Reviewed, UniProtKB/Swiss-Prot Q8YC48 (GLMU_BRUME)

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:	BMEII0684

Organism

Brucella melitensis [Complete proteome] [HAMAP]

Taxonomic identifier

29459 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
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. HAMAP MF_01631
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. HAMAP MF_01631
Pathway	Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. HAMAP MF_01631 Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-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 HAMAP MF_01631.
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 cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW 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 – 454	454	Bifunctional protein glmU HAMAP MF_01631		PRO_0000233745
Regions
	Region	1 – 232	232	Pyrophosphorylase By similarity
	Region	11 – 14	4	Substrate binding By similarity
	Region	83 – 84	2	Substrate binding By similarity
	Region	233 – 253	21	Linker By similarity
	Region	254 – 454	201	N-acetyltransferase By similarity
Sites
	Active site	349	1	Proton acceptor By similarity
	Metal binding	108	1	Magnesium By similarity
	Metal binding	230	1	Magnesium By similarity
	Binding site	78	1	Substrate By similarity
	Binding site	144	1	Substrate By similarity
	Binding site	158	1	Substrate By similarity
	Binding site	173	1	Substrate By similarity
	Binding site	373	1	Acetyl-CoA By similarity
	Binding site	391	1	Acetyl-CoA By similarity
	Binding site	426	1	Acetyl-CoA By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8YC48-1 [UniParc]. Last modified May 2, 2006. Version 2. Checksum: 0D9A7E45C22E2A05	FASTA	454	47,905
	10 20 30 40 50 60 MTDRTCLSIV LAAGEGTRMK SNLPKVLHRV AGLPLVCHVV NAVRGTGKSD VALVVGRGAE 70 80 90 100 110 120 DVRSAVEKIA GPVSAFEQKE RLGTAHAVLA AREAIARGYD DLLIVFGDTP LIEAQSLLAA 130 140 150 160 170 180 RERLAQGADL VVIGFRPASP HGYGRLIEEG GQLVAIIEEK EATDEQKKIG FCNGGLMALR 190 200 210 220 230 240 GQHALALLDA VGNDNAKGEY YLTDIVAIAH GKGLNVTAIE VPVDNVIGIN NRAELAEAET 250 260 270 280 290 300 IWQNRKRREL MLSGVTLIAP ETVFFSYDTV IEPDVVIEPN VFFGPSVHVA SGALIHSFSH 310 320 330 340 350 360 LEGAQVGEKA EIGPFARLRP GADLAEKSKV GNFCEVKNAK VGKGAKINHL AYIGDAVIGA 370 380 390 400 410 420 SSNIGAGTIT CNYDGYNKFK TIIGDNAFIG SNSSLVAPVE IGDNAYIASG SVITADVPAD 430 440 450 ALALGRARQE TKEGRAKILR EKYAAIKAAK SVSK

References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R. Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed: 11756688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094 / Biotype 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008918 Genomic DNA. Translation: AAL53926.1. Different initiation.
PIR	AC3595.
RefSeq	NP_541662.1.
3D structure databases
SMR	Q8YC48. Positions 7-438.
ModBase	Search...
Genome annotation databases
GeneID	1198456.
GenomeReviews	Gene locus BMEII0684 in contig AE008918_GR.
KEGG	bme:BMEII0684.
NMPDR	fig|224914.1.peg.2744.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG688195.
OMA	MERTCLA.
PhylomeDB	Q8YC48.
Enzyme and pathway databases
BioCyc	BMEL224914:BMEII0684-MONOMER.
BRENDA	2.3.1.157. 277959. 2.7.7.23. 277959.
Family and domain databases
HAMAP	MF_01631. GlmU. [Tree]
InterPro	IPR005882. Bifunctional_GlmU. IPR018357. Hexapep_transf_CS. IPR005835. NTP_transferase. IPR011004. Trimer_LpxA-like. [Graphical view]
Pfam	PF00483. NTP_transferase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01173. glmU. 1 hit.
PROSITE	PS00101. HEXAPEP_TRANSFERASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMU_BRUME

Accession

Primary (citable) accession number: Q8YC48

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	May 2, 2006
Last modified:	February 9, 2010
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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