Bifunctional protein glmU - Campylobacter jejuni

Contribute

Send feedback

Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9PPA2 (GLMU_CAMJE)

Last modified June 16, 2009. Version 53. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

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:	Cj0821

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Hide | Top

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

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.

Hide | Top

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 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 protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct	Notes
fliG	Q0PBJ0	1	EBI-1194402,EBI-1191336

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 429

429

Bifunctional protein glmU HAMAP MF_01631

PRO_0000233751

Regions

Region

1 – 223

223

Pyrophosphorylase By similarity

Region

8 – 11

Substrate binding By similarity

Region

81 – 82

Substrate binding By similarity

Region

224 – 244

Linker By similarity

Region

245 – 429

185

N-acetyltransferase By similarity

Sites

Active site

336

Proton acceptor By similarity

Metal binding

102

Magnesium By similarity

Metal binding

221

Magnesium By similarity

Binding site

135

Substrate; via amide nitrogen By similarity

Binding site

149

Substrate By similarity

Binding site

164

Substrate By similarity

Binding site

360

Acetyl-CoA By similarity

Binding site

378

Acetyl-CoA By similarity

Binding site

396

Acetyl-CoA; via amide nitrogen By similarity

Binding site

413

Acetyl-CoA By similarity

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q9PPA2-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 914CFD5EA6281BFF
Show »

FASTA

429

47,906

        10         20         30         40         50         60 
MKTSILILAA GLGTRIKSQK PKVLQELCQK SMILHILKKA FALSDDVSVV LSHQKERVEK 

        70         80         90        100        110        120 
EILEYFPKTQ ILEQDLQNYP GTAGALSGFE PKNERVLILC GDMPLVEQTS LEALLGNNAK 

       130        140        150        160        170        180 
LNLAVFKARD PKSYGRVVIK NDSVEKIVEF KDANTQEKEI NTCNAGVYVI DSRLLKELLP 

       190        200        210        220        230        240 
LIDNNNAAKE YYLTDIVKLA KEKDVMIKAV FVDEDEFMGI NDKFELSIAE NFMQKKIKKY 

       250        260        270        280        290        300 
WMQQGVIFHL PQSTFIGADV EFVGECEVYE NVRIEGKSKI INSIIKSSSV IENSIVENSD 

       310        320        330        340        350        360 
VGPLAHLRPN CELKNTHIGN FVECKNAKLN TVKAGHLSYL GDCEIDSGTN IGCGTITCNY 

       370        380        390        400        410        420 
DGVKKHKTII GKNVFVGSDT QFIAPVKIED EVIIAAGSTV SINVEKGALF INRAGHKMIK 


DYYYKKFQK

« Hide

Hide | Top

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M.

Barrell B.G.
Nature 403:665-668(2000) [PubMed: 10688204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168 / Serotype O:2.

Hide | Top

Cross-references

Sequence databases
	AL111168 Genomic DNA. Translation: CAL34949.1.
PIR	E81354.
RefSeq	YP_002344228.1.
3D structure databases
HSSP	HSSP built from PDB template 1HM0 based on UniProtKB Q97R46.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PPA2. 28 interactions.
Genome annotation databases
GeneID	905125.
GenomeReviews	Gene locus Cj0821 in contig AL111168_GR.
KEGG	cje:Cj0821.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	Q9PPA2. TRMKSKL.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ0821-MON.
BRENDA	2.3.1.157. 255835. 2.7.7.23. 255835.
Family and domain databases
HAMAP	MF_01631. [Tree]
InterPro	IPR001451. Hexapep_transf. IPR018357. Hexapep_transf_CS. IPR005882. UDP_GlcNAc_PyrPase. [Graphical view]
Pfam	PF00132. Hexapep. 4 hits. [Graphical view]
TIGRFAMs	TIGR01173. glmU. 1 hit.
PROSITE	PS00101. HEXAPEP_TRANSFERASES. False negative. [Graphical view]
ProtoNet	Search...

Hide | Top

Entry information

Entry name

GLMU_CAMJE

Accession

Primary (citable) accession number: Q9PPA2
Secondary accession number(s): Q0PA69

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 53 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)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents