Reviewed, UniProtKB/Swiss-Prot Q8KA74 (GLMU_BUCAP)

Names and origin

Protein names

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

Gene names

Name:	glmU
Ordered Locus Names:	BUsg_028

Organism

Buchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]

Taxonomic identifier

98794 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	461 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 – 461	461	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 – 461	211	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	423	1	Acetyl-CoA; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8KA74-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 6D38A10B70780C10	FASTA	461	51,735
	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

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." 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. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013218 Genomic DNA. Translation: AAM67599.1.
RefSeq	NP_660388.1.
3D structure databases
HSSP	HSSP built from PDB template 1HV9 based on UniProtKB P17114.
ModBase	Search...
Genome annotation databases
GeneID	1005844.
GenomeReviews	Gene locus BUsg_028 in contig AE013218_GR.
KEGG	bas:BUsg028.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8KA74.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG028-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. 5 hits. PF01128. IspD. 1 hit. [Graphical view]
TIGRFAMs	TIGR01173. glmU. 1 hit.
PROSITE	PS00101. HEXAPEP_TRANSFERASES. False negative. [Graphical view]
ProDom	Q8KA74. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

GLMU_BUCAP

Accession

Primary (citable) accession number: Q8KA74

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	July 22, 2008
This is version 44 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)