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:	Atu1787
	ORFNames:	AGR_C_3287

From

Agrobacterium tumefaciens (strain C58 / ATCC 33970)

[TaxID: 176299]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1066804; PubMed=11743193 [NCBI, ExPASy, EBI, Israel, Japan]
Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., Nester E.W.;
"The genome of the natural genetic engineer Agrobacterium tumefaciens C58.";
Science 294:2317-2323(2001).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1066803; PubMed=11743194 [NCBI, ExPASy, EBI, Israel, Japan]
Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58.";
Science 294:2323-2328(2001).

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

AE007869; AAK87557.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

AD2796; AD2796.
D97575; D97575.

RefSeq

NP_354772.1; -.

3D structure databases

HSSP

P17114; 1HV9. [HSSP ENTRY / PDB]

ModBase

Q8UEH0.

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: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

IPR003329; Cytidylyl_trans.
IPR001451; Hexapep_transf.
IPR005882; UDP_GlcNAc_PyrPase.
Graphical view of domain structure.

Pfam

PF02348; CTP_transf_3; 1.
PF00132; Hexapep; 6.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01173; glmU; 1.

PROSITE

PS00101; HEXAPEP_TRANSFERASES; 1.

ProtoNet

Q8UEH0.

Genome annotation databases

GeneID

1133825; -.

GenomeReviews

AE007869_GR; Atu1787.

KEGG

atc:AGR_C_3287; -.
atu:Atu1787; -.

Phylogenomic databases

HOGENOM

Q8UEH0; -.

Genome annotation databases

CMR

Q8UEH0; Atu1787.

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_0000233721`
`REGION`	`1 231`	`231`	`Pyrophosphorylase (By similarity).`
`REGION`	`10 13`	`4`	`Substrate binding (By similarity).`
`REGION`	`82 83`	`2`	`Substrate binding (By similarity).`
`REGION`	`232 252`	`21`	`Linker (By similarity).`
`REGION`	`253 453`	`201`	`N-acetyltransferase (By similarity).`
`ACT_SITE`	`348 348`		`Proton acceptor (By similarity).`
`METAL`	`107 107`		`Magnesium (By similarity).`
`METAL`	`229 229`		`Magnesium (By similarity).`
`BINDING`	`77 77`		`Substrate (By similarity).`
`BINDING`	`143 143`		`Substrate (By similarity).`
`BINDING`	`157 157`		`Substrate (By similarity).`
`BINDING`	`172 172`		`Substrate (By similarity).`
`BINDING`	`372 372`		`Acetyl-CoA (By similarity).`
`BINDING`	`390 390`		`Acetyl-CoA (By similarity).`
`BINDING`	`425 425`		`Acetyl-CoA (By similarity).`

Sequence information

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

Molecular weight: 47877 Da [This is the MW of the unprocessed precursor]

CRC64: 9F1826910319BD1C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MERSSLAVIL AAGDSTRMKS SKSKVLHPVA GRPMIGHVVE AVAGAGVGAV ALVVGRDADN 

        70         80         90        100        110        120 
VAAAASLKGL QVEAFLQKER KGTGHAVLAA REAIKRGFDD VIVAYGDVPL ITSATLDRAR 

       130        140        150        160        170        180 
EAIAAGADVA VIGFHTDRPT GYGRLLVENG ELVAIREEKD ATDEERKVTW CNSGLMAING 

       190        200        210        220        230        240 
RNALDLLDRI GNSNVKGEYY LTDVVEIARS LGRRAIAIDA PEKELTGCNN RAELAFIERL 

       250        260        270        280        290        300 
WQERRRHELM VDGVSMIAPE TVFLSFDTKI GQDVLIEPNV VFGPGVTIEP GAIVHAFSHL 

       310        320        330        340        350        360 
EGAHLAEGAV VGPFARLRPG ANLHANAKVG NFCEVKKAEI GEGAKVNHLT YIGDAFVGAG 

       370        380        390        400        410        420 
SNIGAGAITC NYDGYNKSET RIGANSFIGS NSSLVAPVTI GERAYIASGS VITDDVPADA 

       430        440        450 
LAFGRARQEV KPGRAVALRE RAKAQKEAKK KSS

Q8UEH0 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