WBPB_PSEAE
ID WBPB_PSEAE Reviewed; 316 AA.
AC G3XD23; P72133; Q8KIQ7;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate oxidase;
DE EC=1.1.1.335;
DE AltName: Full=UDP-2-acetamido-2-deoxy-alpha-D-glucuronic acid 3-dehydrogenase;
DE AltName: Full=UDP-N-acetyl-D-glucosaminuronic acid 3-oxidase;
DE Short=UDP-D-GlcNAcA 3-oxidase {ECO:0000303|PubMed:18621892};
GN Name=wbpB {ECO:0000312|EMBL:AAG06546.1}; Synonyms=wlbA;
GN OrderedLocusNames=PA3158;
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:AAC45853.1}
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:AAC45853.1};
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:AAM27797.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000269|PubMed:12057956};
RX PubMed=12057956; DOI=10.1128/jb.184.13.3614-3622.2002;
RA Raymond C.K., Sims E.H., Kas A., Spencer D.H., Kutyavin T.V., Ivey R.G.,
RA Zhou Y., Kaul R., Clendenning J.B., Olson M.V.;
RT "Genetic variation at the O-antigen biosynthetic locus in Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 184:3614-3622(2002).
RN [3] {ECO:0000312|EMBL:AAG06546.1}
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 [4] {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 [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP 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 [6] {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 [7] {ECO:0000305, ECO:0000312|PDB:3OA2}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION,
RP CATALYTIC ACTIVITY, KINETIC PARAMETERS, REACTION MECHANISM, AND SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000269|PubMed:20690587};
RX PubMed=20690587; DOI=10.1021/bi101103s;
RA Thoden J.B., Holden H.M.;
RT "Structural and functional studies of WlbA: a dehydrogenase involved in the
RT biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid.";
RL Biochemistry 49:7939-7948(2010).
CC -!- FUNCTION: Plays a role in the biosynthesis of B-band O antigen for
CC serotype O5. Catalyzes the NAD-dependent oxidation of UDP-N-
CC acetylglucosaminuronic acid (UDP-D-GlcNAcA) to UDP-2-acetamido-2-deoxy-
CC 3-oxo-D-glucuronic acid (UDP-3-oxo-D-GlcNAcA). Cannot use UDP-GlcNAc or
CC UDP-GalNAc as the nucleotide sugar substrate, and can use only poorly
CC UDP-D-glucuronic acid (UDP-GlcA). Undergoes an NAD(+) recycling
CC mechanism using 2-oxoglutarate as an oxidant.
CC {ECO:0000269|PubMed:18621892, ECO:0000269|PubMed:19282284,
CC ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:20690587}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + UDP-N-2-acetamido-2-deoxy-alpha-D-glucuronate = H(+)
CC + NADH + UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate;
CC Xref=Rhea:RHEA:33579, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:62250, ChEBI:CHEBI:65040;
CC EC=1.1.1.335; Evidence={ECO:0000269|PubMed:19282284,
CC ECO:0000269|PubMed:19348502};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) + NADH;
CC Xref=Rhea:RHEA:13449, ChEBI:CHEBI:11596, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for UDP-GlcNAcA {ECO:0000269|PubMed:19348502,
CC ECO:0000269|PubMed:20690587};
CC KM=1.35 mM for 2-oxoglutarate {ECO:0000269|PubMed:19348502,
CC ECO:0000269|PubMed:20690587};
CC Vmax=28 umol/min/ug enzyme {ECO:0000269|PubMed:19348502,
CC ECO:0000269|PubMed:20690587};
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: Homotetramer. {ECO:0000269|PubMed:20690587}.
CC -!- MISCELLANEOUS: Seems to proceed via a ping-pong reaction mechanism.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000255}.
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DR EMBL; U50396; AAC45853.1; -; Genomic_DNA.
DR EMBL; AF498416; AAM27797.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06546.1; -; Genomic_DNA.
DR PIR; H83251; H83251.
DR RefSeq; NP_251848.1; NC_002516.2.
DR RefSeq; WP_003113428.1; NZ_QZGE01000023.1.
DR PDB; 3OA2; X-ray; 1.50 A; A/B/C/D=1-316.
DR PDBsum; 3OA2; -.
DR AlphaFoldDB; G3XD23; -.
DR SMR; G3XD23; -.
DR STRING; 208964.PA3158; -.
DR PaxDb; G3XD23; -.
DR DNASU; 882642; -.
DR EnsemblBacteria; AAG06546; AAG06546; PA3158.
DR GeneID; 882642; -.
DR KEGG; pae:PA3158; -.
DR PATRIC; fig|208964.12.peg.3302; -.
DR PseudoCAP; PA3158; -.
DR HOGENOM; CLU_862341_0_0_6; -.
DR OMA; YIAPRHM; -.
DR PhylomeDB; G3XD23; -.
DR BioCyc; MetaCyc:MON-17573; -.
DR BioCyc; PAER208964:G1FZ6-3218-MON; -.
DR BRENDA; 1.1.1.335; 5087.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0070404; F:NADH binding; IDA:UniProtKB.
DR GO; GO:0003954; F:NADH dehydrogenase activity; EXP:PseudoCAP.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase 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:0051262; P:protein tetramerization; IDA:UniProtKB.
DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; EXP:PseudoCAP.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation;
KW Lipopolysaccharide biosynthesis; NAD; Nucleotide-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..316
FT /note="UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate oxidase"
FT /id="PRO_0000419621"
FT BINDING 11..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20690587"
FT BINDING 32..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20690587"
FT BINDING 55
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20690587"
FT BINDING 81..84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20690587"
FT BINDING 101..102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20690587"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20690587"
FT BINDING 171..172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20690587"
FT CONFLICT 213
FT /note="A -> T (in Ref. 1; AAC45853)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="S -> W (in Ref. 2; AAM27797)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3OA2"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:3OA2"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:3OA2"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:3OA2"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:3OA2"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:3OA2"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:3OA2"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:3OA2"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:3OA2"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 181..197
FT /evidence="ECO:0007829|PDB:3OA2"
FT STRAND 199..208
FT /evidence="ECO:0007829|PDB:3OA2"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:3OA2"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:3OA2"
FT TURN 237..242
FT /evidence="ECO:0007829|PDB:3OA2"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 265..274
FT /evidence="ECO:0007829|PDB:3OA2"
FT HELIX 281..296
FT /evidence="ECO:0007829|PDB:3OA2"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:3OA2"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:3OA2"
SQ SEQUENCE 316 AA; 35718 MW; 838B976545FDF5E2 CRC64;
MKNFALIGAA GYIAPRHMRA IKDTGNCLVS AYDINDSVGI IDSISPQSEF FTEFEFFLDH
ASNLKRDSAT ALDYVSICSP NYLHYPHIAA GLRLGCDVIC EKPLVPTPEM LDQLAVIERE
TDKRLYNILQ LRHHQAIIAL KDKVAREKSP HKYEVDLTYI TSRGNWYLKS WKGDPRKSFG
VATNIGVHFY DMLHFIFGKL QRNVVHFTSE YKAAGYLEYE QARVRWFLSV DANDLPESVK
GKKPTYRSIT VNGEEMEFSE GFTDLHTTSY EEILAGRGYG IDDARHCVET VNTIRSAVIV
PASDNEGHPF VAALAR
