UGND_PSEAE
ID UGND_PSEAE Reviewed; 436 AA.
AC G3XD94; P72132; Q7DCB3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=UDP-N-acetyl-D-glucosamine 6-dehydrogenase {ECO:0000312|EMBL:AAG06547.1};
DE Short=UDP-D-GlcNAc 6-dehydrogenase;
DE EC=1.1.1.136 {ECO:0000269|PubMed:15226302};
DE AltName: Full=UDP-N-acetylglucosamine 6-dehydrogenase;
GN Name=wbpA {ECO:0000312|EMBL:AAG06547.1}; OrderedLocusNames=PA3159;
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:AAC45852.1}
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:AAC45852.1};
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:AAM27688.1}
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:AAG06547.1}
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:10930727};
RX PubMed=10930727; DOI=10.1111/j.1574-6968.2000.tb09219.x;
RA Burrows L.L., Pigeon K.E., Lam J.S.;
RT "Pseudomonas aeruginosa B-band lipopolysaccharide genes wbpA and wbpI and
RT their Escherichia coli homologues wecC and wecB are not functionally
RT interchangeable.";
RL FEMS Microbiol. Lett. 189:135-141(2000).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000269|PubMed:15226302};
RX PubMed=15226302; DOI=10.1074/jbc.m404749200;
RA Miller W.L., Wenzel C.Q., Daniels C., Larocque S., Brisson J.R., Lam J.S.;
RT "Biochemical characterization of WbpA, a UDP-N-acetyl-D-glucosamine 6-
RT dehydrogenase involved in O-antigen biosynthesis in Pseudomonas aeruginosa
RT PAO1.";
RL J. Biol. Chem. 279:37551-37558(2004).
RN [6] {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).
CC -!- FUNCTION: Plays a role in the biosynthesis of B-band O antigen for
CC serotype O5. Catalyzes the C-6 dehydrogenation of UDP-D-GlcNAc to UDP-
CC N-acetylglucosaminuronic acid (UDP-D-GlcNAcA).
CC {ECO:0000269|PubMed:10930727, ECO:0000269|PubMed:15226302,
CC ECO:0000269|PubMed:18621892}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + 2 NAD(+) + UDP-N-acetyl-alpha-D-glucosamine = 3 H(+) + 2
CC NADH + UDP-N-2-acetamido-2-deoxy-alpha-D-glucuronate;
CC Xref=Rhea:RHEA:13325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57705, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:65040; EC=1.1.1.136;
CC Evidence={ECO:0000269|PubMed:15226302};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:15226302};
CC Name=NH4(+); Xref=ChEBI:CHEBI:28938;
CC Evidence={ECO:0000269|PubMed:15226302};
CC Note=A monovalent cation. NH4(+) and K(+) are the most effective.
CC {ECO:0000269|PubMed:15226302};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.094 mM for UDP-D-GlcNAc {ECO:0000269|PubMed:15226302};
CC KM=0.22 mM for NAD(+) {ECO:0000269|PubMed:15226302};
CC Vmax=2.9 nmol/min/ug enzyme {ECO:0000269|PubMed:15226302};
CC pH dependence:
CC Optimum pH is 8.0-9.0. {ECO:0000269|PubMed:15226302};
CC Temperature dependence:
CC Optimum temperature is 33-37 degrees Celsius. Active from
CC temperatures ranging from 0 degrees Celsius to 65 degrees Celsius.
CC {ECO:0000269|PubMed:15226302};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:10930727,
CC ECO:0000269|PubMed:15226302, ECO:0000269|PubMed:18621892,
CC ECO:0000269|PubMed:8939432}.
CC -!- SUBUNIT: Homotrimer in solution. May also exist in a dimeric or
CC tetrameric form. {ECO:0000269|PubMed:15226302}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000255}.
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DR EMBL; U50396; AAC45852.1; -; Genomic_DNA.
DR EMBL; AF498410; AAM27688.1; -; Genomic_DNA.
DR EMBL; AF498412; AAM27723.1; -; Genomic_DNA.
DR EMBL; AF498413; AAM27743.1; -; Genomic_DNA.
DR EMBL; AF498416; AAM27796.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06547.1; -; Genomic_DNA.
DR PIR; A83252; A83252.
DR RefSeq; NP_251849.1; NC_002516.2.
DR RefSeq; WP_003113429.1; NZ_QZGE01000023.1.
DR AlphaFoldDB; G3XD94; -.
DR SMR; G3XD94; -.
DR STRING; 208964.PA3159; -.
DR PaxDb; G3XD94; -.
DR PRIDE; G3XD94; -.
DR EnsemblBacteria; AAG06547; AAG06547; PA3159.
DR GeneID; 879921; -.
DR KEGG; pae:PA3159; -.
DR PATRIC; fig|208964.12.peg.3303; -.
DR PseudoCAP; PA3159; -.
DR HOGENOM; CLU_023810_3_2_6; -.
DR InParanoid; G3XD94; -.
DR OMA; WDVIRCA; -.
DR PhylomeDB; G3XD94; -.
DR BioCyc; MetaCyc:MON-17572; -.
DR BioCyc; PAER208964:G1FZ6-3219-MON; -.
DR BRENDA; 1.1.1.336; 5087.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0003954; F:NADH dehydrogenase activity; EXP:PseudoCAP.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0047004; F:UDP-N-acetylglucosamine 6-dehydrogenase activity; EXP:PseudoCAP.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009243; P:O antigen biosynthetic process; EXP:PseudoCAP.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IDA:PseudoCAP.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017476; UDP-Glc/GDP-Man.
DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf.
DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR InterPro; IPR028359; UDP_ManNAc/GlcNAc_DH.
DR Pfam; PF00984; UDPG_MGDP_dh; 1.
DR Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR Pfam; PF03721; UDPG_MGDP_dh_N; 1.
DR PIRSF; PIRSF500136; UDP_ManNAc_DH; 1.
DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52413; SSF52413; 1.
DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Lipopolysaccharide biosynthesis;
KW Membrane; NAD; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..436
FT /note="UDP-N-acetyl-D-glucosamine 6-dehydrogenase"
FT /id="PRO_0000419012"
FT TRANSMEM 13..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 273
FT /evidence="ECO:0000250"
FT BINDING 13..34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 436 AA; 48155 MW; E389F13EBCFF840D CRC64;
MIDVNTVVEK FKSRQALIGI VGLGYVGLPL MLRYNAIGFD VLGIDIDDVK VDKLNAGQCY
IEHIPQAKIA KARASGFEAT TDFSRVSECD ALILCVPTPL NKYREPDMSF VINTTDALKP
YLRVGQVVSL ESTTYPGTTE EELLPRVQEG GLVVGRDIYL VYSPEREDPG NPNFETRTIP
KVIGGHTPQC LEVGIALYEQ AIDRVVPVSS TKAAEMTKLL ENIHRAVNIG LVNEMKIVAD
RMGIDIFEVV DAAATKPFGF TPYYPGPGLG GHCIPIDPFY LTWKAREYGL HTRFIELSGE
VNQAMPEYVL GKLMDGLNEA GRALKGSRVL VLGIAYKKNV DDMRESPSVE IMELIEAKGG
MVAYSDPHVP VFPKMREHHF ELSSEPLTAE NLARFDAVVL ATDHDKFDYE LIKAEAKLVV
DSRGKYRSPA AHIIKA
