ID   B7NR32_ECO7I            Unreviewed;       456 AA.
AC   B7NR32;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   16-JUN-2009, entry version 4.
DE   SubName: Full=Fused N-acetyl glucosamine-1-phosphate uridyltransferase ; glucosamine-1-phosphate acetyl transferase;
DE            EC=2.7.7.23;
GN   Name=glmU; OrderedLocusNames=ECIAI39_4334;
OS   Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA   Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA   Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA   Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA   Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA   Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA   Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Catalyzes the last two sequential reactions in the de
CC       novo biosynthetic pathway for UDP-GlcNAc. Responsible for the
CC       acetylation of Glc-N-1-P to give GlcNAc-1-P and for the uridyl
CC       transfer from UTP to GlcNAc-1-P which produces UDP-GlcNAc (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate =
CC       CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.
CC   -!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
CC       = diphosphate + UDP-N-acetyl-D-glucosamine.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A
CC       biosynthesis.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine
CC       biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from D-
CC       glucosamine 6-phosphate (route II): step 2/2.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine
CC       biosynthesis; UDP-N-acetyl-D-glucosamine from N-acetyl-alpha-D-
CC       glucosamine 1-phosphate: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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DR   EMBL; CU928164; CAR20440.1; -; Genomic_DNA.
DR   RefSeq; YP_002410209.1; -.
DR   GeneID; 7151521; -.
DR   GenomeReviews; CU928164_GR; ECIAI39_4334.
DR   InterPro; IPR001451; Hexapep_transf.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR001228; ISPD_synthase.
DR   InterPro; IPR005882; UDP_GlcNAc_PyrPase.
DR   Pfam; PF00132; Hexapep; 7.
DR   Pfam; PF01128; IspD; 1.
DR   TIGRFAMs; TIGR01173; glmU; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell shape; Cell wall biogenesis/degradation;
KW   Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Nucleotidyltransferase;
KW   Peptidoglycan synthesis; Repeat; Transferase.
SQ   SEQUENCE   456 AA;  49222 MW;  68947CA5BE6D553B CRC64;
     MLNNAMSVVI LAAGKGTRMY SDLPKVLHTL AGKAMVQHVI DAANELGAAH VHLVYGHGGD
     LLKQALKDDN LNWVLQAEQL GTGHAMQQAA PFFADDEDIL MLYGDVPLIS VETLQRLRDA
     KPQGGIGLLT VKLDDPTGYG RITRENGKVT GIVEHKDATD EQRQIQEINT GILIANGADM
     KRWLAKLTNN NAQGEYYITD IIALAYQEGR EIVAVHPQRL SEVEGVNNRL QLSRLERVYQ
     FEQAEKLLLA GVMLRDPARF DLRGTLTHGR DVEIDTNVII EGNVTLGHRV KIGTGCVIKN
     SVIGDDCEIS PYTVVEDANL AAACTIGPFA RLRPGAELLE GAHVGNFVEM KKARLGKGSK
     AGHLTYLGDA EVGDNVNIGA GTITCNYDGA NKFKTIIGDD VFVGSDTQLV APVTVGKGAT
     IAAGTTVTRN VGENALAISR VPQSQKEGWR RPVKKK
//