UniProt functional annotation for P9WMN3

UniProt code: P9WMN3.

Organism:		Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Taxonomy:		Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
Function:		Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:19237750}.
Catalytic activity:		Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N- acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:19237750};
Catalytic activity:		Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:19237750};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:19237750, ECO:0000269|PubMed:23485416, ECO:0000269|Ref.7, ECO:0000269|Ref.8}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:23485416, ECO:0000269|Ref.8}; Note=Binds 1 Mg(2+) ion per subunit (PubMed:19237750, PubMed:19121323, Ref.7, Ref.8, PubMed:23485416). Can also use Co(2+) ion to a lesser extent (Ref.8) (PubMed:23485416). {ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:19237750, ECO:0000269|PubMed:23485416, ECO:0000269|Ref.7, ECO:0000269|Ref.8};
Biophysicochemical properties:		Kinetic parameters: KM=106.75 uM for GlcNAc-1-P (at pH 7.6) {ECO:0000269|PubMed:19121323}; KM=61.86 uM for UTP (at pH 7.6) {ECO:0000269|PubMed:19121323}; KM=240 uM for GlcN-1-P (at pH 7.6) {ECO:0000269|PubMed:19121323}; KM=304 uM for acetyl-CoA (at pH 7.6) {ECO:0000269|PubMed:19121323}; Vmax=1.869 umol/min/mg enzyme (Uridyltransferase activity) (at pH 7.6) {ECO:0000269|PubMed:19121323}; Vmax=4.489 umol/min/mg enzyme (Acetyltransferase activity) (at pH 7.6) {ECO:0000269|PubMed:19121323};
Pathway:		Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. {ECO:0000255|HAMAP-Rule:MF_01631}.
Pathway:		Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N- acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. {ECO:0000255|HAMAP- Rule:MF_01631}.
Pathway:		Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01631}.
Subunit:		Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:19237750, ECO:0000269|PubMed:19407371, ECO:0000269|Ref.7}.
Subcellular location:		Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}.
Ptm:		Phosphorylated at the C-terminal domain by PknB. The phosphorylation is required for acetyltransferase activity, but does not affect uridyltransferase activity. {ECO:0000269|PubMed:19121323}.
Similarity:		In the N-terminal section; belongs to the N- acetylglucosamine-1-phosphate uridyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01631}.
Similarity:		In the C-terminal section; belongs to the transferase hexapeptide repeat family. {ECO:0000255|HAMAP-Rule:MF_01631}.

Annotations taken from UniProtKB at the EBI.