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:	Cj0821

From

Campylobacter jejuni

[TaxID: 197]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.

Protein existence

1: Evidence at protein level;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC 11168 / Serotype O:2;
DOI=10.1038/35001088; PubMed=10688204 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., Barrell B.G.;
"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences.";
Nature 403:665-668(2000).

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 .
INTERACTION:
Q0PBJ0:fliG; NbExp=1; IntAct=EBI-1194402, EBI-1191336;
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

AL111168; CAL34949.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E81354; E81354.

3D structure databases

HSSP

Q97R46; 1HM0. [HSSP ENTRY / PDB]

ModBase

Q9PPA2.

Protein-protein interaction databases

IntAct

Q9PPA2; -.

Enzyme and pathway databases

BioCyc

CJEJ192222:CJ0821-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:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
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

IPR001451; Hexapep_transf.
IPR005835; NTP_transferase.
IPR005882; UDP_GlcNAc_PyrPase.
Graphical view of domain structure.

Pfam

PF00132; Hexapep; 4.
PF00483; NTP_transferase; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01173; glmU; 1.

PROSITE

PS00101; HEXAPEP_TRANSFERASES; FALSE_NEG.

ProtoNet

Q9PPA2.

Genome annotation databases

GenomeReviews

AL111168_GR; Cj0821.

KEGG

cje:Cj0821; -.

CMR

Q9PPA2; Cj0821.

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`	`1 429`	`429`	`Bifunctional protein glmU.`	`PRO_0000233751`
`REGION`	`1 223`	`223`	`Pyrophosphorylase (By similarity).`
`REGION`	`8 11`	`4`	`Substrate binding (By similarity).`
`REGION`	`81 82`	`2`	`Substrate binding (By similarity).`
`REGION`	`224 244`	`21`	`Linker (By similarity).`
`REGION`	`245 429`	`185`	`N-acetyltransferase (By similarity).`
`ACT_SITE`	`336 336`		`Proton acceptor (By similarity).`
`METAL`	`102 102`		`Magnesium (By similarity).`
`METAL`	`221 221`		`Magnesium (By similarity).`
`BINDING`	`135 135`		`Substrate; via amide nitrogen (By similarity).`
`BINDING`	`149 149`		`Substrate (By similarity).`
`BINDING`	`164 164`		`Substrate (By similarity).`
`BINDING`	`360 360`		`Acetyl-CoA (By similarity).`
`BINDING`	`378 378`		`Acetyl-CoA (By similarity).`
`BINDING`	`396 396`		`Acetyl-CoA; via amide nitrogen (By similarity).`
`BINDING`	`413 413`		`Acetyl-CoA (By similarity).`

Sequence information

Length: 429 AA [This is the length of the unprocessed precursor]

Molecular weight: 47906 Da [This is the MW of the unprocessed precursor]

CRC64: 914CFD5EA6281BFF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKTSILILAA GLGTRIKSQK PKVLQELCQK SMILHILKKA FALSDDVSVV LSHQKERVEK 

        70         80         90        100        110        120 
EILEYFPKTQ ILEQDLQNYP GTAGALSGFE PKNERVLILC GDMPLVEQTS LEALLGNNAK 

       130        140        150        160        170        180 
LNLAVFKARD PKSYGRVVIK NDSVEKIVEF KDANTQEKEI NTCNAGVYVI DSRLLKELLP 

       190        200        210        220        230        240 
LIDNNNAAKE YYLTDIVKLA KEKDVMIKAV FVDEDEFMGI NDKFELSIAE NFMQKKIKKY 

       250        260        270        280        290        300 
WMQQGVIFHL PQSTFIGADV EFVGECEVYE NVRIEGKSKI INSIIKSSSV IENSIVENSD 

       310        320        330        340        350        360 
VGPLAHLRPN CELKNTHIGN FVECKNAKLN TVKAGHLSYL GDCEIDSGTN IGCGTITCNY 

       370        380        390        400        410        420 
DGVKKHKTII GKNVFVGSDT QFIAPVKIED EVIIAAGSTV SINVEKGALF INRAGHKMIK 


DYYYKKFQK

Q9PPA2 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