GNU_ECO57
ID GNU_ECO57 Reviewed; 331 AA.
AC Q8X7P7;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase {ECO:0000303|PubMed:19923219};
DE EC=5.1.3.26 {ECO:0000269|PubMed:19923219};
DE AltName: Full=GlcNAc-P-P-Und 4-epimerase {ECO:0000303|PubMed:19923219};
GN Name=gnu {ECO:0000303|PubMed:23799153};
GN Synonyms=gne {ECO:0000303|PubMed:19923219};
GN OrderedLocusNames=Z3206, ECs2847;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O55:H7;
RX PubMed=11976290; DOI=10.1128/jb.184.10.2620-2625.2002;
RA Wang L., Huskic S., Cisterne A., Rothemund D., Reeves P.R.;
RT "The O-antigen gene cluster of Escherichia coli O55:H7 and identification
RT of a new UDP-GlcNAc C4 epimerase gene.";
RL J. Bacteriol. 184:2620-2625(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=19923219; DOI=10.1074/jbc.m109.061630;
RA Rush J.S., Alaimo C., Robbiani R., Wacker M., Waechter C.J.;
RT "A novel epimerase that converts GlcNAc-P-P-undecaprenol to GalNAc-P-P-
RT undecaprenol in Escherichia coli O157.";
RL J. Biol. Chem. 285:1671-1680(2010).
RN [5]
RP FUNCTION.
RX PubMed=23799153; DOI=10.1371/journal.pone.0067646;
RA Cunneen M.M., Liu B., Wang L., Reeves P.R.;
RT "Biosynthesis of UDP-GlcNAc, UndPP-GlcNAc and UDP-GlcNAcA involves three
RT easily distinguished 4-epimerase enzymes, Gne, Gnu and GnaB.";
RL PLoS ONE 8:E67646-E67646(2013).
CC -!- FUNCTION: Involved in biosynthesis of the repeating tetrasaccharide
CC unit of the O-antigen. Catalyzes the reversible epimerization of the
CC hydroxyl group at position C4 of undecaprenyl pyrophosphate-N-
CC acetylglucosamine (UndPP-GlcNAc) to yield undecaprenyl pyrophosphate-N-
CC acetylgalactosamine (UndPP-GalNAc). {ECO:0000269|PubMed:19923219,
CC ECO:0000303|PubMed:23799153}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl
CC diphosphate = N-acetyl-alpha-D-galactosaminyl-di-trans,octa-cis-
CC undecaprenyl diphosphate; Xref=Rhea:RHEA:34103, ChEBI:CHEBI:62959,
CC ChEBI:CHEBI:74214; EC=5.1.3.26;
CC Evidence={ECO:0000269|PubMed:19923219};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:P09147};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19923219}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AF461121; AAL67550.1; -; Genomic_DNA.
DR EMBL; AE005174; AAG57102.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36270.1; -; Genomic_DNA.
DR PIR; B85830; B85830.
DR PIR; G90984; G90984.
DR RefSeq; NP_310874.1; NC_002695.1.
DR RefSeq; WP_000999466.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X7P7; -.
DR SMR; Q8X7P7; -.
DR STRING; 155864.EDL933_3114; -.
DR EnsemblBacteria; AAG57102; AAG57102; Z3206.
DR EnsemblBacteria; BAB36270; BAB36270; ECs_2847.
DR GeneID; 66674060; -.
DR GeneID; 912320; -.
DR KEGG; ece:Z3206; -.
DR KEGG; ecs:ECs_2847; -.
DR PATRIC; fig|386585.9.peg.2980; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_6_2_6; -.
DR OMA; PLGAIHN; -.
DR BioCyc; MetaCyc:MON-18065; -.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IDA:UniProtKB.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell membrane; Galactose metabolism;
KW Glucose metabolism; Isomerase; Membrane; NAD; Reference proteome.
FT CHAIN 1..331
FT /note="N-acetyl-alpha-D-glucosaminyl-diphospho-
FT ditrans,octacis-undecaprenol 4-epimerase"
FT /id="PRO_0000183266"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P09147"
FT BINDING 13..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147"
FT BINDING 34..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147"
FT BINDING 47..48
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147"
FT BINDING 109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09147"
FT BINDING 132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09147"
FT BINDING 136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147"
FT BINDING 183..184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09147"
FT BINDING 199..201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09147"
SQ SEQUENCE 331 AA; 37142 MW; 02F50912AC721273 CRC64;
MNDNVLLIGA SGFVGTRLLE TAIADFNIKN LDKQQSHFYP EITQIGDVRD QQALDQALAG
FDTVVLLAAE HRDDVSPTSL YYDVNVQGTR NVLAAMEKNG VKNIIFTSSV AVYGLNKHNP
DENHPHDPFN HYGKSKWQAE EVLREWYNKA PTERSLTIIR PTVIFGERNR GNVYNLLKQI
AGGKFMMVGA GTNYKSMAYV GNIVEFIKYK LKNVAAGYEV YNYVDKPDLN MNQLVAEVEQ
SLNKKIPSMH LPYPLGMLGG YCFDILSKIT GKKYAVSSVR VKKFCATTQF DATKVHSSGF
VAPYTLSQGL DRTLQYEFVH AKKDDITFVS E
