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Q8G5P1 (GLMU_BIFLO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 71. 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:BL0964
OrganismBifidobacterium longum (strain NCC 2705) [Reference proteome] [HAMAP]
Taxonomic identifier206672 [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-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. HAMAP-Rule 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-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. HAMAP-Rule MF_01631

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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-Rule MF_01631
PRO_0000233737

Regions

Region1 – 235235Pyrophosphorylase By similarity
Region9 – 124UDP-GlcNAc binding By similarity
Region81 – 822UDP-GlcNAc binding By similarity
Region236 – 25621Linker By similarity
Region257 – 460204N-acetyltransferase By similarity
Region391 – 3922Acetyl-CoA binding By similarity

Sites

Active site3681Proton acceptor By similarity
Metal binding1091Magnesium By similarity
Metal binding2331Magnesium By similarity
Binding site231UDP-GlcNAc By similarity
Binding site761UDP-GlcNAc By similarity
Binding site1461UDP-GlcNAc; via amide nitrogen By similarity
Binding site1611UDP-GlcNAc By similarity
Binding site1761UDP-GlcNAc By similarity
Binding site2331UDP-GlcNAc By similarity
Binding site3381Acetyl-CoA; amide nitrogen By similarity
Binding site3561Acetyl-CoA By similarity
Binding site3711Acetyl-CoA By similarity
Binding site3821Acetyl-CoA By similarity
Binding site4281Acetyl-CoA; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8G5P1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 080C4F98C0BA2B6F

FASTA46049,094
        10         20         30         40         50         60 
MALSAAIVLA AGEGTRMRSN KPKVLHAFAG KTFLNRVMDS VAALNPDTLA VVVHFQAERV 

        70         80         90        100        110        120 
AEAARSYDEQ VTIVNQDDIP GTGRAVQCAM AQLTEAGKVD GPVLIAASDM PLLDSETLHR 

       130        140        150        160        170        180 
LVEFHTASGN GATVLTTILD DPTGYGRIIR DREGNVLRIV EQKDANRSEL AVQEVNTSVY 

       190        200        210        220        230        240 
VFEASVLTEA IAGLKSNNAQ GEFYLTDALE TAKAAGKVGA FAAPDPLTVE GVNDRVQLAA 

       250        260        270        280        290        300 
LSKTYNRRVC ERWMRDGVTI LDPETTWIED DVQIGRDATI LPGSFLQGHT VVGEDAIVGP 

       310        320        330        340        350        360 
YTTLIDATVD EGAVVERSRV QESHIGARTN IGPWTYLRPG NEFGEDAKAG AFVEMKKAHI 

       370        380        390        400        410        420 
GNGTKVPHLS YVGDAQLGDH TNIGGGTITA NYDGVHKNRT TIGSGCHVGA GNLFVAPVEV 

       430        440        450        460 
GDNVTTGAGS VVRHAVPSDT MVYSENTQHN VEGWKPAWER

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References

[1]"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCC 2705.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014295 Genomic DNA. Translation: AAN24775.1.
RefSeqNP_696139.1. NC_004307.2.

3D structure databases

ProteinModelPortalQ8G5P1.
ModBaseSearch...

Protein-protein interaction databases

STRING206672.BL0964.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN24775; AAN24775; BL0964.
GeneID1022467.
KEGGblo:BL0964.
PATRIC21118397. VBIBifLon107831_0668.

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHOG000283476.
KOK04042.
OMAEPQTHLR.
ProtClustDBPRK14352.

Enzyme and pathway databases

BioCycBLON206672:GI1E-630-MONOMER.
UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PANTHERPTHR22572:SF17. PTHR22572:SF17. 1 hit.
PfamPF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_BIFLO
AccessionPrimary (citable) accession number: Q8G5P1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: March 1, 2003
Last modified: May 29, 2013
This is version 71 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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