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UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase (UDP-3-oxo-D-GlcNAcA aminotransferase) (EC 2.6.1.98) (UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronic acid transaminase) (UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase)

 WBPE_PSEAE              Reviewed;         359 AA.
Q9HZ76; P72136;
03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
23-MAY-2018, entry version 89.
RecName: Full=UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase;
Short=UDP-3-oxo-D-GlcNAcA aminotransferase;
EC=2.6.1.98;
AltName: Full=UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronic acid transaminase;
AltName: Full=UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase {ECO:0000303|PubMed:19282284};
Name=wbpE {ECO:0000312|EMBL:AAG06543.1}; OrderedLocusNames=PA3155;
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /
JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=208964;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC45856.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1 {ECO:0000312|EMBL:AAC45856.1};
PubMed=8939432; DOI=10.1046/j.1365-2958.1996.1351503.x;
Burrows L.L., Charter D.F., Lam J.S.;
"Molecular characterization of the Pseudomonas aeruginosa serotype O5
(PAO1) B-band lipopolysaccharide gene cluster.";
Mol. Microbiol. 22:481-495(1996).
[2] {ECO:0000312|EMBL:AAG06543.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1;
PubMed=10984043; DOI=10.1038/35023079;
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an
opportunistic pathogen.";
Nature 406:959-964(2000).
[3] {ECO:0000305}
FUNCTION, AND PATHWAY.
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1 {ECO:0000269|PubMed:18621892};
PubMed=18621892; DOI=10.1128/JB.00579-08;
Westman E.L., Preston A., Field R.A., Lam J.S.;
"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.";
J. Bacteriol. 190:6060-6069(2008).
[4] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1 {ECO:0000269|PubMed:19348502};
PubMed=19348502; DOI=10.1021/bi900186u;
Larkin A., Imperiali B.;
"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.";
Biochemistry 48:5446-5455(2009).
[5] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1 {ECO:0000269|PubMed:19282284};
PubMed=19282284; DOI=10.1074/jbc.M808583200;
Westman E.L., McNally D.J., Charchoglyan A., Brewer D., Field R.A.,
Lam J.S.;
"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.";
J. Biol. Chem. 284:11854-11862(2009).
[6] {ECO:0000305, ECO:0000312|PDB:3NU7}
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, AND SUBUNIT.
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1 {ECO:0000269|PubMed:20604544};
PubMed=20604544; DOI=10.1021/bi100805b;
Larkin A., Olivier N.B., Imperiali B.;
"Structural analysis of WbpE from Pseudomonas aeruginosa PAO1: a
nucleotide sugar aminotransferase involved in O-antigen assembly.";
Biochemistry 49:7227-7237(2010).
[7] {ECO:0000312|PDB:3NYU}
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL
PHOSPHATE.
Holden H.M., Thoden J.B.;
"X-ray crystal structure of the Wbpe (WlbE) aminotransferase from
Pseudomonas aeruginosa as the PLP internal aldimine adduct with lysine
185.";
Submitted (JUL-2010) to the PDB data bank.
[8] {ECO:0000312|PDB:3NYU}
X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF MUTANT ALA-185 IN COMPLEX
WITH THE EXTERNAL ALDIMINE OF PLP WITH NUCLEOTIDE SUGAR PRODUCT.
Holden H.M., Thoden J.B.;
"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.";
Submitted (JUL-2010) to the PDB data bank.
[9] {ECO:0000312|PDB:3NYU}
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF MUTANT ALA-185 IN COMPLEX
WITH PYRIDOXAL PHOSPHATE.
Holden H.M., Thoden J.B.;
"X-ray structure of the K185A mutant of WbpE (WlbE) from Pseudomonas
aeruginosa in complex with PLP at 1.45 angstrom resolution.";
Submitted (JUL-2010) to the PDB data bank.
-!- FUNCTION: 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.
{ECO:0000269|PubMed:18621892, ECO:0000269|PubMed:19282284,
ECO:0000269|PubMed:19348502}.
-!- CATALYTIC ACTIVITY: 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. {ECO:0000269|PubMed:19282284,
ECO:0000269|PubMed:19348502}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:19348502,
ECO:0000269|PubMed:20604544};
Note=Binds 1 pyridoxal phosphate per subunit.
{ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:20604544};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8.0 for the coupled WbpB/WbpE reaction.
{ECO:0000269|PubMed:19348502};
Temperature dependence:
Optimum temperature is 30 degrees Celsius for the coupled
WbpB/WbpE reaction. {ECO:0000269|PubMed:19348502};
-!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
biosynthesis. {ECO:0000269|PubMed:18621892,
ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502,
ECO:0000269|PubMed:8939432}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20604544,
ECO:0000269|Ref.7, ECO:0000269|Ref.8, ECO:0000269|Ref.9}.
-!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC45856.1; Type=Frameshift; Positions=274; Evidence={ECO:0000305};
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EMBL; U50396; AAC45856.1; ALT_FRAME; Genomic_DNA.
EMBL; AE004091; AAG06543.1; -; Genomic_DNA.
PIR; E83251; E83251.
RefSeq; NP_251845.1; NC_002516.2.
RefSeq; WP_003113425.1; NC_002516.2.
PDB; 3NU7; X-ray; 1.95 A; A/B=1-359.
PDB; 3NU8; X-ray; 1.50 A; A/B=1-359.
PDB; 3NUB; X-ray; 1.90 A; A/B=1-359.
PDB; 3NYS; X-ray; 1.45 A; A=1-359.
PDB; 3NYT; X-ray; 1.30 A; A=1-359.
PDB; 3NYU; X-ray; 1.50 A; A/B/C/D=1-359.
PDBsum; 3NU7; -.
PDBsum; 3NU8; -.
PDBsum; 3NUB; -.
PDBsum; 3NYS; -.
PDBsum; 3NYT; -.
PDBsum; 3NYU; -.
ProteinModelPortal; Q9HZ76; -.
SMR; Q9HZ76; -.
STRING; 208964.PA3155; -.
PaxDb; Q9HZ76; -.
PRIDE; Q9HZ76; -.
DNASU; 882653; -.
EnsemblBacteria; AAG06543; AAG06543; PA3155.
GeneID; 882653; -.
KEGG; pae:PA3155; -.
PATRIC; fig|208964.12.peg.3299; -.
PseudoCAP; PA3155; -.
eggNOG; ENOG4105CF4; Bacteria.
eggNOG; COG0399; LUCA.
HOGENOM; HOG000230164; -.
InParanoid; Q9HZ76; -.
KO; K13017; -.
OMA; PGFTYIA; -.
PhylomeDB; Q9HZ76; -.
BioCyc; MetaCyc:MONOMER-17574; -.
BioCyc; PAER208964:G1FZ6-3215-MONOMER; -.
BRENDA; 2.6.1.98; 5087.
UniPathway; UPA00281; -.
EvolutionaryTrace; Q9HZ76; -.
Proteomes; UP000002438; Chromosome.
GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
GO; GO:0008483; F:transaminase activity; EXP:PseudoCAP.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IDA:UniProtKB.
GO; GO:0009243; P:O antigen biosynthetic process; EXP:PseudoCAP.
GO; GO:0000271; P:polysaccharide biosynthetic process; IDA:PseudoCAP.
GO; GO:0006065; P:UDP-glucuronate biosynthetic process; EXP:PseudoCAP.
CDD; cd00616; AHBA_syn; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR000653; DegT/StrS_aminotransferase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
PANTHER; PTHR30244; PTHR30244; 1.
Pfam; PF01041; DegT_DnrJ_EryC1; 1.
PIRSF; PIRSF000390; PLP_StrS; 1.
SUPFAM; SSF53383; SSF53383; 1.
1: Evidence at protein level;
3D-structure; Aminotransferase; Cell wall biogenesis/degradation;
Complete proteome; Lipopolysaccharide biosynthesis;
Pyridoxal phosphate; Reference proteome; Transferase.
CHAIN 1 359 UDP-2-acetamido-2-deoxy-3-oxo-D-
glucuronate aminotransferase.
/FTId=PRO_0000419620.
REGION 29 31 Nucleotide sugar substrate binding.
REGION 308 309 Nucleotide sugar substrate binding.
BINDING 184 184 Nucleotide sugar substrate.
BINDING 229 229 Nucleotide sugar substrate.
MOD_RES 185 185 N6-(pyridoxal phosphate)lysine.
{ECO:0000269|PubMed:20604544}.
MUTAGEN 60 60 T->A: Minimal loss of activity.
{ECO:0000269|PubMed:20604544}.
MUTAGEN 156 156 D->A: Minimal loss of activity.
{ECO:0000269|PubMed:20604544}.
MUTAGEN 159 159 Q->A: Minimal loss of activity.
{ECO:0000269|PubMed:20604544}.
MUTAGEN 180 180 S->A: Minimal loss of activity.
{ECO:0000269|PubMed:20604544}.
MUTAGEN 185 185 K->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:20604544}.
MUTAGEN 227 227 N->A: Minimal loss of activity.
{ECO:0000269|PubMed:20604544}.
MUTAGEN 229 229 R->A: Minimal loss of activity.
{ECO:0000269|PubMed:20604544}.
MUTAGEN 308 308 H->A: Minimal loss of activity.
{ECO:0000269|PubMed:20604544}.
MUTAGEN 309 309 Y->A: Minimal loss of activity.
{ECO:0000269|PubMed:20604544}.
CONFLICT 276 276 N -> D (in Ref. 1; AAC45856).
{ECO:0000305}.
HELIX 8 28 {ECO:0000244|PDB:3NYT}.
HELIX 35 48 {ECO:0000244|PDB:3NYT}.
STRAND 51 57 {ECO:0000244|PDB:3NYT}.
HELIX 59 69 {ECO:0000244|PDB:3NYT}.
STRAND 77 84 {ECO:0000244|PDB:3NYT}.
HELIX 87 94 {ECO:0000244|PDB:3NYT}.
STRAND 98 102 {ECO:0000244|PDB:3NYT}.
TURN 106 108 {ECO:0000244|PDB:3NYT}.
HELIX 113 115 {ECO:0000244|PDB:3NYT}.
HELIX 117 119 {ECO:0000244|PDB:3NYT}.
STRAND 124 127 {ECO:0000244|PDB:3NYT}.
HELIX 132 134 {ECO:0000244|PDB:3NYT}.
HELIX 139 148 {ECO:0000244|PDB:3NYT}.
STRAND 153 156 {ECO:0000244|PDB:3NYT}.
TURN 158 162 {ECO:0000244|PDB:3NYT}.
STRAND 172 180 {ECO:0000244|PDB:3NYT}.
STRAND 185 187 {ECO:0000244|PDB:3NYT}.
STRAND 194 199 {ECO:0000244|PDB:3NYT}.
HELIX 201 210 {ECO:0000244|PDB:3NYT}.
STRAND 215 217 {ECO:0000244|PDB:3NYT}.
HELIX 232 243 {ECO:0000244|PDB:3NYT}.
HELIX 245 265 {ECO:0000244|PDB:3NYT}.
STRAND 282 287 {ECO:0000244|PDB:3NYT}.
HELIX 291 301 {ECO:0000244|PDB:3NYT}.
HELIX 313 315 {ECO:0000244|PDB:3NYT}.
HELIX 317 319 {ECO:0000244|PDB:3NYT}.
STRAND 322 324 {ECO:0000244|PDB:3NYS}.
HELIX 327 335 {ECO:0000244|PDB:3NYT}.
STRAND 336 339 {ECO:0000244|PDB:3NYT}.
HELIX 347 358 {ECO:0000244|PDB:3NYT}.
SEQUENCE 359 AA; 38925 MW; A7466AC204A45815 CRC64;
MIEFIDLKNQ QARIKDKIDA GIQRVLRHGQ YILGPEVTEL EDRLADFVGA KYCISCANGT
DALQIVQMAL GVGPGDEVIT PGFTYVATAE TVALLGAKPV YVDIDPRTYN LDPQLLEAAI
TPRTKAIIPV SLYGQCADFD AINAIASKYG IPVIEDAAQS FGASYKGKRS CNLSTVACTS
FFPSKPLGCY GDGGAIFTND DELATAIRQI ARHGQDRRYH HIRVGVNSRL DTLQAAILLP
KLEIFEEEIA LRQKVAAEYD LSLKQVGIGT PFIEVNNISV YAQYTVRMDN RESVQASLKA
AGVPTAVHYP IPLNKQPAVA DEKAKLPVGD KAATQVMSLP MHPYLDTASI KIICAALTN


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