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B8GRB6 (GLMU_THISH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:Tgr7_3303
OrganismThioalkalivibrio sp. (strain HL-EbGR7) [Complete proteome] [HAMAP]
Taxonomic identifier396588 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeThioalkalivibrio

Protein attributes

Sequence length459 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 – 459459Bifunctional protein GlmU HAMAP-Rule MF_01631
PRO_1000186508

Regions

Region1 – 230230Pyrophosphorylase By similarity
Region10 – 134UDP-GlcNAc binding By similarity
Region80 – 812UDP-GlcNAc binding By similarity
Region102 – 1043UDP-GlcNAc binding By similarity
Region231 – 25121Linker By similarity
Region252 – 459208N-acetyltransferase By similarity
Region387 – 3882Acetyl-CoA binding By similarity

Sites

Active site3641Proton acceptor By similarity
Metal binding1041Magnesium By similarity
Metal binding2281Magnesium By similarity
Binding site241UDP-GlcNAc By similarity
Binding site751UDP-GlcNAc By similarity
Binding site1401UDP-GlcNAc; via amide nitrogen By similarity
Binding site1551UDP-GlcNAc By similarity
Binding site1701UDP-GlcNAc By similarity
Binding site2281UDP-GlcNAc By similarity
Binding site3341Acetyl-CoA; amide nitrogen By similarity
Binding site3521Acetyl-CoA By similarity
Binding site3671Acetyl-CoA By similarity
Binding site3781Acetyl-CoA By similarity
Binding site4061Acetyl-CoA By similarity
Binding site4241Acetyl-CoA; via amide nitrogen By similarity
Binding site4411Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
B8GRB6 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 6D7E892C8B1ED632

FASTA45949,073
        10         20         30         40         50         60 
MTTPTSILIL AAGQGTRMRS SLPKVLQPLA GRPLLSHVLD TARSLDPHRL VVVYGHGGDR 

        70         80         90        100        110        120 
VREAFPEDDI RWVHQAEQRG TGHAVQVALP ETDADDRVLI LYGDVPLVRG ETVRRLLAQL 

       130        140        150        160        170        180 
DEGGDLVILT AALKSPTGYG RILRDDSGRV QRIVEEKDAS DSERRVNEVN TGIMAARASD 

       190        200        210        220        230        240 
FTRWLSKVTN DNAQGEFYLT DCVALANTEG RRVEAVVGHE AIELMGVNDK RQLAEQERAY 

       250        260        270        280        290        300 
QRREAERLMV QGVTVIDPAR LDVRGEVEAG RDVSLDINVI LQGSVKLGEG AKVGAGCVII 

       310        320        330        340        350        360 
DSEIGPGAHI LPHTVIEGAV IGAGASVGPF ARIRPGTHTD SNAKIGNFVE VKNARVGEGS 

       370        380        390        400        410        420 
KINHLSYVGD SELGRDVNIG AGTITCNYDG ANKHKTIIGD RAFIGSNTAL VAPLTVGEGA 

       430        440        450 
TIGAGTTLNK DAPPGELTVA RAKAITIPGW KRPVKKPKE 

« Hide

References

[1]"Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7."
Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N., Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.
Stand. Genomic Sci. 4:23-35(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HL-EbGR7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001339 Genomic DNA. Translation: ACL74370.1.
RefSeqYP_002515357.1. NC_011901.1.

3D structure databases

ProteinModelPortalB8GRB6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING396588.Tgr7_3303.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL74370; ACL74370; Tgr7_3303.
GeneID7315531.
KEGGtgr:Tgr7_3303.
PATRIC23966096. VBIThiSp19295_3262.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
KOK04042.
OMANKHKTII.
OrthoDBEOG6Z6FQZ.

Enzyme and pathway databases

BioCycTSUL396588:GH5B-3355-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]
PfamPF00132. Hexapep. 4 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF51161. SSF51161. 1 hit.
TIGRFAMsTIGR01173. glmU. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLMU_THISH
AccessionPrimary (citable) accession number: B8GRB6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways