WBJC_PSEA1
ID WBJC_PSEA1 Reviewed; 372 AA.
AC Q9XC60; A0A022PF25;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=UDP-2-acetamido-2,6-beta-L-arabino-hexul-4-ose reductase {ECO:0000305|PubMed:12464616};
DE EC=1.1.1.367 {ECO:0000269|PubMed:12464616, ECO:0000269|PubMed:15778500};
GN Name=wbjC {ECO:0000303|PubMed:10400585};
GN ORFNames=PA103_0193 {ECO:0000312|EMBL:EYU08748.1};
OS Pseudomonas aeruginosa (strain ATCC 29260 / BCRC 12902 / CIP 102967 / NCIMB
OS 11965 / PA103).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1081927;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29260 / BCRC 12902 / CIP 102967 / NCIMB 11965 / PA103;
RX PubMed=10400585; DOI=10.1128/jb.181.14.4275-4284.1999;
RA Dean C.R., Franklund C.V., Retief J.D., Coyne M.J. Jr., Hatano K.,
RA Evans D.J., Pier G.B., Goldberg J.B.;
RT "Characterization of the serogroup O11 O-antigen locus of Pseudomonas
RT aeruginosa PA103.";
RL J. Bacteriol. 181:4275-4284(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29260 / BCRC 12902 / CIP 102967 / NCIMB 11965 / PA103;
RA Ozer E.A., Allen J.P., Hauser A.R.;
RT "Characterization of the core and accessory genome of Pseudomonas
RT aeruginosa.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCGM 1900;
RA Tada T., Miyoshi-Akiyama T., Shimada K., Shimojima M., Kirikae T.;
RT "Complete genome sequence of Pseudomonas aeruginosa NCGM1900.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=12464616; DOI=10.1074/jbc.m203867200;
RA Kneidinger B., O'Riordan K., Li J., Brisson J.R., Lee J.C., Lam J.S.;
RT "Three highly conserved proteins catalyze the conversion of UDP-N-acetyl-D-
RT glucosamine to precursors for the biosynthesis of O antigen in Pseudomonas
RT aeruginosa O11 and capsule in Staphylococcus aureus type 5. Implications
RT for the UDP-N-acetyl-L-fucosamine biosynthetic pathway.";
RL J. Biol. Chem. 278:3615-3627(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15778500; DOI=10.1074/jbc.m500612200;
RA Mulrooney E.F., Poon K.K., McNally D.J., Brisson J.R., Lam J.S.;
RT "Biosynthesis of UDP-N-acetyl-L-fucosamine, a precursor to the biosynthesis
RT of lipopolysaccharide in Pseudomonas aeruginosa serotype O11.";
RL J. Biol. Chem. 280:19535-19542(2005).
CC -!- FUNCTION: Bifunctional enzyme that mediates C-3 epimerization of the
CC second intermediate followed by reduction at C-4 during serogroup O11
CC O-antigen biosynthesis, thus catalyzing the conversion of UDP-N-acetyl-
CC D-glucosamine to precursors for the biosynthesis of O antigen.
CC {ECO:0000269|PubMed:12464616, ECO:0000269|PubMed:15778500}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-
CC 4-ulose = NAD(+) + UDP-2-acetamido-2,6-dideoxy-beta-L-talose;
CC Xref=Rhea:RHEA:40159, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:60101, ChEBI:CHEBI:62372;
CC EC=1.1.1.367; Evidence={ECO:0000269|PubMed:12464616,
CC ECO:0000269|PubMed:15778500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-
CC 4-ulose = NADP(+) + UDP-2-acetamido-2,6-dideoxy-beta-L-talose;
CC Xref=Rhea:RHEA:30835, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:60101, ChEBI:CHEBI:62372;
CC EC=1.1.1.367; Evidence={ECO:0000269|PubMed:12464616,
CC ECO:0000269|PubMed:15778500};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9. {ECO:0000303|PubMed:15778500};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000303|PubMed:12464616}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P09147}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AF147795; AAD45266.1; -; Genomic_DNA.
DR EMBL; JARI01000007; EYU08748.1; -; Genomic_DNA.
DR EMBL; AP014622; BAP22247.1; -; Genomic_DNA.
DR RefSeq; WP_003091436.1; NZ_KK111590.1.
DR AlphaFoldDB; Q9XC60; -.
DR SMR; Q9XC60; -.
DR KEGG; paeb:NCGM1900_3148; -.
DR PATRIC; fig|1081927.4.peg.190; -.
DR HOGENOM; CLU_063221_0_0_6; -.
DR UniPathway; UPA00281; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009243; P:O antigen biosynthetic process; IDA:UniProtKB.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase.
FT CHAIN 1..372
FT /note="UDP-2-acetamido-2,6-beta-L-arabino-hexul-4-ose
FT reductase"
FT /id="PRO_0000430726"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 7..30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q93VR3"
FT BINDING 53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 103
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q93VR3"
FT BINDING 107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q93VR3"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 279..282
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
SQ SEQUENCE 372 AA; 41437 MW; 5B4FA8A7DAEC3D45 CRC64;
MKVLVTGANG FVGRNLCAHL AERGGIEVVP FTRESSVGNL PELIRSVDFI FHLAGVNRPE
KPEEFKIGNS ELTYALCEAV RSNGRAIPLL YTSSIQAEVD NEYGLSKRAA EEHLQVLGED
IGCPVYIFRL PNVFGKWSRP NYNSAVATFC HNIIRDIPIQ INNSSAEITL VYIDDVVRTF
MKVMDGKLSN AVSLQVEPQY QISVGELAEQ LYEFRNSRKS LTTARVGSGL TRALYSTYLS
FLPEDSFSYD VPMHSDPRGT FVEMLKTADS GQFSFFTAHP GVTRGGHYHH SKTEKFLVIK
GMARFKFRNI LTGAFYEICT NGEKAEIVET VPGWTHDITN VGTDDMVVML WANEVFDREN
PDTYACSVGE GA
