Reviewed, UniProtKB/Swiss-Prot Q89B26 (GLMU_BUCBP)

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:	bbp_029

Organism

Buchnera aphidicola subsp. Baizongia pistaciae [Complete proteome] [HAMAP]

Taxonomic identifier

135842 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	448 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. HAMAP MF_01631 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-D-glucosamine. HAMAP MF_01631
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. HAMAP MF_01631 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. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. HAMAP MF_01631
Subunit structure	Homotrimer By similarity.
Subcellular location	Cytoplasm By 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	cell morphogenesis Inferred from electronic annotation. Source: HAMAP cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW isoprenoid biosynthetic process Inferred from electronic annotation. Source: InterPro lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: InterPro peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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	Feature identifier
Molecule processing
	Chain	1 – 448	448	Bifunctional protein glmU HAMAP MF_01631		PRO_0000068700
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 – 448	198	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	169	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)
	Q89B26-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: FDEE666538B7AB9B	FASTA	448	50,129
	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

References

[1]

"Reductive genome evolution in Buchnera aphidicola." 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. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016826 Genomic DNA. Translation: AAO26772.1.
RefSeq	NP_777667.1.
3D structure databases
HSSP	HSSP built from PDB template 1HV9 based on UniProtKB P17114.
ModBase	Search...
Genome annotation databases
GeneID	1058362.
GenomeReviews	Gene locus bbp_029 in contig AE016826_GR.
KEGG	bab:bbp029.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q89B26.
OMA	Q89B26. TRMKSKL.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_029-MON.
Family and domain databases
HAMAP	MF_01631. [Tree]
InterPro	IPR001451. Hexapep_transf. IPR018357. Hexapep_transf_CS. IPR001228. ISPD_synthase. IPR005882. UDP_GlcNAc_PyrPase. [Graphical view]
Pfam	PF00132. Hexapep. 7 hits. PF01128. IspD. 1 hit. [Graphical view]
TIGRFAMs	TIGR01173. glmU. 1 hit.
PROSITE	PS00101. HEXAPEP_TRANSFERASES. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMU_BUCBP

Accession

Primary (citable) accession number: Q89B26

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	June 1, 2003
Last modified:	June 16, 2009
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)