Bifunctional protein GlmU - Bordetella pertussis

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Q7VT27 (GLMU_BORPE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. History...

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

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Bifunctional protein GlmU

Including the following 2 domains:

UDP-N-acetylglucosamine pyrophosphorylase
EC=2.7.7.23
Alternative name(s):
N-acetylglucosamine-1-phosphate uridyltransferase
Glucosamine-1-phosphate N-acetyltransferase
EC=2.3.1.157

Gene names

Name:	glmU
Ordered Locus Names:	BP3730

Organism

Bordetella pertussis

Taxonomic identifier

520 [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 Reference proteome
Gene Ontology (GO)
Biological process	cell morphogenesis Inferred from electronic annotation. Source: InterPro 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: UniProtKB-KW 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: EC glucosamine-1-phosphate N-acetyltransferase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: InterPro
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_0000233742

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

Sequences

Sequence

Length

Mass (Da)

Tools

Q7VT27 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: FD2B6BECD5A7C66D
Show »

FASTA

457

48,400

        10         20         30         40         50         60 
MLNVVILAAG LGKRMQSDLP KVLHTLAGRP MLDHVIGSAR QLQPARIIVV VGHGADRVKA 

        70         80         90        100        110        120 
AFEGQPGLQF 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

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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.

Maskell D.J.
Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640422 Genomic DNA. Translation: CAE43987.1.
RefSeq	NP_882233.1. NC_002929.2.
3D structure databases
ProteinModelPortal	Q7VT27.
SMR	Q7VT27. Positions 2-452.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2665001.
GenomeReviews	Gene locus BP3730 in contig BX470248_GR.
KEGG	bpe:BP3730.
NMPDR	fig\|257313.1.peg.3303.
PATRIC	21161138. VBIBorPer7866_4033.
Phylogenomic databases
HOGENOM	HBG688195.
OMA	GSKVNHL.
PhylomeDB	Q7VT27.
ProtClustDB	CLSK921175.
Enzyme and pathway databases
BioCyc	BPER257313:BP3730-MONOMER.
Family and domain databases
HAMAP	MF_01631. GlmU. [Tree]
InterPro	IPR005882. Bifunctional_GlmU. IPR001451. Hexapep_transf. IPR018357. Hexapep_transf_CS. IPR011004. Trimer_LpxA-like. [Graphical view]
KO	K04042.
PANTHER	PTHR22572:SF17. PTHR22572:SF17. 1 hit.
Pfam	PF00132. Hexapep. 3 hits. [Graphical view]
SUPFAM	SSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMs	TIGR01173. GlmU. 1 hit.
PROSITE	PS00101. HEXAPEP_TRANSFERASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMU_BORPE

Accession

Primary (citable) accession number: Q7VT27

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents