Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase

Gene

wbpE

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the amination of UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronic acid (UDP-3-oxo-D-GlcNAcA) to UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid (UDP-GlcNAc3NA), using L-glutamate as the preferred amine donor.3 Publications

Catalytic activityi

UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate = UDP-2-acetamido-2-deoxy-D-ribo-hex-3-uluronate + L-glutamate.2 Publications

Cofactori

pyridoxal 5'-phosphate2 PublicationsNote: Binds 1 pyridoxal phosphate per subunit.2 Publications

pH dependencei

Optimum pH is 8.0 for the coupled WbpB/WbpE reaction.1 Publication

Temperature dependencei

Optimum temperature is 30 degrees Celsius for the coupled WbpB/WbpE reaction.1 Publication

Pathwayi: LPS O-antigen biosynthesis

This protein is involved in the pathway LPS O-antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.4 Publications
View all proteins of this organism that are known to be involved in the pathway LPS O-antigen biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei184 – 1841Nucleotide sugar substrate
Binding sitei229 – 2291Nucleotide sugar substrate

GO - Molecular functioni

  • pyridoxal phosphate binding Source: UniProtKB
  • transaminase activity Source: UniProtKB-KW

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • lipopolysaccharide biosynthetic process Source: UniProtKB
  • O antigen biosynthetic process Source: UniProtKB-UniPathway
  • polysaccharide biosynthetic process Source: PseudoCAP
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Cell wall biogenesis/degradation, Lipopolysaccharide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17574.
BRENDAi2.6.1.98. 5087.
UniPathwayiUPA00281.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase (EC:2.6.1.98)
Short name:
UDP-3-oxo-D-GlcNAcA aminotransferase
Alternative name(s):
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronic acid transaminase
UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase1 Publication
Gene namesi
Name:wbpEImported
Ordered Locus Names:PA3155
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3155.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601T → A: Minimal loss of activity. 1 Publication
Mutagenesisi156 – 1561D → A: Minimal loss of activity. 1 Publication
Mutagenesisi159 – 1591Q → A: Minimal loss of activity. 1 Publication
Mutagenesisi180 – 1801S → A: Minimal loss of activity. 1 Publication
Mutagenesisi185 – 1851K → A: Abolishes catalytic activity. 1 Publication
Mutagenesisi227 – 2271N → A: Minimal loss of activity. 1 Publication
Mutagenesisi229 – 2291R → A: Minimal loss of activity. 1 Publication
Mutagenesisi308 – 3081H → A: Minimal loss of activity. 1 Publication
Mutagenesisi309 – 3091Y → A: Minimal loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferasePRO_0000419620Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei185 – 1851N6-(pyridoxal phosphate)lysine1 Publication

Proteomic databases

PaxDbiQ9HZ76.

Interactioni

Subunit structurei

Homodimer.4 Publications

Protein-protein interaction databases

STRINGi208964.PA3155.

Structurei

Secondary structure

1
359
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2821Combined sources
Helixi35 – 4814Combined sources
Beta strandi51 – 577Combined sources
Helixi59 – 6911Combined sources
Beta strandi77 – 848Combined sources
Helixi87 – 948Combined sources
Beta strandi98 – 1025Combined sources
Turni106 – 1083Combined sources
Helixi113 – 1153Combined sources
Helixi117 – 1193Combined sources
Beta strandi124 – 1274Combined sources
Helixi132 – 1343Combined sources
Helixi139 – 14810Combined sources
Beta strandi153 – 1564Combined sources
Turni158 – 1625Combined sources
Beta strandi172 – 1809Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi194 – 1996Combined sources
Helixi201 – 21010Combined sources
Beta strandi215 – 2173Combined sources
Helixi232 – 24312Combined sources
Helixi245 – 26521Combined sources
Beta strandi282 – 2876Combined sources
Helixi291 – 30111Combined sources
Helixi313 – 3153Combined sources
Helixi317 – 3193Combined sources
Beta strandi322 – 3243Combined sources
Helixi327 – 3359Combined sources
Beta strandi336 – 3394Combined sources
Helixi347 – 35812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NU7X-ray1.95A/B1-359[»]
3NU8X-ray1.50A/B1-359[»]
3NUBX-ray1.90A/B1-359[»]
3NYSX-ray1.45A1-359[»]
3NYTX-ray1.30A1-359[»]
3NYUX-ray1.50A/B/C/D1-359[»]
ProteinModelPortaliQ9HZ76.
SMRiQ9HZ76. Positions 1-359.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HZ76.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni29 – 313Nucleotide sugar substrate binding
Regioni308 – 3092Nucleotide sugar substrate binding

Sequence similaritiesi

Belongs to the DegT/DnrJ/EryC1 family.Curated

Phylogenomic databases

eggNOGiENOG4105CF4. Bacteria.
COG0399. LUCA.
HOGENOMiHOG000230164.
InParanoidiQ9HZ76.
KOiK13017.
OMAiGVNTIIY.
OrthoDBiEOG6TXQZ2.
PhylomeDBiQ9HZ76.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000653. DegT/StrS_aminotransferase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF01041. DegT_DnrJ_EryC1. 1 hit.
[Graphical view]
PIRSFiPIRSF000390. PLP_StrS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HZ76-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIEFIDLKNQ QARIKDKIDA GIQRVLRHGQ YILGPEVTEL EDRLADFVGA
60 70 80 90 100
KYCISCANGT DALQIVQMAL GVGPGDEVIT PGFTYVATAE TVALLGAKPV
110 120 130 140 150
YVDIDPRTYN LDPQLLEAAI TPRTKAIIPV SLYGQCADFD AINAIASKYG
160 170 180 190 200
IPVIEDAAQS FGASYKGKRS CNLSTVACTS FFPSKPLGCY GDGGAIFTND
210 220 230 240 250
DELATAIRQI ARHGQDRRYH HIRVGVNSRL DTLQAAILLP KLEIFEEEIA
260 270 280 290 300
LRQKVAAEYD LSLKQVGIGT PFIEVNNISV YAQYTVRMDN RESVQASLKA
310 320 330 340 350
AGVPTAVHYP IPLNKQPAVA DEKAKLPVGD KAATQVMSLP MHPYLDTASI

KIICAALTN
Length:359
Mass (Da):38,925
Last modified:March 1, 2001 - v1
Checksum:iA7466AC204A45815
GO

Sequence cautioni

The sequence AAC45856.1 differs from that shown. Reason: Frameshift at position 274. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti276 – 2761N → D in AAC45856 (PubMed:8939432).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50396 Genomic DNA. Translation: AAC45856.1. Frameshift.
AE004091 Genomic DNA. Translation: AAG06543.1.
PIRiE83251.
RefSeqiNP_251845.1. NC_002516.2.
WP_003113425.1. NZ_ASJY01000511.1.

Genome annotation databases

EnsemblBacteriaiAAG06543; AAG06543; PA3155.
GeneIDi882653.
KEGGipae:PA3155.
PATRICi19840877. VBIPseAer58763_3299.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50396 Genomic DNA. Translation: AAC45856.1. Frameshift.
AE004091 Genomic DNA. Translation: AAG06543.1.
PIRiE83251.
RefSeqiNP_251845.1. NC_002516.2.
WP_003113425.1. NZ_ASJY01000511.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NU7X-ray1.95A/B1-359[»]
3NU8X-ray1.50A/B1-359[»]
3NUBX-ray1.90A/B1-359[»]
3NYSX-ray1.45A1-359[»]
3NYTX-ray1.30A1-359[»]
3NYUX-ray1.50A/B/C/D1-359[»]
ProteinModelPortaliQ9HZ76.
SMRiQ9HZ76. Positions 1-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA3155.

Proteomic databases

PaxDbiQ9HZ76.

Protocols and materials databases

DNASUi882653.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG06543; AAG06543; PA3155.
GeneIDi882653.
KEGGipae:PA3155.
PATRICi19840877. VBIPseAer58763_3299.

Organism-specific databases

PseudoCAPiPA3155.

Phylogenomic databases

eggNOGiENOG4105CF4. Bacteria.
COG0399. LUCA.
HOGENOMiHOG000230164.
InParanoidiQ9HZ76.
KOiK13017.
OMAiGVNTIIY.
OrthoDBiEOG6TXQZ2.
PhylomeDBiQ9HZ76.

Enzyme and pathway databases

UniPathwayiUPA00281.
BioCyciMetaCyc:MONOMER-17574.
BRENDAi2.6.1.98. 5087.

Miscellaneous databases

EvolutionaryTraceiQ9HZ76.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000653. DegT/StrS_aminotransferase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF01041. DegT_DnrJ_EryC1. 1 hit.
[Graphical view]
PIRSFiPIRSF000390. PLP_StrS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of the Pseudomonas aeruginosa serotype O5 (PAO1) B-band lipopolysaccharide gene cluster."
    Burrows L.L., Charter D.F., Lam J.S.
    Mol. Microbiol. 22:481-495(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  3. "Biosynthesis of a rare di-N-acetylated sugar in the lipopolysaccharides of both Pseudomonas aeruginosa and Bordetella pertussis occurs via an identical scheme despite different gene clusters."
    Westman E.L., Preston A., Field R.A., Lam J.S.
    J. Bacteriol. 190:6060-6069(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 122281 Publication.
  4. "Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1."
    Larkin A., Imperiali B.
    Biochemistry 48:5446-5455(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 122281 Publication.
  5. "Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa."
    Westman E.L., McNally D.J., Charchoglyan A., Brewer D., Field R.A., Lam J.S.
    J. Biol. Chem. 284:11854-11862(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 122281 Publication.
  6. "Structural analysis of WbpE from Pseudomonas aeruginosa PAO1: a nucleotide sugar aminotransferase involved in O-antigen assembly."
    Larkin A., Olivier N.B., Imperiali B.
    Biochemistry 49:7227-7237(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL PHOSPHATE; PYRIDOXAMINE PHOSPHATE AND THE EXTERNAL ALDIMINE OF PLP WITH NUCLEOTIDE SUGAR PRODUCT, COFACTOR, MUTAGENESIS OF THR-60; ASP-156; GLN-159; SER-180; LYS-185; ASN-227; ARG-229; HIS-308 AND TYR-309, SUBUNIT.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 122281 Publication.
  7. "X-ray crystal structure of the Wbpe (WlbE) aminotransferase from Pseudomonas aeruginosa as the PLP internal aldimine adduct with lysine 185."
    Holden H.M., Thoden J.B.
    Submitted (JUL-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE.
  8. "X-ray crystal structure of the WlbE (WpbE) aminotransferase from Pseudomonas aeruginosa, mutation K185A, in complex with the PLP external aldimine adduct with UDP-3-amino-2-N-acetyl-glucuronic acid, at 1.3 angstrom resolution."
    Holden H.M., Thoden J.B.
    Submitted (JUL-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF MUTANT ALA-185 IN COMPLEX WITH THE EXTERNAL ALDIMINE OF PLP WITH NUCLEOTIDE SUGAR PRODUCT.
  9. "X-ray structure of the K185A mutant of WbpE (WlbE) from Pseudomonas aeruginosa in complex with PLP at 1.45 angstrom resolution."
    Holden H.M., Thoden J.B.
    Submitted (JUL-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF MUTANT ALA-185 IN COMPLEX WITH PYRIDOXAL PHOSPHATE.

Entry informationi

Entry nameiWBPE_PSEAE
AccessioniPrimary (citable) accession number: Q9HZ76
Secondary accession number(s): P72136
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: March 1, 2001
Last modified: November 11, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.