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:	bll4608

From

Bradyrhizobium japonicum

[TaxID: 375]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Bradyrhizobium.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(2002).

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

BA000040; BAC49873.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_771248.1; -.

3D structure databases

HSSP

Q97R46; 1G95. [HSSP ENTRY / PDB]

ModBase

Q89LD7.

Enzyme and pathway databases

BioCyc

BJAP224911:BLL4608-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; 7.
PF01128; IspD; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01173; glmU; 1.

PROSITE

PS00101; HEXAPEP_TRANSFERASES; 1.

Genome annotation databases

GeneID

1052462; -.

GenomeReviews

BA000040_GR; bll4608.

KEGG

bja:bll4608; -.

NMPDR

fig|224911.1.peg.4608; -.

Phylogenomic databases

HOGENOM

Q89LD7; -.

Genome annotation databases

CMR

Q89LD7; bll4608.

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`	`1 451`	`451`	`Bifunctional protein glmU.`	`PRO_0000233743`
`REGION`	`1 232`	`232`	`Pyrophosphorylase (By similarity).`
`REGION`	`11 14`	`4`	`Substrate binding (By similarity).`
`REGION`	`83 84`	`2`	`Substrate binding (By similarity).`
`REGION`	`233 253`	`21`	`Linker (By similarity).`
`REGION`	`254 451`	`198`	`N-acetyltransferase (By similarity).`
`ACT_SITE`	`349 349`		`Proton acceptor (By similarity).`
`METAL`	`108 108`		`Magnesium (By similarity).`
`METAL`	`230 230`		`Magnesium (By similarity).`
`BINDING`	`78 78`		`Substrate (By similarity).`
`BINDING`	`144 144`		`Substrate (By similarity).`
`BINDING`	`158 158`		`Substrate (By similarity).`
`BINDING`	`173 173`		`Substrate (By similarity).`
`BINDING`	`373 373`		`Acetyl-CoA (By similarity).`
`BINDING`	`426 426`		`Acetyl-CoA (By similarity).`

Sequence information

Length: 451 AA [This is the length of the unprocessed precursor]

Molecular weight: 47462 Da [This is the MW of the unprocessed precursor]

CRC64: 352471823C117F71 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTARSSLTIV LAAGEGTRMR SHLPKVLHPV AHQTLLAHVL TAAPKGTGTS LAVVIGPDHQ 

        70         80         90        100        110        120 
AVADEARRIR PDAVTFVQAE RLGTAHAVLA AREAIARGVD DLLIAFGDTP LISAETFARL 

       130        140        150        160        170        180 
RAPLANGAAL AALGFRAADP AGYGRFIVEG DRLVAIREQA DASADERKID LCNAGVMAID 

       190        200        210        220        230        240 
GRRALAILDK IGNANSKGEY YLTDAVEIVR EQGWESVVIE TSEDEVRGIN TKAQLAEAES 

       250        260        270        280        290        300 
VMQARLRKAA MEAGVTLIAP ETVYLSADTV FGKDVTIEPF VVIGPGVSIA DGTVIHSFSH 

       310        320        330        340        350        360 
IVETTLGRNV SIGPYARLRP GTSLGDGARI GNFVETKAAT LEAGVKVNHL SYIGDATVGA 

       370        380        390        400        410        420 
NSNIGAGTIT CNYDGFKKHK TIIGQGAFVG TNSSLVAPVK IGNGAYIGSG SVITRDVPDD 

       430        440        450 
AMALERNQQT IREGGAARYR EMKTRGKKPE K

Q89LD7 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