Bifunctional protein glmU - Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828)

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Reviewed, UniProtKB/Swiss-Prot A8FLN0 (GLMU_CAMJ8)

Last modified February 9, 2010. Version 22. History...

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

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

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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:	C8J_0768

Organism

Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828) [Complete proteome] [HAMAP]

Taxonomic identifier

407148 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

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Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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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.

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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...

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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_1000073645

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

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Sequences

Sequence

Length

Mass (Da)

Tools

A8FLN0-1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 7C83EAFD1FCFCF70
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FASTA

429

48,145

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

        70         80         90        100        110        120 
EILEYFPKTQ ILEQDLQNYP GTAGALRGFE PKNERVLILC GDMPLVEQTS LEALLSNNAK 

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

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

       250        260        270        280        290        300 
WMQQGVIFHL PQSTFIGTDV EFMGECEVYE 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 SVNVEKGALF INRAEHKMIK 


DYYYKKFQK

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References

[1]	"The complete genome sequence of Campylobacter jejuni strain 81116 (NCTC11828)." Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M., van Vliet A.H.M. J. Bacteriol. 189:8402-8403(2007) [PubMed: 17873037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000814 Genomic DNA. Translation: ABV52367.1.
RefSeq	YP_001482344.1.
3D structure databases
SMR	A8FLN0. Positions 5-417.
ModBase	Search...
Protein-protein interaction databases
STRING	A8FLN0.
Genome annotation databases
GeneID	5618086.
GenomeReviews	Gene locus C8J_0768 in contig CP000814_GR.
KEGG	cju:C8J_0768.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1207.
HOGENOM	HBG688195.
OMA	GSKVNHL.
Family and domain databases
HAMAP	MF_01631. GlmU. [Tree]
InterPro	IPR005882. Bifunctional_GlmU. 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. False negative. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

GLMU_CAMJ8

Accession

Primary (citable) accession number: A8FLN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	November 13, 2007
Last modified:	February 9, 2010
This is version 22 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)

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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

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

Family and domain databases

Entry information

Relevant documents