waaA

Functionⁱ

Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of two 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.2 Publications

Catalytic activityⁱ

Lipid IV(A) + CMP-beta-Kdo = alpha-Kdo-(2->6)-lipid IV(A) + CMP.2 Publications

Alpha-Kdo-(2->6)-lipid IV(A) + CMP-beta-Kdo = alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IV(A) + CMP.2 Publications

Activity regulationⁱ

Catalytic activity is inhibited by the antibiotic polymixin B and by Re endotoxin.1 Publication

Kineticsⁱ

V_max=
18 µmol/min/mg enzyme (at pH 8)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.6
  "Biosynthesis of endotoxins. Purification and catalytic properties of 3-deoxy-D-manno-octulosonic acid transferase from Escherichia coli."
  Belunis C.J., Raetz C.R.
  J. Biol. Chem. 267:9988-9997(1992) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIFUNCTIONALITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PATHWAY.

pH dependenceⁱ

Optimum pH is 7.1 Publication

Pathwayⁱ: KDO(2)-lipid A biosynthesis

This protein is involved in step 1 and 2 of the subpathway that synthesizes KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A).1 Publication
Proteins known to be involved in the 4 steps of the subpathway in this organism are:

3-deoxy-D-manno-octulosonic acid transferase (waaA)
3-deoxy-D-manno-octulosonic acid transferase (waaA)
Lipid A biosynthesis lauroyltransferase (lpxL)
Lipid A biosynthesis myristoyltransferase (lpxM)

This subpathway is part of the pathway KDO(2)-lipid A biosynthesis, which is itself part of Glycolipid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A), the pathway KDO(2)-lipid A biosynthesis and in Glycolipid biosynthesis.

Pathwayⁱ: LPS core biosynthesis

This protein is involved in the pathway LPS core biosynthesis, which is part of Bacterial outer membrane biogenesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway LPS core biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	60	Proton acceptorBy similarity	1
Siteⁱ	130	Transition state stabilizerBy similarity	1
Siteⁱ	208	Transition state stabilizerBy similarity	1

GO - Molecular functionⁱ

transferase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 1577828
- 2651435

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

Kdo2-lipid A biosynthetic process Source: UniProtKB-UniPathway
lipid A biosynthetic process
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 7499229
lipopolysaccharide core region biosynthetic process Source: UniProtKB-UniPathway

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Transferase
Biological process	Lipopolysaccharide biosynthesis

Enzyme and pathway databases

BioCycⁱ	EcoCyc:KDOTRANS-MONOMER MetaCyc:KDOTRANS-MONOMER
BRENDAⁱ	2.4.99.12 2026 2.4.99.13 2026
SABIO-RKⁱ	P0AC75
UniPathwayⁱ	UPA00360;UER00483 UPA00360;UER00484 UPA00958

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: 3-deoxy-D-manno-octulosonic acid transferase (EC:2.4.99.122 Publications, EC:2.4.99.132 Publications) Short name: Kdo transferase Alternative name(s): Bifunctional Kdo transferase Kdo-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase
Gene namesⁱ	Name:waaA Synonyms:kdtA Ordered Locus Names:b3633, JW3608
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10520 waaA

EcoGeneⁱ

EG10520 waaA

Subcellular locationⁱ

Cell inner membrane
1 Publication
Manual assertion inferred by curator fromⁱ
- Ref.6
  "Biosynthesis of endotoxins. Purification and catalytic properties of 3-deoxy-D-manno-octulosonic acid transferase from Escherichia coli."
  Belunis C.J., Raetz C.R.
  J. Biol. Chem. 267:9988-9997(1992) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIFUNCTIONALITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PATHWAY.
; Single-pass membrane protein
1 Publication
Manual assertion inferred by curator fromⁱ
- Ref.6
  "Biosynthesis of endotoxins. Purification and catalytic properties of 3-deoxy-D-manno-octulosonic acid transferase from Escherichia coli."
  Belunis C.J., Raetz C.R.
  J. Biol. Chem. 267:9988-9997(1992) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIFUNCTIONALITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PATHWAY.
; Cytoplasmic side
1 Publication
Manual assertion inferred by curator fromⁱ
- Ref.6
  "Biosynthesis of endotoxins. Purification and catalytic properties of 3-deoxy-D-manno-octulosonic acid transferase from Escherichia coli."
  Belunis C.J., Raetz C.R.
  J. Biol. Chem. 267:9988-9997(1992) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIFUNCTIONALITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PATHWAY.

Topology

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transmembraneⁱ	3 – 23	Helical; Signal-anchorSequence analysisAdd BLAST		21

GO - Cellular componentⁱ

integral component of membrane Source: UniProtKB-KW
membrane
Source: EcoliWiki
Inferred from direct assayⁱ
- 2651435
plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 1577828

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Cells lacking this gene display growth defects, absence of Kdo transferase activity, and accumulate massive amounts of lipid IV(A).1 Publication

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000080286	1 – 425	3-deoxy-D-manno-octulosonic acid transferaseAdd BLAST		425

Post-translational modificationⁱ

Degraded by the protease FtsH; therefore FtsH regulates the addition of the sugar moiety to the LPS and thus the maturation of the LPS precursor.1 Publication

Proteomic databases

PaxDbⁱ	P0AC75
PRIDEⁱ	P0AC75

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	4263240, 354 interactors
Database of interacting proteins More...DIPⁱ	DIP-48036N
IntActⁱ	P0AC75, 16 interactors
STRINGⁱ	316385.ECDH10B_3815

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P0AC75
SMRⁱ	P0AC75
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	268 – 269	CMP-Kdo bindingBy similarity	2
Regionⁱ	309 – 311	CMP-Kdo bindingBy similarity	3
Regionⁱ	335 – 338	CMP-Kdo bindingBy similarity	4

Domainⁱ

The N-terminal half of KdtA is responsible for determining the number of Kdo residues that are transferred to lipid IVA.1 Publication

Sequence similaritiesⁱ

Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 30 subfamily.Curated

Keywords - Domainⁱ

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG4105D8A Bacteria COG1519 LUCA
HOGENOMⁱ	HOG000257156
InParanoidⁱ	P0AC75
KEGG Orthology (KO) More...KOⁱ	K02527
PhylomeDBⁱ	P0AC75

Family and domain databases

Gene3Dⁱ	3.40.50.11720, 1 hit
InterProⁱ	View protein in InterPro IPR001296 Glyco_trans_1 IPR007507 Glycos_transf_N IPR038107 Glycos_transf_N_sf IPR039901 Kdotransferase
PANTHERⁱ	PTHR42755 PTHR42755, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00534 Glycos_transf_1, 1 hit PF04413 Glycos_transf_N, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0AC75-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MLELLYTALL YLIQPLIWIR LWVRGRKAPA YRKRWGERYG FYRHPLKPGG 
        60         70         80         90        100
IMLHSVSVGE TLAAIPLVRA LRHRYPDLPI TVTTMTPTGS ERVQSAFGKD 
       110        120        130        140        150
VQHVYLPYDL PDALNRFLNK VDPKLVLIME TELWPNLIAA LHKRKIPLVI 
       160        170        180        190        200
ANARLSARSA AGYAKLGKFV RRLLRRITLI AAQNEEDGAR FVALGAKNNQ 
       210        220        230        240        250
VTVTGSLKFD ISVTPQLAAK AVTLRRQWAP HRPVWIATST HEGEESVVIA 
       260        270        280        290        300
AHQALLQQFP NLLLILVPRH PERFPDAINL VRQAGLSYIT RSSGEVPSTS 
       310        320        330        340        350
TQVVVGDTMG ELMLLYGIAD LAFVGGSLVE RGGHNPLEAA AHAIPVLMGP 
       360        370        380        390        400
HTFNFKDICA RLEQASGLIT VTDATTLAKE VSSLLTDADY RSFYGRHAVE 
       410        420 
VLYQNQGALQ RLLQLLEPYL PPKTH

Length:425

Mass (Da):47,291

Last modified:November 8, 2005 - v1

Checksum:ⁱB063850A1FF392AF

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M60670 Genomic DNA Translation: AAA24043.1 M86305 Genomic DNA Translation: AAA03745.1 U00039 Genomic DNA Translation: AAB18610.1 U00096 Genomic DNA Translation: AAC76657.1 AP009048 Genomic DNA Translation: BAE77659.1
PIRⁱ	JU0467
NCBI Reference Sequences More...RefSeqⁱ	NP_418090.1, NC_000913.3 WP_000891564.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76657; AAC76657; b3633 BAE77659; BAE77659; BAE77659
GeneIDⁱ	949048
KEGGⁱ	ecj:JW3608 eco:b3633
PATRICⁱ	fig\|1411691.4.peg.3073

Protein	Similar proteins		Species	Score	Length	Source
P0AC75	3-deoxy-D-manno-octulosonic acid transferase		ECO57		425	UniRef100_P0AC77
3-deoxy-D-manno-octulosonic acid transferase		ECOL6		425
3-deoxy-D-manno-octulosonic acid transferase		Shigella sp.		425
3-deoxy-D-manno-octulosonic-acid transferase		KLEPN		425
3-deoxy-D-manno-octulosonic-acid transferase		Escherichia coli D6-113.11		425
+86

Protein	Similar proteins		Species	Score	Length	Source
P0AC75	3-deoxy-D-manno-octulosonic acid transferase		ECO57		425	UniRef90_P0AC77
3-deoxy-D-manno-octulosonic acid transferase		ECOL6		425
3-deoxy-D-manno-octulosonic acid transferase		Shigella sp.		425
3-deoxy-D-manno-octulosonic-acid transferase		KLEPN		425
3-deoxy-D-manno-octulosonic-acid transferase		Escherichia coli D6-113.11		425
+766

Protein	Similar proteins		Species	Score	Length	Source
P0AC75	3-deoxy-D-manno-octulosonic acid transferase		ECO57		425	UniRef50_P0AC77
3-deoxy-D-manno-octulosonic acid transferase		ECOL6		425
3-deoxy-D-manno-octulosonic acid transferase		HAEIN		427
3-deoxy-D-manno-octulosonic acid transferase		Shigella sp.		425
3-deoxy-D-manno-octulosonic-acid transferase		KLEPN		425
+1486

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M60670 Genomic DNA Translation: AAA24043.1 M86305 Genomic DNA Translation: AAA03745.1 U00039 Genomic DNA Translation: AAB18610.1 U00096 Genomic DNA Translation: AAC76657.1 AP009048 Genomic DNA Translation: BAE77659.1
PIRⁱ	JU0467
RefSeqⁱ	NP_418090.1, NC_000913.3 WP_000891564.1, NZ_LN832404.1

3D structure databases

ProteinModelPortalⁱ	P0AC75
SMRⁱ	P0AC75
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4263240, 354 interactors
DIPⁱ	DIP-48036N
IntActⁱ	P0AC75, 16 interactors
STRINGⁱ	316385.ECDH10B_3815

Proteomic databases

PaxDbⁱ	P0AC75
PRIDEⁱ	P0AC75

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76657; AAC76657; b3633 BAE77659; BAE77659; BAE77659
GeneIDⁱ	949048
KEGGⁱ	ecj:JW3608 eco:b3633
PATRICⁱ	fig\|1411691.4.peg.3073

Organism-specific databases

EchoBASEⁱ	EB0515
EcoGeneⁱ	EG10520 waaA

Phylogenomic databases

eggNOGⁱ	ENOG4105D8A Bacteria COG1519 LUCA
HOGENOMⁱ	HOG000257156
InParanoidⁱ	P0AC75
KOⁱ	K02527
PhylomeDBⁱ	P0AC75

Enzyme and pathway databases

UniPathwayⁱ	UPA00360;UER00483 UPA00360;UER00484 UPA00958
BioCycⁱ	EcoCyc:KDOTRANS-MONOMER MetaCyc:KDOTRANS-MONOMER
BRENDAⁱ	2.4.99.12 2026 2.4.99.13 2026
SABIO-RKⁱ	P0AC75

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P0AC75

PROⁱ

PR:P0AC75

Family and domain databases

Gene3Dⁱ	3.40.50.11720, 1 hit
InterProⁱ	View protein in InterPro IPR001296 Glyco_trans_1 IPR007507 Glycos_transf_N IPR038107 Glycos_transf_N_sf IPR039901 Kdotransferase
PANTHERⁱ	PTHR42755 PTHR42755, 1 hit
Pfamⁱ	View protein in Pfam PF00534 Glycos_transf_1, 1 hit PF04413 Glycos_transf_N, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	KDTA_ECOLI
Accessionⁱ	P0AC75Primary (citable) accession number: P0AC75 Secondary accession number(s): P23282, Q2M7U7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
	Last sequence update:	November 8, 2005
	Last modified:	November 7, 2018
	This is version 100 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0AC75 (KDTA_ECOLI)

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3-deoxy-D-manno-octulosonic acid transferase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

pH dependencei

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: KDO(2)-lipid A biosynthesis

Pathwayi: LPS core biosynthesis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Kineticsⁱ

pH dependenceⁱ

Pathwayⁱ: KDO(2)-lipid A biosynthesis

Pathwayⁱ: LPS core biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ