Reviewed, UniProtKB/Swiss-Prot P28017 (GLMU_BACME)

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
Synonyms:	gcaD, tms

Organism

Bacillus megaterium

Taxonomic identifier

1404 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	68 AA.
Sequence status	Fragment.
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
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	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 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 – ›68	›68	Bifunctional protein glmU HAMAP MF_01631		PRO_0000068707
Experimental info
	Non-terminal residue	68	1

Sequences

	Sequence		Length	Mass (Da)
	P28017-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: CD40139522E5A130	FASTA	68	7,399
	10 20 30 40 50 60 MSKRYAVILA AGQGTRMKSS LYKVLHPVCG KPMVQHVIDQ LSRLDLTNLI TVVGHGAEKV KSHVGDKS

References

[1]	"spoVG sequence of Bacillus megaterium and Bacillus subtilis." Hudspeth D.S.S., Vary P.S. Biochim. Biophys. Acta 1130:229-231(1992) [PubMed: 1373326] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PV361.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X62377 Genomic DNA. Translation: CAA44241.1.
PIR	S18901.
3D structure databases
HSSP	HSSP built from PDB template 1HV9 based on UniProtKB P17114.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.3.1.157. 325. 2.7.7.23. 325.
Family and domain databases
HAMAP	MF_01631. [Tree]
InterPro	IPR018357. Hexapep_transf_CS. [Graphical view]
PROSITE	PS00101. HEXAPEP_TRANSFERASES. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMU_BACME

Accession

Primary (citable) accession number: P28017

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 42 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)