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A5WHT0 (GLMU_PSYWF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:PsycPRwf_2281
OrganismPsychrobacter sp. (strain PRwf-1) [Complete proteome] [HAMAP]
Taxonomic identifier349106 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length455 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 – 455455Bifunctional protein GlmU HAMAP-Rule MF_01631
PRO_1000073649

Regions

Region1 – 228228Pyrophosphorylase By similarity
Region10 – 134UDP-GlcNAc binding By similarity
Region80 – 812UDP-GlcNAc binding By similarity
Region102 – 1043UDP-GlcNAc binding By similarity
Region229 – 24921Linker By similarity
Region250 – 455206N-acetyltransferase By similarity
Region385 – 3862Acetyl-CoA binding By similarity

Sites

Active site3621Proton acceptor By similarity
Metal binding1041Magnesium By similarity
Metal binding2261Magnesium By similarity
Binding site241UDP-GlcNAc By similarity
Binding site751UDP-GlcNAc By similarity
Binding site1381UDP-GlcNAc; via amide nitrogen By similarity
Binding site1531UDP-GlcNAc By similarity
Binding site1681UDP-GlcNAc By similarity
Binding site2261UDP-GlcNAc By similarity
Binding site3321Acetyl-CoA; amide nitrogen By similarity
Binding site3501Acetyl-CoA By similarity
Binding site3651Acetyl-CoA By similarity
Binding site3761Acetyl-CoA By similarity
Binding site4221Acetyl-CoA; via amide nitrogen By similarity
Binding site4391Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
A5WHT0 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 6074BD4D1C91F6F6

FASTA45549,296
        10         20         30         40         50         60 
MNNTLTTIIL AAGKGTRMQS AKPKVLQILA DKPLLAHVLD TCQSISVDKT IVVYGFGGDQ 

        70         80         90        100        110        120 
VQQAMTDYSL TWVEQTEQLG TGHAVKVALD ELPSTGKSLI LYGDVPLVSA ETLSRLKQAN 

       130        140        150        160        170        180 
VQGMSMLTLT VDNPFGLGRI KRDEQGNITA IVEQKDASEQ EQAIREINSG IYCVDNALLH 

       190        200        210        220        230        240 
QYLPNLSNDN AQQEYYLTDI VKMAVADGIA IAAIEPDYEF EIEGVNNRQQ LAQLERKWQA 

       250        260        270        280        290        300 
KLVEDLQVQG VQFADPNRVD IRGEVSVGQD VFVDINVVFK GKVSLGNNVT IEAGCMIKDS 

       310        320        330        340        350        360 
QIGDNVHIKP YCVFDDAQVA QGATIGPFAH LRPQTVLEKN TRLGNFVEIK KSRIGEGSKV 

       370        380        390        400        410        420 
NHLSYVGDAQ IGAGVNFGAG AITCNYDGVN KHQTIVGDNA FIGTNTSLVA PVTIGQTATI 

       430        440        450 
GAGSVITKNV EDNALAIGRG RQVQKDNYQR PEKKK 

« Hide

References

[1]"Complete sequence of chromosome of Psychrobacter sp. PRwf-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PRwf-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000713 Genomic DNA. Translation: ABQ95221.1.
RefSeqYP_001281171.1. NC_009524.1.

3D structure databases

ProteinModelPortalA5WHT0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349106.PsycPRwf_2281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ95221; ABQ95221; PsycPRwf_2281.
GeneID5205575.
KEGGprw:PsycPRwf_2281.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHOG000283476.
KOK04042.
OMANKHKTII.
OrthoDBEOG6Z6FQZ.
ProtClustDBCLSK839594.

Enzyme and pathway databases

BioCycPPRW349106:GHZF-2351-MONOMER.
UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
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.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_PSYWF
AccessionPrimary (citable) accession number: A5WHT0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 10, 2007
Last modified: February 19, 2014
This is version 51 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