	X-ray	1.90	A/B	1-267	[»]
1LRN	X-ray	2.10	A/B	1-267	[»]
1LRO	X-ray	1.80	A/B	1-267	[»]
1LRQ	X-ray	1.80	A/B	1-267	[»]
1PCK	X-ray	1.80	A/B	1-267	[»]
1PCW	X-ray	1.85	A/B	1-267	[»]
1PE1	X-ray	1.74	A/B	1-267	[»]
1T8X	X-ray	1.80	A/B	1-267	[»]
1T96	X-ray	1.85	A/B	1-267	[»]
1T99	X-ray	1.85	A/B	1-267	[»]
1ZHA	X-ray	1.74	A/B	1-267	[»]
1ZJI	X-ray	2.25	A/B	1-267	[»]
2A21	X-ray	1.80	A/B	1-267	[»]
2A2I	X-ray	1.95	A/B	1-267	[»]
2EF9	X-ray	2.00	A/B	1-267	[»]
2NWR	X-ray	1.50	A/B	1-267	[»]
2NWS	X-ray	1.80	A/B	1-267	[»]
2NX1	X-ray	1.80	A/B	1-267	[»]
2NX3	X-ray	2.10	A/B/C/D/E/F/G/H/I/J/K/L	1-267	[»]
2NXG	X-ray	1.95	A/B	2-264	[»]
2NXH	X-ray	2.11	A/B/C/D/E/F/G/H/I/J/K/L	2-264	[»]
2NXI	X-ray	2.30	A/B/C/D/E/F/G/H/I/J/K/L	2-264	[»]
3E0I	X-ray	1.70	A/B	1-267	[»]
3E12	X-ray	1.70	A/B	1-267	[»]

ProteinModelPortal

O66496.

SMR

O66496. Positions 2-264.

ModBase

Search...

Protein-protein interaction databases

STRING

224324.aq_085.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC06457; AAC06457; aq_085.

GeneID

1192509.

KEGG

aae:aq_085.

PATRIC

20957869. VBIAquAeo85532_0075.

Phylogenomic databases

eggNOG

COG2877.

HOGENOM

HOG000023021.

KO

K01627.

OMA

YHEDESI.

ProtClustDB

PRK05198.

Enzyme and pathway databases

BioCyc

AAEO224324:GJBH-71-MONOMER.

BRENDA

2.5.1.55. 396.

UniPathway

UPA00030.
UPA00357; UER00474.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

HAMAP

MF_00056. KDO8P_synth.

InterPro

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

PANTHER

PTHR21057:SF2. PTHR21057:SF2. 1 hit.

Pfam

PF00793. DAHP_synth_1. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01362. KDO8P_synth. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O66496.

Entry information

Entry name

KDSA_AQUAE

Accession

Primary (citable) accession number: O66496

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program