Reviewed, UniProtKB/Swiss-Prot Q7W321 (GLMU_BORPA)

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:	BPP4229

Organism

Bordetella parapertussis [Complete proteome] [HAMAP]

Taxonomic identifier

519 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	457 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 – 457	457	Bifunctional protein glmU HAMAP MF_01631		PRO_0000233741
Regions
	Region	1 – 230	230	Pyrophosphorylase By similarity
	Region	7 – 10	4	Substrate binding By similarity
	Region	78 – 79	2	Substrate binding By similarity
	Region	231 – 251	21	Linker By similarity
	Region	252 – 457	206	N-acetyltransferase By similarity
Sites
	Active site	364	1	Proton acceptor By similarity
	Metal binding	106	1	Magnesium By similarity
	Metal binding	228	1	Magnesium By similarity
	Binding site	73	1	Substrate By similarity
	Binding site	140	1	Substrate; via amide nitrogen By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	170	1	Substrate By similarity
	Binding site	388	1	Acetyl-CoA By similarity
	Binding site	406	1	Acetyl-CoA By similarity
	Binding site	424	1	Acetyl-CoA; via amide nitrogen By similarity
	Binding site	441	1	Acetyl-CoA By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7W321-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 6D1797EFE35F0266	FASTA	457	48,385
	10 20 30 40 50 60 MLNVVILAAG LGKRMQSDLP KVLHTLAGRP MLDHVIGSAR QLQPARIIVV VGHGADRVKA 70 80 90 100 110 120 AFEGLPGLQF ALQQPQHGTG HAVQQAVPQL LEGDGEDDVT LVLYGDVPLV QPATLQNLLQ 130 140 150 160 170 180 ARGRGVAVLT EVLADSTGYG RIVRDAQGQV CRIVEHKDAS EAERAIKEVN TGILAAPTAR 190 200 210 220 230 240 LKDWLGRITN DNAQGEYYLT DVIGLAVGDG VPVGAAQPGA SWETLGVNSR VQQAQLERAW 250 260 270 280 290 300 QSELARRQLE AGVTLADPAR FDVRGTLSCG RDVFIDVGCV FEGTVTLGDG VRVGPHCVLR 310 320 330 340 350 360 DVAVQAGARI EAYSHLQQAK VGQEAVVGPY ARLRPGADLG ERSHVGNFVE IKNSVLQADS 370 380 390 400 410 420 KANHLAYIGD ADIGARVNVG AGTITCNYDG VNKHRTVIED DAFIGSDTQL VAPVRVGKGA 430 440 450 TLGAGTTLTK DAPAGQLTIS RARQSTIEGW KRPVKKS

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640436 Genomic DNA. Translation: CAE39508.1.
RefSeq	NP_886358.1.
3D structure databases
SMR	Q7W321. Positions 2-452.
ModBase	Search...
Genome annotation databases
GeneID	1664998.
KEGG	bpa:BPP4229.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG688195.
OMA	GSKVNHL.
PhylomeDB	Q7W321.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP4229-MONOMER.
BRENDA	2.3.1.157. 263123. 2.7.7.23. 263123.
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_BORPA

Accession

Primary (citable) accession number: Q7W321

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
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)