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A9IVJ6 (GLMU_BART1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional protein GlmU

Including the following 2 domains:

  1. UDP-N-acetylglucosamine pyrophosphorylase
    EC=2.7.7.23
    Alternative name(s):
    N-acetylglucosamine-1-phosphate uridyltransferase
  2. Glucosamine-1-phosphate N-acetyltransferase
    EC=2.3.1.157
Gene names
Name:glmU
Ordered Locus Names:BT_1367
OrganismBartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]
Taxonomic identifier382640 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454Bifunctional protein GlmU HAMAP MF_01631
PRO_0000337710

Regions

Region1 – 231231Pyrophosphorylase By similarity
Region82 – 832Substrate binding By similarity
Region232 – 25221Linker By similarity
Region253 – 454202N-acetyltransferase By similarity

Sites

Active site3481Proton acceptor By similarity
Metal binding1071Magnesium By similarity
Metal binding2291Magnesium By similarity
Binding site771Substrate By similarity
Binding site1431Substrate; via amide nitrogen By similarity
Binding site1571Substrate By similarity
Binding site1721Substrate By similarity
Binding site3721Acetyl-CoA By similarity
Binding site3901Acetyl-CoA By similarity
Binding site4081Acetyl-CoA; via amide nitrogen By similarity
Binding site4251Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
A9IVJ6 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 6159609382103339

FASTA45449,347
        10         20         30         40         50         60 
MVRSCLSIVL SAGEGTRMKS PLPKVLHKIA GLPLICHVLK QIELAESSQV AVVVGCGGQE 

        70         80         90        100        110        120 
VTHVVQSFVK DVMIFEQKER LGTAHAVLSA RFALQKGVDD ILIVFGDTPL IQQESLHQMR 

       130        140        150        160        170        180 
AQLADGADVV FAGFHTQDPT GYGRLLEKNG QLIAIVEEKD ASEEEKKISF CNGGILAMRG 

       190        200        210        220        230        240 
KHALSLLEKV DNNNMKKEYY LTDIASLASR EGLDVRVVEV PFENIVGINN CLELSRADSL 

       250        260        270        280        290        300 
WQKRKARDLM LSGVTLLKPE TVYFSYDTEI EPGVVIEPNV YFGLGVKVQS GAVIRAFSYL 

       310        320        330        340        350        360 
EGAVVGQDAQ IGPYARLRPG TELAKSVKVG NFCEVKQAKV GESSKINHLS YIGDAEIGAH 

       370        380        390        400        410        420 
TNIGAGTITC NYDGFNKYKT VIGDHAFVGS NTALVSPLVI GDGSYVASGS VITENIPMNS 

       430        440        450 
MAFGRARQVI KEGYATKFRA RLLEKNLSEN KQKK

« Hide

References

[1]"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
Nat. Genet. 39:1469-1476(2007) [PubMed: 18037886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIP 105476 / IBS 506.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM260525 Genomic DNA. Translation: CAK01729.1.
RefSeqYP_001609724.1. NC_010161.1.

3D structure databases

ProteinModelPortalA9IVJ6.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9IVJ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5829022.
GenomeReviewsGene locus BT_1367 in contig AM260525_GR.
PATRIC20550535. VBIBarTri113218_1409.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG688195.
OMAGSKVNHL.
ProtClustDBPRK14353.

Enzyme and pathway databases

BioCycBTRI382640:BT_1367-MONOMER.

Family and domain databases

HAMAPMF_01631. GlmU.
[Tree]
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PANTHERPTHR22572:SF17. PTHR22572:SF17. 1 hit.
PfamPF00132. Hexapep. 4 hits.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. GlmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_BART1
AccessionPrimary (citable) accession number: A9IVJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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