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:	bbp_029

From

Buchnera aphidicola subsp. Baizongia pistaciae

[TaxID: 135842]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).

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 .
SUBUNIT: Homotrimer (By similarity).
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

AE016826; AAO26772.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_777667.1; -.

3D structure databases

HSSP

P17114; 1HV9. [HSSP ENTRY / PDB]

ModBase

Q89B26.

Enzyme and pathway databases

BioCyc

BAPH224915:BBP_029-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; FALSE_NEG.

Genome annotation databases

GeneID

1058362; -.

GenomeReviews

AE016826_GR; bbp_029.

KEGG

bab:bbp029; -.

Phylogenomic databases

HOGENOM

Q89B26; -.

Genome annotation databases

CMR

Q89B26; bbp_029.

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`	`1 448`	`448`	`Bifunctional protein glmU.`	`PRO_0000068700`
`REGION`	`1 229`	`229`	`Pyrophosphorylase (By similarity).`
`REGION`	`11 14`	`4`	`Substrate binding (By similarity).`
`REGION`	`81 82`	`2`	`Substrate binding (By similarity).`
`REGION`	`230 250`	`21`	`Linker (By similarity).`
`REGION`	`251 448`	`198`	`N-acetyltransferase (By similarity).`
`ACT_SITE`	`363 363`		`Proton acceptor (By similarity).`
`METAL`	`105 105`		`Magnesium (By similarity).`
`METAL`	`227 227`		`Magnesium (By similarity).`
`BINDING`	`76 76`		`Substrate (By similarity).`
`BINDING`	`140 140`		`Substrate; via amide nitrogen (By similarity).`
`BINDING`	`154 154`		`Substrate (By similarity).`
`BINDING`	`169 169`		`Substrate (By similarity).`
`BINDING`	`387 387`		`Acetyl-CoA (By similarity).`
`BINDING`	`405 405`		`Acetyl-CoA (By similarity).`
`BINDING`	`423 423`		`Acetyl-CoA; via amide nitrogen (By similarity).`

Sequence information

Length: 448 AA [This is the length of the unprocessed precursor]

Molecular weight: 50129 Da [This is the MW of the unprocessed precursor]

CRC64: FDEE666538B7AB9B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNNHTLNIII LAAGKGTRMQ FDHPKLLHLL GGKPILEHVI NLAQSLCPKT ITVIYNKQYK 

        70         80         90        100        110        120 
KFKIKNKNNS ITWIKQKKIL GTGNAISQII NNYKDHENIL ILYGDVPLIS KNSIQKMLLK 

       130        140        150        160        170        180 
KKNSTITLLT AKLNNPEEYG RIIRKNKKIV KIIEYKDATD EQLNIKEVNS GILIVSSTNL 

       190        200        210        220        230        240 
KKWIFQIHAK NNQNEYYITD IISLANKDNH KINSVRPEKN DEIQGINNLL QLVRAEKIYQ 

       250        260        270        280        290        300 
KQQAKLLLLS GIMIYNPSNF SLRGTLKHGK NIKIDHGVIL EGSVKIGNSV IIEPGCIIKN 

       310        320        330        340        350        360 
STIGNNCTIK AYSIIEKTII SNKCIVGPFT HLQHGTVLKN NTHVGNFVEI KKTTLGSYSK 

       370        380        390        400        410        420 
AKHLSYLGNS QIGQKVNIGA GTVTCNYNGK KKLDTIIGDN VFIGSSTQLI APINIKKGTI 

       430        440 
IAAGTTVMKN IHEPSLVYNE KKQIHKKL

Q89B26 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