2-dehydro-3-deoxyphosphooctonate aldolase - Aquifex aeolicus (strain VF5)

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O66496 (KDSA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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)

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

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 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	Oligomer.
Subcellular location	Cytoplasm By similarity HAMAP MF_00056.
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	lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-deoxy-8-phosphooctulonate synthase 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

Chain

1 – 267

267

2-dehydro-3-deoxyphosphooctonate aldolase HAMAP MF_00056

PRO_0000187099

Secondary structure

267

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

O66496 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 0A3CFEA3337F1964
Show »

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

« Hide

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: 9537320] [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: 10491295] [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: 12441100] [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...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1192509.

GenomeReviews

Gene locus aq_085 in contig AE000657_GR.

KEGG

aae:aq_085.

NMPDR

fig|224324.1.peg.71.

PATRIC

20957869. VBIAquAeo85532_0075.

Phylogenomic databases

HOGENOM

HBG575990.

OMA

NFFLMAG.

PhylomeDB

O66496.

ProtClustDB

PRK05198.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_085-MONOMER.

BRENDA

2.5.1.55. 396.

Family and domain databases

HAMAP

MF_00056. KDO8P_synth.
[Tree]

InterPro

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

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

K01627.

Pfam

PF00793. DAHP_synth_1. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01362. KDO8P_synth. 1 hit.

ProtoNet

Search...

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:	January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents