Bifunctional protein glmU - Bradyrhizobium japonicum

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Reviewed, UniProtKB/Swiss-Prot Q89LD7 (GLMU_BRAJA)

Last modified June 16, 2009. Version 40. 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:	bll4608

Organism

Bradyrhizobium japonicum [Complete proteome] [HAMAP]

Taxonomic identifier

375 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

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Protein attributes

Sequence length	451 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.

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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 cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW isoprenoid biosynthetic process Inferred from electronic annotation. Source: InterPro 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 – 451

451

Bifunctional protein glmU HAMAP MF_01631

PRO_0000233743

Regions

Region

1 – 232

232

Pyrophosphorylase By similarity

Region

11 – 14

Substrate binding By similarity

Region

83 – 84

Substrate binding By similarity

Region

233 – 253

Linker By similarity

Region

254 – 451

198

N-acetyltransferase By similarity

Sites

Active site

349

Proton acceptor By similarity

Metal binding

108

Magnesium By similarity

Metal binding

230

Magnesium By similarity

Binding site

Substrate By similarity

Binding site

144

Substrate By similarity

Binding site

158

Substrate By similarity

Binding site

173

Substrate By similarity

Binding site

373

Acetyl-CoA By similarity

Binding site

426

Acetyl-CoA By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q89LD7-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 352471823C117F71
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FASTA

451

47,462

        10         20         30         40         50         60 
MTARSSLTIV LAAGEGTRMR SHLPKVLHPV AHQTLLAHVL TAAPKGTGTS LAVVIGPDHQ 

        70         80         90        100        110        120 
AVADEARRIR PDAVTFVQAE RLGTAHAVLA AREAIARGVD DLLIAFGDTP LISAETFARL 

       130        140        150        160        170        180 
RAPLANGAAL AALGFRAADP AGYGRFIVEG DRLVAIREQA DASADERKID LCNAGVMAID 

       190        200        210        220        230        240 
GRRALAILDK IGNANSKGEY YLTDAVEIVR EQGWESVVIE TSEDEVRGIN TKAQLAEAES 

       250        260        270        280        290        300 
VMQARLRKAA MEAGVTLIAP ETVYLSADTV FGKDVTIEPF VVIGPGVSIA DGTVIHSFSH 

       310        320        330        340        350        360 
IVETTLGRNV SIGPYARLRP GTSLGDGARI GNFVETKAAT LEAGVKVNHL SYIGDATVGA 

       370        380        390        400        410        420 
NSNIGAGTIT CNYDGFKKHK TIIGQGAFVG TNSSLVAPVK IGNGAYIGSG SVITRDVPDD 

       430        440        450 
AMALERNQQT IREGGAARYR EMKTRGKKPE K

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References

[1]

"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed: 12597275] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: USDA 110.

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Cross-references

Sequence databases
	BA000040 Genomic DNA. Translation: BAC49873.1.
RefSeq	NP_771248.1.
3D structure databases
HSSP	HSSP built from PDB template 1G95 based on UniProtKB Q97R46.
ModBase	Search...
Genome annotation databases
GeneID	1052462.
GenomeReviews	Gene locus bll4608 in contig BA000040_GR.
KEGG	bja:bll4608.
NMPDR	fig\|224911.1.peg.4608.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q89LD7.
OMA	Q89LD7. MERTCLA.
Enzyme and pathway databases
BioCyc	BJAP224911:BLL4608-MON.
BRENDA	2.3.1.157. 280. 2.7.7.23. 280.
Family and domain databases
HAMAP	MF_01631. [Tree]
InterPro	IPR001451. Hexapep_transf. IPR018357. Hexapep_transf_CS. IPR001228. ISPD_synthase. IPR005882. UDP_GlcNAc_PyrPase. [Graphical view]
Pfam	PF00132. Hexapep. 7 hits. PF01128. IspD. 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_BRAJA

Accession

Primary (citable) accession number: Q89LD7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	June 1, 2003
Last modified:	June 16, 2009
This is version 40 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

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents