Q8YHF1 (KDSA_BRUME) 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:	BMEI0850

Organism

Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]

Taxonomic identifier

224914 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	277 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
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
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 – 277

277

2-dehydro-3-deoxyphosphooctonate aldolase HAMAP MF_00056

PRO_0000187107

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

277

Helix Strand Turn

Details...

Beta strand

6 – 9

4

Helix

33 – 39

7

Helix

43 – 49

7

Beta strand

55 – 57

3

Helix

77 – 89

13

Beta strand

94 – 97

4

Helix

101 – 107

7

Turn

108 – 110

3

Beta strand

112 – 116

5

Helix

118 – 120

3

Helix

124 – 132

9

Beta strand

136 – 140

5

Helix

147 – 149

3

Helix

150 – 158

9

Beta strand

165 – 169

5

Helix

185 – 189

5

Beta strand

196 – 199

4

Helix

200 – 203

4

Helix

218 – 220

3

Helix

221 – 230

10

Beta strand

240 – 243

4

Helix

244 – 246

3

Helix

257 – 259

3

Helix

260 – 274

15

Sequences

	Sequence		Length	Mass (Da)
	Q8YHF1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 1C7D6532BA2F0DD8	FASTA	277	29,498
	10 20 30 40 50 60 MVTANSTVKV GNVTFSNSAP LALIAGPCQM ETRDHAFEMA GRLKEMTDKL GIGLVYKSSF 70 80 90 100 110 120 DKANRTSLKA ARGIGLEKAL EVFSDLKKEY GFPVLTDIHT EEQCAAVAPV VDVLQIPAFL 130 140 150 160 170 180 CRQTDLLIAA ARTGRVVNVK KGQFLAPWDM KNVLAKITES GNPNVLATER GVSFGYNTLV 190 200 210 220 230 240 SDMRALPIMA GLGAPVIFDA THSVQQPGGQ GGSTGGQREF VETLARAAVA VGVAGLFIET 250 260 270 HEDPDNAPSD GPNMVPIDKM PALLEKLMAF DRIAKAL

References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R. Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed: 11756688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE008917 Genomic DNA. Translation: AAL52031.1.

PIR

AD3358.

RefSeq

NP_539767.1. NC_003317.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FS2	X-ray	1.85	A/B	1-277	[»]

ProteinModelPortal

Q8YHF1.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1196561.

GenomeReviews

Gene locus BMEI0850 in contig AE008917_GR.

KEGG

bme:BMEI0850.

NMPDR

fig|224914.1.peg.849.

PATRIC

17801879. VBIBruMel146950_3259.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG575990.

OMA

ESRDHAF.

PhylomeDB

Q8YHF1.

ProtClustDB

PRK05198.

Enzyme and pathway databases

BioCyc

BMEL224914:BMEI0850-MONOMER.

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.

KO

K01627.

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_BRUME

Accession

Primary (citable) accession number: Q8YHF1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2002
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program