UDP-N-acetylglucosamine pyrophosphorylase
     (EC 2.7.7.23)
     (N-acetylglucosamine-1-phosphate uridyltransferase)
Glucosamine-1-phosphate N-acetyltransferase
     (EC 2.3.1.157)

Gene name

	Name:	glmU
	Synonyms:	gcaD, tms

From

Bacillus megaterium

[TaxID: 1404]

Taxonomy

Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.

Protein existence

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=PV361; DOI=10.1016/0167-4781(92)90536-9; PubMed=1373326 [NCBI, ExPASy, EBI, Israel, Japan] Hudspeth D.S.S., Vary P.S.; "spoVG sequence of Bacillus megaterium and Bacillus subtilis."; Biochim. Biophys. Acta 1130:229-231(1992).

Comments

FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-GlcNAc. Responsible for the acetylation of Glc-N-1-P to give GlcNAc-1-P and for the uridyl transfer from UTP to GlcNAc-1-P which produces UDP-GlcNAc (By similarity).
CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.
CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-D-glucosamine.
COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from D-glucosamine 6-phosphate (route II): step 2/2 .
PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine biosynthesis; UDP-N-acetyl-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1 .
PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
SIMILARITY: In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X62377; CAA44241.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S18901; S18901.

3D structure databases

HSSP

P17114; 1HV9. [HSSP ENTRY / PDB]

ModBase

P28017.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0019134;	Molecular function: glucosamine-1-phosphate N-acetyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from HAMAP).
GO:0003977;	Molecular function: UDP-N-acetylglucosamine diphosphorylase activity (inferred from electronic annotation from HAMAP).
GO:0009252;	Biological process: peptidoglycan biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0008360;	Biological process: regulation of cell shape (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01631; -; 1.
PBIL [Tree]

InterPro

IPR001451; Hexapep_transf.
Graphical view of domain structure.

PROSITE

PS00101; HEXAPEP_TRANSFERASES; PARTIAL.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acyltransferase; Cell shape; Cell wall biogenesis/degradation; Cytoplasm; Magnesium; Metal-binding; Multifunctional enzyme; Nucleotidyltransferase; Peptidoglycan synthesis; Repeat; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 >68`	`>68`	`Bifunctional protein glmU.`	`PRO_0000068707`
`NON_TER`	`68 68`

Sequence information

Length: 68 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 7399 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: CD40139522E5A130 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKRYAVILA AGQGTRMKSS LYKVLHPVCG KPMVQHVIDQ LSRLDLTNLI TVVGHGAEKV 


KSHVGDKS

P28017 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools