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B0B8N1 (KDSA_CHLT2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:CTL0024
OrganismChlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B) [Complete proteome] [HAMAP]
Taxonomic identifier471472 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 processLipopolysaccharide biosynthesis
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processlipopolysaccharide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-deoxy-8-phosphooctulonate synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2692692-dehydro-3-deoxyphosphooctonate aldolase HAMAP MF_00056
PRO_1000091804

Experimental info

Sequence conflict331A → G in AAB17556. Ref.1
Sequence conflict1851F → S in AAB17556. Ref.1
Sequence conflict2251I → K in AAB17556. Ref.1

Sequences

Sequence LengthMass (Da)Tools
B0B8N1 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: EE0B823CA45815EB

FASTA26929,645
        10         20         30         40         50         60 
MFPENKMLLI AGPCVIEDNS VFETARRLKE IVAPYASSVH WIFKSSYDKA NRSSVHNYRG 

        70         80         90        100        110        120 
PGLRLGLQTL AKIKEELDVE ILTDVHSPDE AREAAKVCDI IQVPAFLCRQ TDLLVTAGET 

       130        140        150        160        170        180 
QAIVNIKKGQ FLSPWEMQGP IDKVLSTGNN KIILTERGCS FGYNNLVSDM RSIEVLRRFG 

       190        200        210        220        230        240 
FPVVFDGTHS VQLPGALHSQ SGGQTEFIPV LTRSAIAAGV QGLFIETHPN PSSALSDAAS 

       250        260 
MLSLKDLERL LPAWVQLFTY IQEMDAVSV

« Hide

References

« Hide 'large scale' references
[1]"Identification, characterization, and developmental regulation of Chlamydia trachomatis 3-deoxy-D-manno-octulosonate (KDO)-8-phosphate synthetase and CMP-KDO synthetase."
Wylie J.L., Iliffe E.R., Wang L.L., McClarty G.
Infect. Immun. 65:1527-1530(1997) [PubMed: 9119498] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Chlamydia trachomatis: genome sequence analysis of lymphogranuloma venereum isolates."
Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D., Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.
Genome Res. 18:161-171(2008) [PubMed: 18032721] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 434/Bu / ATCC VR-902B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U72493 Genomic DNA. Translation: AAB17556.1.
AM884176 Genomic DNA. Translation: CAP03468.1.
RefSeqYP_001654115.1. NC_010287.1.

3D structure databases

ProteinModelPortalB0B8N1.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0B8N1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5858018.
GenomeReviewsGene locus CTL0024 in contig AM884176_GR.
KEGGctb:CTL0024.
PATRIC20375466. VBIChlTra32542_0027.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG575990.
OMAESRDHAF.
ProtClustDBPRK05198.

Enzyme and pathway databases

BioCycCTRA471472:CTL0024-MONOMER.

Family and domain databases

HAMAPMF_00056. KDO8P_synth.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006269. KDO8P_synthase.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK01627.
PANTHERPTHR21057:SF2. KDO8P_synthase. 1 hit.
PfamPF00793. DAHP_synth_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01362. KDO8P_synth. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKDSA_CHLT2
AccessionPrimary (citable) accession number: B0B8N1
Secondary accession number(s): O84662, P77849
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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