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:	BUsg_028

From

Buchnera aphidicola subsp. Schizaphis graminum

[TaxID: 98794]

[HAMAP proteome]

Taxonomy

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

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(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 .
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

AE013218; AAM67599.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_660388.1; -.

3D structure databases

HSSP

P17114; 1HV9. [HSSP ENTRY / PDB]

ModBase

Q8KA74.

Enzyme and pathway databases

BioCyc

BAPH198804:BUSG028-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; 5.
PF01128; IspD; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01173; glmU; 1.

PROSITE

PS00101; HEXAPEP_TRANSFERASES; FALSE_NEG.

ProtoNet

Q8KA74.

Genome annotation databases

GeneID

1005844; -.

GenomeReviews

AE013218_GR; BUsg_028.

KEGG

bas:BUsg028; -.

Phylogenomic databases

HOGENOM

Q8KA74; -.

Genome annotation databases

CMR

Q8KA74; BUsg_028.

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`	`1 461`	`461`	`Bifunctional protein glmU.`	`PRO_0000068699`
`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`	`251 461`	`211`	`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`	`387 387`		`Acetyl-CoA (By similarity).`
`BINDING`	`423 423`		`Acetyl-CoA; via amide nitrogen (By similarity).`

Sequence information

Length: 461 AA [This is the length of the unprocessed precursor]

Molecular weight: 51735 Da [This is the MW of the unprocessed precursor]

CRC64: 6D38A10B70780C10 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLKKEINVVI LAAGKGTRMQ SSYPKVLHKL GGKTILEHVI NIAKSVKPKK IILVYNNKEK 

        70         80         90        100        110        120 
EIKSKISDTS IDWVIQKEQK GTGDAILKAS KKFSDKDDIV VLYGDMPYIS IESIKKLFTS 

       130        140        150        160        170        180 
KKQSDISLLT AYVKNPDGYG RVFKKNGKVI KIIEEQDANF HEKKIKEVYS GTFIANGKDL 

       190        200        210        220        230        240 
KRWLNQINNK NIKKEFYATD IVHFANLENS TIKTVQVLNC KEILGVNNKL QLSILEKIFR 

       250        260        270        280        290        300 
KKQVNDLLLS GVTLKDPNHF ILRGILKHGK NIEIDTGVIL EGNIILGNNI KIGVGSVIKN 

       310        320        330        340        350        360 
SFIDDQTEIK EYTIIENVKI GKKCIIGPFA HLRPKTVLDD QIHVGNFVEI KDSIIKKESK 

       370        380        390        400        410        420 
IKHLSYFGNS EIGSQVNIGA GSITCNYDGV NKFKTIIGDN VLIGANTKLI APIKITKNAT 

       430        440        450        460 
IAAGTTLTQD VNTPCLIYNN KEQKQKKNWK RPQKIIKKTD Q

Q8KA74 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