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Q5PBV0 (GLMU_ANAMM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:AM058
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length428 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 – 428428Bifunctional protein GlmU HAMAP MF_01631
PRO_0000233723

Regions

Region1 – 221221Pyrophosphorylase By similarity
Region6 – 94Substrate binding By similarity
Region79 – 802Substrate binding By similarity
Region222 – 24221Linker By similarity
Region243 – 428186N-acetyltransferase By similarity

Sites

Active site3381Proton acceptor By similarity
Metal binding1051Magnesium By similarity
Metal binding2191Magnesium By similarity
Binding site741Substrate By similarity
Binding site1401Substrate; via amide nitrogen By similarity
Binding site3621Acetyl-CoA By similarity
Binding site3981Acetyl-CoA; via amide nitrogen By similarity
Binding site4151Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PBV0 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 6973CB6AC2326801

FASTA42845,168
        10         20         30         40         50         60 
MDIVILAAGC GSRMCSTTPK ILHKLGNAPI IKHVLQLADE LRPKRAVIVT NAAVNGPVAA 

        70         80         90        100        110        120 
LAGEHNLRLN TVLQGEIAGT GGAATSALQA LKNPSEEIVL ILYGDTPLLD KATVCHALDR 

       130        140        150        160        170        180 
LSSGAKIVLV AFKSENNQYG RIVLGSSGNV LEVSHGRDTN GLAVSGAIAG YRQVISGLLG 

       190        200        210        220        230        240 
GLSCRDGELY LTDIVQSAAE KNVEVGYVIA DERKAMGINT RADLAIAESY FQCMKRASFL 

       250        260        270        280        290        300 
QSGVTLTSPD QVFFSIDTQI AQDVIVHPYV VFGAGVAVEP GAEILSYSHL EFCHIKKGAI 

       310        320        330        340        350        360 
VGPFARVRGN STIDRGCVVG NFVEIKESSL GEMSKVKHLS YLGNSTIGKN TNVGAGTVIC 

       370        380        390        400        410        420 
NYDGRNKQHS DIGNNCFVGA NSTIVSPIKV GDNAAIAAGS VITEDLPPRS LGIARSRQTT 


KPEYKTRR

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References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: St. Maries.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000030 Genomic DNA. Translation: AAV86229.1.
RefSeqYP_153484.1. NC_004842.2.

3D structure databases

ProteinModelPortalQ5PBV0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5PBV0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3171039.
GenomeReviewsGene locus AM058 in contig CP000030_GR.
KEGGama:AM058.
PATRIC20946231. VBIAnaMar46146_0055.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHBG688195.
OMAMERTCLA.
ProtClustDBCLSK2463660.

Enzyme and pathway databases

BioCycAMAR234826:AM058-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]
KOK04042.
PANTHERPTHR22572:SF17. PTHR22572:SF17. 1 hit.
PfamPF00132. Hexapep. 4 hits.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_ANAMM
AccessionPrimary (citable) accession number: Q5PBV0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 50 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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