B0B9V8 · KDTA_CHLT2

Function

function

Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of three 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Thus generates the genus-specific LPS epitope of Chlamydia, composed of the trisaccharide alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo.

Catalytic activity

Pathway

Bacterial outer membrane biogenesis; LPS core biosynthesis.

Features

Showing features for active site, site, binding site.

TypeIDPosition(s)Description
Active site67Proton acceptor
Site138Transition state stabilizer
Site216Transition state stabilizer
Binding site275-276CMP (UniProtKB | ChEBI)
Binding site315-317CMP (UniProtKB | ChEBI)
Binding site342-345CMP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular FunctionKdo transferase activity
Biological Processlipopolysaccharide core region biosynthetic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    3-deoxy-D-manno-octulosonic acid transferase
  • EC number
  • Short names
    Kdo transferase
  • Alternative names
    • Kdo(2)-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase
    • Kdo-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase
    • Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase
    • Trifunctional Kdo transferase

Gene names

    • Name
      waaA
    • Synonyms
      gseA, kdtA
    • Ordered locus names
      CTL0460

Organism names

Accessions

  • Primary accession
    B0B9V8
  • Secondary accessions
    • P0C0Z9
    • Q46394
    • Q46395
    • Q46396
    • Q46401
    • Q57440

Proteomes

Subcellular Location

Cell inner membrane
; Single-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane5-27Helical; Signal-anchor

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003917961-4313-deoxy-D-manno-octulosonic acid transferase

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    431
  • Mass (Da)
    49,497
  • Last updated
    2008-02-26 v1
  • Checksum
    664A7504F4E749AC
MIRRWLTSRLYDAFLVCAFFVSAPRIFYKVFFHGKYIDSWKIRFGVQKPFVKGEGPLVWFHGASVGEVSLLAPLLNRWREEFPEWRFVVTTCSEAGVHTARRLYESLGATVFVLPLDLSCIIKSVVRKLAPDIVIFSEGDCWLHFLTESKRLGAKAFLINGKLSEHSCKRFSFLKRLGRNYFAPLDLLILQDELYKQRFMQIGISSDKIHVTGNMKTFIESSLATNRRDFWRAKLQISSQDRLIVLGSMHPKDVEVWAEVVSHFHNSSTKILWVPRHLEKLKEHAKLLEKAGILFGLWSQGASFRQYNSLIMDAMGVLKDIYSAADIAFVGGTFDPSVGGHNLLEPLQKEAPLMFGPYIYSQSVLAERLREKEAGLSVNKETLLDVVTDLLQNEKNRQAYIEKGKSFLKQEENSFQQTWEILKSQITCMKI

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict301in Ref. 1; AAA23139 and 2; CAA80374
Sequence conflict397-431in Ref. 1; AAA23139

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M64618
EMBL· GenBank· DDBJ
AAA23139.1
EMBL· GenBank· DDBJ
Genomic DNA
Z22659
EMBL· GenBank· DDBJ
CAA80374.1
EMBL· GenBank· DDBJ
Genomic DNA
AM884176
EMBL· GenBank· DDBJ
CAP03899.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp