Bifunctional protein glmU - Bordetella avium (strain 197N)

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Reviewed, UniProtKB/Swiss-Prot Q2KTX5 (GLMU_BORA1)

Last modified February 9, 2010. Version 31. 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:	BAV3275

Organism

Bordetella avium (strain 197N) [Complete proteome] [HAMAP]

Taxonomic identifier

360910 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

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Protein attributes

Sequence length	457 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 – 457

457

Bifunctional protein glmU HAMAP MF_01631

PRO_0000244289

Regions

Region

1 – 230

230

Pyrophosphorylase By similarity

Region

7 – 10

Substrate binding By similarity

Region

78 – 79

Substrate binding By similarity

Region

231 – 251

Linker By similarity

Region

252 – 457

206

N-acetyltransferase By similarity

Sites

Active site

364

Proton acceptor By similarity

Metal binding

106

Magnesium By similarity

Metal binding

228

Magnesium By similarity

Binding site

Substrate By similarity

Binding site

140

Substrate; via amide nitrogen By similarity

Binding site

155

Substrate By similarity

Binding site

170

Substrate By similarity

Binding site

388

Acetyl-CoA By similarity

Binding site

406

Acetyl-CoA By similarity

Binding site

424

Acetyl-CoA; via amide nitrogen By similarity

Binding site

441

Acetyl-CoA By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q2KTX5-1 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 6A8CF3D958880450
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FASTA

457

48,762

        10         20         30         40         50         60 
MLNVVILAAG LGKRMQSDLP KVLHTLAGQP MLGHVLESAR DLQPGRIVVV VGHGAERVEA 

        70         80         90        100        110        120 
AYAGQAGLSF ALQRPQHGTG HAVQQAVPQL MEGDGAEDAT LVLYGDVPLV QPETLRRLMA 

       130        140        150        160        170        180 
ARGQGVAVLT EVLPDATGYG RIVRDAQGQV TRIVEHKDAN EQERAIKEVN TGILVAPTAK 

       190        200        210        220        230        240 
LKDWLTRIDN NNAQGEYYLT DIIALAVADG VTVSAAQPAA SWETLGVNSR AQQAELERRW 

       250        260        270        280        290        300 
QAELARRQLE AGVTLADPAR FDQRGTLECG RDVYIDVGCV FEGRVKLGDG VRVGPHCVLR 

       310        320        330        340        350        360 
DVEVGAGTQI EAYSHLQQAR VGDEARVGPY ARLRPGADLG NQAHVGNFVE IKNAVLGEAS 

       370        380        390        400        410        420 
KANHLAYIGD ADIGARVNVG AGTITCNYDG VNKHRTIIED DAFIGSDTQL VAPVRVGRGA 

       430        440        450 
TLAAGTTLTR DAPADSLTLS RIRQSTVPGW KRPVKKS

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References

[1]

"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AM167904 Genomic DNA. Translation: CAJ50885.1.
RefSeq	YP_787770.1.
3D structure databases
SMR	Q2KTX5. Positions 2-452.
ModBase	Search...
Genome annotation databases
GeneID	6266479.
GenomeReviews	Gene locus BAV3275 in contig AM167904_GR.
KEGG	bav:BAV3275.
NMPDR	fig\|521.1.peg.1982.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG688195.
OMA	GSKVNHL.
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...

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Entry information

Entry name

GLMU_BORA1

Accession

Primary (citable) accession number: Q2KTX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	March 7, 2006
Last modified:	February 9, 2010
This is version 31 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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents