Reviewed, UniProtKB/Swiss-Prot P57139 (GLMU_BUCAI)

Names and origin

Protein names

Recommended name:
    Bifunctional protein glmU
Including the following 2 domains:
    1- Recommended name:
            UDP-N-acetylglucosamine pyrophosphorylase
              EC=2.7.7.23
        Alternative name(s):
            N-acetylglucosamine-1-phosphate uridyltransferase
    2- Recommended name:
            Glucosamine-1-phosphate N-acetyltransferase
              EC=2.3.1.157

Gene names

Name:	glmU
Ordered Locus Names:	BU027

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]

Taxonomic identifier

118099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	459 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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. 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. 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. Context: Lipopolysaccharide (LPS) biosynthesis; lipid A biosynthesis.
Subunit structure	Homotrimer By similarity.
Subcellular location	CytoplasmBy similarity.
Sequence similarities	In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family. In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Domain	Repeat
Ligand	Magnesium Metal-binding
Molecular function	Acyltransferase Nucleotidyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	UDP-N-acetylglucosamine diphosphorylase activity Inferred from electronic annotation. Source: HAMAP glucosamine-1-phosphate N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 459	459	Bifunctional protein glmU
Regions
	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 – 459	209	N-acetyltransferase By similarity
Sites
	Active site	363	1	Proton acceptor By similarity
	Metal binding	105	1	Magnesium By similarity
	Metal binding	227	1	Magnesium By similarity
	Binding site	76	1	Substrate By similarity
	Binding site	140	1	Substrate; via amide nitrogen By similarity
	Binding site	154	1	Substrate By similarity
	Binding site	387	1	Acetyl-CoA By similarity
	Binding site	405	1	Acetyl-CoA By similarity
	Binding site	423	1	Acetyl-CoA; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57139-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: C26CAFBD3852AAF4	FASTA	459	51,182
	10 20 30 40 50 60 MLTQEIIIVI LAAGKGTRMK SNHPKVLHFL GGKTILEHVI ETAQSIKPKK IILVYSDQKK 70 80 90 100 110 120 PVLSNIYNIP IQWIIQKKPQ GTGHAILLAI KKISDNTEIL VLYGDVPFIS PVSIKKLQKS 130 140 150 160 170 180 KKQSKISLLT AKVKNPNGYG RILRKKGKVI SIIEDQDASN EQKNIKEIYS GIFIAQSKDL 190 200 210 220 230 240 TRWLKKIDKK NEKQEFYATD IIALAHLEGS FIKTIEPLNY EEILGINNKL QLSNLEKIFQ 250 260 270 280 290 300 KKQINKLLIN GVTIKDPSHF IFRGTLQHGQ NVEIDTGVIL ENNVILGDDV KIGPGCIIRN 310 320 330 340 350 360 SSIDSNTNIQ AYTIIENSKI GKGCIIGPFA HLRSNTLLDR NVHIGNFVET KDTFIKNESK 370 380 390 400 410 420 VKHLSYLGNS EIGSKVNIGA GSITCNYDGA NKFKTIIGDN VLVGSNTQLI APIKIAKNTT 430 440 450 IAAGTTVTKD VNTPCLVYNT KEQKYKKNWM RSKKIIKKN

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tokyo 1998.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000003 Genomic DNA. Translation: BAB12754.1.
RefSeq	NP_239868.1.
3D structure databases
HSSP	HSSP built from PDB template 1HV9 based on UniProtKB P17114.
ModBase	Search...
Genome annotation databases
GeneID	1109535.
GenomeReviews	Gene locus BU027 in contig BA000003_GR.
KEGG	buc:BU027.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P57139.
Enzyme and pathway databases
BioCyc	BSP107806:BU027-MON.
Family and domain databases
HAMAP	MF_01631. [Tree]
InterPro	IPR001451. Hexapep_transf. IPR001228. ISPD_synthase. IPR005882. UDP_GlcNAc_PyrPase. [Graphical view]
Pfam	PF00132. Hexapep. 6 hits. PF01128. IspD. 1 hit. [Graphical view]
TIGRFAMs	TIGR01173. glmU. 1 hit.
PROSITE	PS00101. HEXAPEP_TRANSFERASES. 1 hit. [Graphical view]
ProDom	P57139. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

GLMU_BUCAI

Accession

Primary (citable) accession number: P57139

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	July 22, 2008
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)