WBPE_PSEAE
ID WBPE_PSEAE Reviewed; 359 AA.
AC Q9HZ76; P72136;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase;
DE Short=UDP-3-oxo-D-GlcNAcA aminotransferase;
DE EC=2.6.1.98;
DE AltName: Full=UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronic acid transaminase;
DE AltName: Full=UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase {ECO:0000303|PubMed:19282284};
GN Name=wbpE {ECO:0000312|EMBL:AAG06543.1}; OrderedLocusNames=PA3155;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC45856.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000312|EMBL:AAC45856.1};
RX PubMed=8939432; DOI=10.1046/j.1365-2958.1996.1351503.x;
RA Burrows L.L., Charter D.F., Lam J.S.;
RT "Molecular characterization of the Pseudomonas aeruginosa serotype O5
RT (PAO1) B-band lipopolysaccharide gene cluster.";
RL Mol. Microbiol. 22:481-495(1996).
RN [2] {ECO:0000312|EMBL:AAG06543.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3] {ECO:0000305}
RP FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000269|PubMed:18621892};
RX PubMed=18621892; DOI=10.1128/jb.00579-08;
RA Westman E.L., Preston A., Field R.A., Lam J.S.;
RT "Biosynthesis of a rare di-N-acetylated sugar in the lipopolysaccharides of
RT both Pseudomonas aeruginosa and Bordetella pertussis occurs via an
RT identical scheme despite different gene clusters.";
RL J. Bacteriol. 190:6060-6069(2008).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000269|PubMed:19348502};
RX PubMed=19348502; DOI=10.1021/bi900186u;
RA Larkin A., Imperiali B.;
RT "Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the
RT Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa
RT PAO1.";
RL Biochemistry 48:5446-5455(2009).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000269|PubMed:19282284};
RX PubMed=19282284; DOI=10.1074/jbc.m808583200;
RA Westman E.L., McNally D.J., Charchoglyan A., Brewer D., Field R.A.,
RA Lam J.S.;
RT "Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway
RT for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
RT in Pseudomonas aeruginosa.";
RL J. Biol. Chem. 284:11854-11862(2009).
RN [6] {ECO:0007744|PDB:3NU7, ECO:0007744|PDB:3NU8, ECO:0007744|PDB:3NUB}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL
RP PHOSPHATE; PYRIDOXAMINE PHOSPHATE AND THE EXTERNAL ALDIMINE OF PLP WITH
RP NUCLEOTIDE SUGAR PRODUCT, COFACTOR, MUTAGENESIS OF THR-60; ASP-156;
RP GLN-159; SER-180; LYS-185; ASN-227; ARG-229; HIS-308 AND TYR-309, AND
RP SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000269|PubMed:20604544};
RX PubMed=20604544; DOI=10.1021/bi100805b;
RA Larkin A., Olivier N.B., Imperiali B.;
RT "Structural analysis of WbpE from Pseudomonas aeruginosa PAO1: a nucleotide
RT sugar aminotransferase involved in O-antigen assembly.";
RL Biochemistry 49:7227-7237(2010).
RN [7] {ECO:0000312|PDB:3NYU}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE.
RA Holden H.M., Thoden J.B.;
RT "X-ray crystal structure of the Wbpe (WlbE) aminotransferase from
RT Pseudomonas aeruginosa as the PLP internal aldimine adduct with lysine
RT 185.";
RL Submitted (JUL-2010) to the PDB data bank.
RN [8] {ECO:0000312|PDB:3NYU}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF MUTANT ALA-185 IN COMPLEX WITH
RP THE EXTERNAL ALDIMINE OF PLP WITH NUCLEOTIDE SUGAR PRODUCT.
RA Holden H.M., Thoden J.B.;
RT "X-ray crystal structure of the WlbE (WpbE) aminotransferase from
RT Pseudomonas aeruginosa, mutation K185A, in complex with the PLP external
RT aldimine adduct with UDP-3-amino-2-N-acetyl-glucuronic acid, at 1.3
RT angstrom resolution.";
RL Submitted (JUL-2010) to the PDB data bank.
RN [9] {ECO:0000312|PDB:3NYU}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF MUTANT ALA-185 IN COMPLEX WITH
RP PYRIDOXAL PHOSPHATE.
RA Holden H.M., Thoden J.B.;
RT "X-ray structure of the K185A mutant of WbpE (WlbE) from Pseudomonas
RT aeruginosa in complex with PLP at 1.45 angstrom resolution.";
RL Submitted (JUL-2010) to the PDB data bank.
CC -!- FUNCTION: Plays a role in the biosynthesis of B-band O antigen for
CC serotype O5. Catalyzes the amination of UDP-2-acetamido-2-deoxy-3-oxo-
CC D-glucuronic acid (UDP-3-oxo-D-GlcNAcA) to UDP-2-acetamido-3-amino-2,3-
CC dideoxy-D-glucuronic acid (UDP-GlcNAc3NA), using L-glutamate as the
CC preferred amine donor. {ECO:0000269|PubMed:18621892,
CC ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate + UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-
CC uluronate = 2-oxoglutarate + UDP-2-acetamido-3-amino-2,3-dideoxy-
CC alpha-D-glucuronate; Xref=Rhea:RHEA:33583, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:62245, ChEBI:CHEBI:62250; EC=2.6.1.98;
CC Evidence={ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:20604544};
CC Note=Binds 1 pyridoxal phosphate per subunit.
CC {ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:20604544};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0 for the coupled WbpB/WbpE reaction.
CC {ECO:0000269|PubMed:19348502};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius for the coupled WbpB/WbpE
CC reaction. {ECO:0000269|PubMed:19348502};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:18621892,
CC ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502,
CC ECO:0000269|PubMed:8939432}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20604544, ECO:0000269|Ref.7,
CC ECO:0000269|Ref.8, ECO:0000269|Ref.9}.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC45856.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U50396; AAC45856.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE004091; AAG06543.1; -; Genomic_DNA.
DR PIR; E83251; E83251.
DR RefSeq; NP_251845.1; NC_002516.2.
DR RefSeq; WP_003113425.1; NZ_QZGE01000023.1.
DR PDB; 3NU7; X-ray; 1.95 A; A/B=1-359.
DR PDB; 3NU8; X-ray; 1.50 A; A/B=1-359.
DR PDB; 3NUB; X-ray; 1.90 A; A/B=1-359.
DR PDB; 3NYS; X-ray; 1.45 A; A=1-359.
DR PDB; 3NYT; X-ray; 1.30 A; A=1-359.
DR PDB; 3NYU; X-ray; 1.50 A; A/B/C/D=1-359.
DR PDBsum; 3NU7; -.
DR PDBsum; 3NU8; -.
DR PDBsum; 3NUB; -.
DR PDBsum; 3NYS; -.
DR PDBsum; 3NYT; -.
DR PDBsum; 3NYU; -.
DR AlphaFoldDB; Q9HZ76; -.
DR SMR; Q9HZ76; -.
DR STRING; 208964.PA3155; -.
DR PaxDb; Q9HZ76; -.
DR PRIDE; Q9HZ76; -.
DR DNASU; 882653; -.
DR EnsemblBacteria; AAG06543; AAG06543; PA3155.
DR GeneID; 882653; -.
DR KEGG; pae:PA3155; -.
DR PATRIC; fig|208964.12.peg.3299; -.
DR PseudoCAP; PA3155; -.
DR HOGENOM; CLU_033332_6_1_6; -.
DR InParanoid; Q9HZ76; -.
DR OMA; PGDAVFC; -.
DR PhylomeDB; Q9HZ76; -.
DR BioCyc; MetaCyc:MON-17574; -.
DR BioCyc; PAER208964:G1FZ6-3215-MON; -.
DR BRENDA; 2.6.1.98; 5087.
DR UniPathway; UPA00281; -.
DR EvolutionaryTrace; Q9HZ76; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009243; P:O antigen biosynthetic process; IDA:UniProtKB.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IDA:PseudoCAP.
DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; EXP:PseudoCAP.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244; PTHR30244; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Cell wall biogenesis/degradation;
KW Lipopolysaccharide biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..359
FT /note="UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate
FT aminotransferase"
FT /id="PRO_0000419620"
FT BINDING 29
FT /ligand="UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-
FT uluronate"
FT /ligand_id="ChEBI:CHEBI:62250"
FT /evidence="ECO:0007744|PDB:3NUB"
FT BINDING 31
FT /ligand="UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-
FT uluronate"
FT /ligand_id="ChEBI:CHEBI:62250"
FT /evidence="ECO:0007744|PDB:3NUB"
FT BINDING 184
FT /ligand="UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-
FT uluronate"
FT /ligand_id="ChEBI:CHEBI:62250"
FT /evidence="ECO:0007744|PDB:3NUB"
FT BINDING 229
FT /ligand="UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-
FT uluronate"
FT /ligand_id="ChEBI:CHEBI:62250"
FT /evidence="ECO:0007744|PDB:3NUB"
FT BINDING 308
FT /ligand="UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-
FT uluronate"
FT /ligand_id="ChEBI:CHEBI:62250"
FT /evidence="ECO:0007744|PDB:3NUB"
FT BINDING 309
FT /ligand="UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-
FT uluronate"
FT /ligand_id="ChEBI:CHEBI:62250"
FT /evidence="ECO:0007744|PDB:3NUB"
FT MOD_RES 185
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:20604544"
FT MUTAGEN 60
FT /note="T->A: Minimal loss of activity."
FT /evidence="ECO:0000269|PubMed:20604544"
FT MUTAGEN 156
FT /note="D->A: Minimal loss of activity."
FT /evidence="ECO:0000269|PubMed:20604544"
FT MUTAGEN 159
FT /note="Q->A: Minimal loss of activity."
FT /evidence="ECO:0000269|PubMed:20604544"
FT MUTAGEN 180
FT /note="S->A: Minimal loss of activity."
FT /evidence="ECO:0000269|PubMed:20604544"
FT MUTAGEN 185
FT /note="K->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:20604544"
FT MUTAGEN 227
FT /note="N->A: Minimal loss of activity."
FT /evidence="ECO:0000269|PubMed:20604544"
FT MUTAGEN 229
FT /note="R->A: Minimal loss of activity."
FT /evidence="ECO:0000269|PubMed:20604544"
FT MUTAGEN 308
FT /note="H->A: Minimal loss of activity."
FT /evidence="ECO:0000269|PubMed:20604544"
FT MUTAGEN 309
FT /note="Y->A: Minimal loss of activity."
FT /evidence="ECO:0000269|PubMed:20604544"
FT CONFLICT 276
FT /note="N -> D (in Ref. 1; AAC45856)"
FT /evidence="ECO:0000305"
FT HELIX 8..28
FT /evidence="ECO:0007829|PDB:3NYT"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:3NYT"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:3NYT"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:3NYT"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:3NYT"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:3NYT"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:3NYT"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:3NYT"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3NYT"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3NYT"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:3NYT"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:3NYT"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:3NYT"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:3NYT"
FT TURN 158..162
FT /evidence="ECO:0007829|PDB:3NYT"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:3NYT"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3NYT"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:3NYT"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:3NYT"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3NYT"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:3NYT"
FT HELIX 245..265
FT /evidence="ECO:0007829|PDB:3NYT"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:3NYT"
FT HELIX 291..301
FT /evidence="ECO:0007829|PDB:3NYT"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:3NYT"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3NYT"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:3NYS"
FT HELIX 327..335
FT /evidence="ECO:0007829|PDB:3NYT"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:3NYT"
FT HELIX 347..358
FT /evidence="ECO:0007829|PDB:3NYT"
SQ 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
