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Database: UniProt
Entry: A0A0G0LT51_9BACT
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ID   A0A0G0LT51_9BACT        Unreviewed;       410 AA.
AC   A0A0G0LT51;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Bifunctional protein GlmU {ECO:0000313|EMBL:KKQ55766.1};
GN   ORFNames=US75_C0014G0015 {ECO:0000313|EMBL:KKQ55766.1};
OS   Candidatus Woesebacteria bacterium GW2011_GWC1_38_13.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1618583 {ECO:0000313|EMBL:KKQ55766.1, ECO:0000313|Proteomes:UP000034096};
RN   [1] {ECO:0000313|EMBL:KKQ55766.1, ECO:0000313|Proteomes:UP000034096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
CC         diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
CC         Evidence={ECO:0000256|ARBA:ARBA00001851};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-
CC         acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157;
CC         Evidence={ECO:0000256|ARBA:ARBA00000731};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC       glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC       alpha-D-glucosamine 6-phosphate (route II): step 2/2.
CC       {ECO:0000256|ARBA:ARBA00005166}.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC       glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
CC       acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005208}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC       hexapeptide repeat family. {ECO:0000256|ARBA:ARBA00007707}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC       acetylglucosamine-1-phosphate uridyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00007947}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKQ55766.1}.
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DR   EMBL; LBUE01000014; KKQ55766.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0LT51; -.
DR   STRING; 1618583.US75_C0014G0015; -.
DR   UniPathway; UPA00113; UER00532.
DR   Proteomes; UP000034096; Unassembled WGS sequence.
DR   GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR023915; Bifunctiontional_GlmU_arc-type.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   NCBIfam; TIGR03992; Arch_glmU; 1.
DR   PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR   PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..193
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   410 AA;  45553 MW;  15C4248D994034EA CRC64;
     MKNQIVILAA GDSSRFYPFN GVHKSLFQIA GKPLLKHTLD NVGKLKDFEI ILVLSRKNQK
     VEREILENMS IGNGVRIIYQ KNSLGQGDGI LTAKELIKEN FFVINAQQFN FNSQKYFLGL
     QRTQNIYSAV VGALTTEEPW KYGVLKLDKD KVLGIVEKPE RGKEPSNVRI SGIYYFSKEF
     LSELEKTNIS EYSLEDTLNR LAGFGKVGKV DLDQETPSLK YPWDLLKVKN YFLGDLKRNI
     YEKSQISSSA TIRGDVYIGK GAMVYDYAVI DGPAYIGDDA VIGAYCHIRG GSVIEKNAEL
     QHYVDFKNSV IGEHSTIHSG FIGDSIIGKN VKIGAGFITA NKRLDRENVR VFVKGVKVDS
     NLRGLGLIIG DNTKLGICVT AMPGTVVGEN STVYPNAKLS GTYQNNQKIK
//
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