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
	OrderedLocusNames:	Bcep18194_A6330

From

Burkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194))

[TaxID: 269483]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.;
"Complete sequence of chromosome 1 of Burkholderia sp. 383.";
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.

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

CP000151; ABB09924.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_370568.1; -.

3D structure databases

ModBase

Q39C92.

Enzyme and pathway databases

BioCyc

BSP36773:BCEP18194_A6330-MON; -.

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:0008299;	Biological process: isoprenoid biosynthetic process (inferred from electronic annotation from InterPro).
GO:0009103;	Biological process: lipopolysaccharide biosynthetic process (inferred from electronic annotation from InterPro).
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.
IPR001228; ISPD_synthase.
IPR005882; UDP_GlcNAc_PyrPase.
Graphical view of domain structure.

Pfam

PF00132; Hexapep; 6.
PF01128; IspD; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01173; glmU; 1.

PROSITE

PS00101; HEXAPEP_TRANSFERASES; 2.

ProtoNet

Q39C92.

Genome annotation databases

GeneID

3751563; -.

GenomeReviews

CP000151_GR; Bcep18194_A6330.

KEGG

bur:Bcep18194_A6330; -.

NMPDR

fig|269483.3.peg.7149; -.

Phylogenomic databases

HOGENOM

Q39C92; -.

Genome annotation databases

CMR

Q39C92; Bcep18194_A6330.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 453`	`453`	`Bifunctional protein glmU.`	`PRO_0000233750`
`REGION`	`1 225`	`225`	`Pyrophosphorylase (By similarity).`
`REGION`	`6 9`	`4`	`Substrate binding (By similarity).`
`REGION`	`76 77`	`2`	`Substrate binding (By similarity).`
`REGION`	`226 246`	`21`	`Linker (By similarity).`
`REGION`	`247 453`	`207`	`N-acetyltransferase (By similarity).`
`ACT_SITE`	`359 359`		`Proton acceptor (By similarity).`
`METAL`	`100 100`		`Magnesium (By similarity).`
`METAL`	`223 223`		`Magnesium (By similarity).`
`BINDING`	`71 71`		`Substrate (By similarity).`
`BINDING`	`135 135`		`Substrate; via amide nitrogen (By similarity).`
`BINDING`	`150 150`		`Substrate (By similarity).`
`BINDING`	`165 165`		`Substrate (By similarity).`
`BINDING`	`383 383`		`Acetyl-CoA (By similarity).`
`BINDING`	`401 401`		`Acetyl-CoA (By similarity).`
`BINDING`	`419 419`		`Acetyl-CoA; via amide nitrogen (By similarity).`

Sequence information

Length: 453 AA [This is the length of the unprocessed precursor]

Molecular weight: 48063 Da [This is the MW of the unprocessed precursor]

CRC64: 0E329ED377FA4FAE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNIVILAAGT GKRMRSALPK VLHPLAGRPL LSHVIDTART LQPSRLVVVV GHGAEQVQAA 

        70         80         90        100        110        120 
VAAPDVQFAV QAEQLGTGHA VRQALPLLDP AQPTLVLYGD VPLTRASTLQ RLVDAAREGR 

       130        140        150        160        170        180 
YGILTVTLDD PTGYGRIVRD AAGFVTRIVE QKDASPEQLK IAEINTGIIV TPTAQLSMWL 

       190        200        210        220        230        240 
GALKNENAQG EYYLTDVVEL AIEAGFEVVT AQPDEEWETL GVNSKAQLAE LERIHQRNIA 

       250        260        270        280        290        300 
EALLVDGVTL ADPARLDVRG TLRCGRDVSI DVNCVFEGNV TLADNVTIGA NCVIRNASVG 

       310        320        330        340        350        360 
AGTRIDAFTH IDGAELGAHT VIGPYARLRP GAQLADEAHV GNFVEVKNAV IGHGSKANHL 

       370        380        390        400        410        420 
TYIGDADIGA RVNIGAGTIT CNYDGANKFR TVIEDDVFVG SDTQLVAPVR VGRGVTIAAG 

       430        440        450 
TTIWKDVADG LLALNEKTQT AKSGYVRPVK KKS

Q39C92 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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