Bifunctional protein GlmU - Ralstonia solanacearum (strain GMI1000)

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Q8Y304 (GLMU_RALSO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. 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:	RSc0177
ORF Names:	RS01048

Organism

Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum) [Complete proteome] [HAMAP]

Taxonomic identifier

267608 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Ralstonia ›

Protein attributes

Sequence length	455 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-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain By similarity. HAMAP-Rule MF_01631
Catalytic activity	Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. HAMAP-Rule MF_01631 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. HAMAP-Rule MF_01631
Cofactor	Binds 1 magnesium ion per subunit By similarity.
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-Rule 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-Rule MF_01631
Subunit structure	Homotrimer By similarity.
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.

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	UDP-N-acetylglucosamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway cell morphogenesis Inferred from electronic annotation. Source: HAMAP lipid A biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 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...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 455

455

Bifunctional protein GlmU HAMAP-Rule MF_01631

PRO_0000233830

Regions

Region

1 – 225

225

Pyrophosphorylase By similarity

Region

6 – 9

UDP-GlcNAc binding By similarity

Region

76 – 77

UDP-GlcNAc binding By similarity

Region

98 – 100

UDP-GlcNAc binding By similarity

Region

226 – 246

Linker By similarity

Region

247 – 455

209

N-acetyltransferase By similarity

Region

382 – 383

Acetyl-CoA binding By similarity

Sites

Active site

359

Proton acceptor By similarity

Metal binding

100

Magnesium By similarity

Metal binding

223

Magnesium By similarity

Binding site

UDP-GlcNAc By similarity

Binding site

UDP-GlcNAc By similarity

Binding site

135

UDP-GlcNAc; via amide nitrogen By similarity

Binding site

150

UDP-GlcNAc By similarity

Binding site

165

UDP-GlcNAc By similarity

Binding site

223

UDP-GlcNAc By similarity

Binding site

329

Acetyl-CoA; amide nitrogen By similarity

Binding site

347

Acetyl-CoA By similarity

Binding site

362

Acetyl-CoA By similarity

Binding site

373

Acetyl-CoA By similarity

Binding site

401

Acetyl-CoA By similarity

Binding site

419

Acetyl-CoA; via amide nitrogen By similarity

Binding site

436

Acetyl-CoA By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8Y304 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: D7A3647EA8320BD4
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FASTA

455

48,670

        10         20         30         40         50         60 
MNIVILAAGL GKRMRSALPK VLHPLAGKPL LAHVIETARS LSPTRLVVVV GHGGDRVRDM 

        70         80         90        100        110        120 
VGAPDVTFAT QDQQLGTGHA VMQALDQLDD TVPTLVLYGD VPLTRAETLN ALVGAAGQDH 

       130        140        150        160        170        180 
LGVLTVHLDD PTGYGRIVRD ATGRITRIVE QKDANETQLA IHEVNTGILV CPTARLKTWL 

       190        200        210        220        230        240 
ATLRNDNAQG EYYLTDVIER AASEGLPITS AHPLAEWETL GVNSKVQLAE LERIHQRNLA 

       250        260        270        280        290        300 
QQLLEDGVTL IDPARIDIRG RLTCGRDVVI DIDCIFEGNV TLGDGVRIGA HAVIRDAAIQ 

       310        320        330        340        350        360 
AGAEILPFCH IEQATVGAQS RIGPYARLRP GTELAEDVHI GNFVEVKNSQ IAAHSKANHL 

       370        380        390        400        410        420 
AYVGDATVGS RVNIGAGTIT CNYDGANKFR TIIEDDAFIG SDTQLVAPVR VGRGATLGAG 

       430        440        450 
TTLTKDAPEG QLTVSRARQT TVNGWQRPVK QKKDA

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References

[1]

"Genome sequence of the plant pathogen Ralstonia solanacearum."
Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M., Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M., Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M., Moisan A.

Boucher C.A.
Nature 415:497-502(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GMI1000.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL646052 Genomic DNA. Translation: CAD13705.1.
RefSeq	NP_518298.1. NC_003295.1.
3D structure databases
ProteinModelPortal	Q8Y304.
SMR	Q8Y304. Positions 1-447.
ModBase	Search...
Protein-protein interaction databases
STRING	267608.RSc0177.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAD13705; CAD13705; RSc0177.
GeneID	1218980.
KEGG	rso:RSc0177.
PATRIC	20258893. VBIRalSol70888_0181.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1207.
HOGENOM	HOG000283476.
KO	K04042.
OMA	EPQTHLR.
ProtClustDB	CLSK896503.
Enzyme and pathway databases
UniPathway	UPA00113; UER00532. UPA00113; UER00533. UPA00973.
Family and domain databases
HAMAP	MF_01631. GlmU.
InterPro	IPR005882. Bifunctional_GlmU. IPR001451. Hexapep_transf. IPR025877. MobA-like_NTP_Trfase_dom. IPR011004. Trimer_LpxA-like. [Graphical view]
PANTHER	PTHR22572:SF17. PTHR22572:SF17. 1 hit.
Pfam	PF00132. Hexapep. 3 hits. PF12804. NTP_transf_3. 1 hit. [Graphical view]
SUPFAM	SSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMs	TIGR01173. glmU. 1 hit.
PROSITE	PS00101. HEXAPEP_TRANSFERASES. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMU_RALSO

Accession

Primary (citable) accession number: Q8Y304

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 71 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

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents