Skip Header

Contribute Send feedback
Read comments (?) or add your own

A1A1R9 (GLMU_BIFAA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BAD_0871
OrganismBifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) [Complete proteome] [HAMAP]
Taxonomic identifier367928 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length460 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 – 460460Bifunctional protein GlmU HAMAP MF_01631
PRO_1000056139

Regions

Region1 – 235235Pyrophosphorylase By similarity
Region9 – 124Substrate binding By similarity
Region81 – 822Substrate binding By similarity
Region236 – 25621Linker By similarity
Region257 – 460204N-acetyltransferase By similarity

Sites

Active site3681Proton acceptor By similarity
Metal binding1091Magnesium By similarity
Metal binding2331Magnesium By similarity
Binding site761Substrate By similarity
Binding site1461Substrate; via amide nitrogen By similarity
Binding site1611Substrate By similarity
Binding site1761Substrate By similarity
Binding site3921Acetyl-CoA By similarity
Binding site4281Acetyl-CoA; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A1A1R9 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: E243BA4B85253779

FASTA46048,981
        10         20         30         40         50         60 
MALSAAIILA AGEGTRMRSN KPKVLHTLAG KTFLNRVMDS VAALDPDTLA VVVHYQAERV 

        70         80         90        100        110        120 
AEAARSYNEH VTIVEQDDIP GTGRAVQCAM AQLTQKDDLD GAVLIAASDM PLLDTDTLDQ 

       130        140        150        160        170        180 
LLAFHEKSGN GATVLTTILD DPTGYGRIIR DSEGNVLRIV EQKDANSSEL AVREVNTSVY 

       190        200        210        220        230        240 
VFDAKLLAEA IANLKSNNAQ GEFYLTDALE AAKANGAVGA FAAPDPLSVE GVNDRVQLAA 

       250        260        270        280        290        300 
LAKAHNKRVC EHWMREGVTI LDPDTTWIED DVQIARDAVI LPGCFLQGHT VIGEAAEVGP 

       310        320        330        340        350        360 
YTTLIGATID AEAHVERSRV QETHIGRAAN IGPWTYLRPG NELGEGSKAG AFVEMKKAHI 

       370        380        390        400        410        420 
GNGTKVPHLS YVGDADLGEH TNIGGGTITA NYDGVHKHHT TIGSNVHVGA GNLFVAPVTV 

       430        440        450        460 
GDGVTTGAGS VVRHDVPSDS MVYSENTQHV VEGWKPEWER

« Hide

References

[1]"Bifidobacterium adolescentis complete genome sequence."
Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S., Tanaka K., Watanabe K.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15703 / DSM 20083 / NCTC 11814 / E194a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009256 Genomic DNA. Translation: BAF39652.1.
RefSeqYP_909734.1. NC_008618.1.

3D structure databases

ProteinModelPortalA1A1R9.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1A1R9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4557001.
GenomeReviewsGene locus BAD_0871 in contig AP009256_GR.
KEGGbad:BAD_0871.
NMPDRfig|1680.3.peg.1510.
PATRIC21101161. VBIBifAdo27973_0945.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHBG688195.
OMAGSKVNHL.
ProtClustDBPRK14352.

Family and domain databases

HAMAPMF_01631. GlmU.
[Tree]
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR011004. Trimer_LpxA-like.
[Graphical view]
KOK04042.
PANTHERPTHR22572:SF17. PTHR22572:SF17. 1 hit.
PfamPF00132. Hexapep. 3 hits.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. GlmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_BIFAA
AccessionPrimary (citable) accession number: A1A1R9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 40 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents