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B8J9N1 (GLMU_ANAD2) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 37. 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:A2cp1_4101
OrganismAnaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258) [Complete proteome] [HAMAP]
Taxonomic identifier455488 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length488 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 – 488488Bifunctional protein GlmU HAMAP-Rule MF_01631
PRO_1000186392

Regions

Region1 – 237237Pyrophosphorylase By similarity
Region13 – 164UDP-GlcNAc binding By similarity
Region87 – 882UDP-GlcNAc binding By similarity
Region110 – 1123UDP-GlcNAc binding By similarity
Region238 – 25821Linker By similarity
Region259 – 488230N-acetyltransferase By similarity
Region394 – 3952Acetyl-CoA binding By similarity

Sites

Active site3711Proton acceptor By similarity
Metal binding1121Magnesium By similarity
Metal binding2351Magnesium By similarity
Binding site271UDP-GlcNAc By similarity
Binding site821UDP-GlcNAc By similarity
Binding site1491UDP-GlcNAc; via amide nitrogen By similarity
Binding site1641UDP-GlcNAc By similarity
Binding site1791UDP-GlcNAc By similarity
Binding site2351UDP-GlcNAc By similarity
Binding site3411Acetyl-CoA; amide nitrogen By similarity
Binding site3591Acetyl-CoA By similarity
Binding site3741Acetyl-CoA By similarity
Binding site3851Acetyl-CoA By similarity
Binding site4131Acetyl-CoA By similarity
Binding site4311Acetyl-CoA; via amide nitrogen By similarity
Binding site4481Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
B8J9N1 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 889645503870632F

FASTA48850,902
        10         20         30         40         50         60 
MPRTRTPLAA IVLAAGKGTR MKSNKAKVLH EVAGRPLAYY PVKRALELGA SPVVVVVGHQ 

        70         80         90        100        110        120 
AEAVEAALSA ALPEAPLRFA VQEQQLGTAH AVLAAKRALR GYRGPVLILS GDTPLLRAET 

       130        140        150        160        170        180 
LEAVVSAGRR ARAAVSLATM TLEVPRGYGR VVRDARGRPA RIVEEKDATE AERAVREVNA 

       190        200        210        220        230        240 
GLYCVDAELL WKKLAKVGTA NAQREFYLTD LVPMAAQAGG VAGVEVPAEE ASGVNDRVEL 

       250        260        270        280        290        300 
SRANRVMVGR LAEAFMRAGV TIEDPARFDC DEGVEIGADA VIEPNVRLRG RTRVGARTRV 

       310        320        330        340        350        360 
GVGAVITDGV LADGVTVNPY TVISEAQVAE GAILGPFSRL RPGADIGPEA HVGNFVEVKK 

       370        380        390        400        410        420 
SRLGKGAKAN HLAYLGDAEI GAGANIGAGT ITCNYDGERK NPTRIGEGAF IGSDSILVAP 

       430        440        450        460        470        480 
IEIGAGAYVA AGSTLTDPVP AGALALGRAR QVTKEGWVAQ RQAEKQMKGT ATGPASARKG 


RPAARRAS 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-1."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Beliaev A.S., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-1 / ATCC BAA-258.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001359 Genomic DNA. Translation: ACL67419.1.
RefSeqYP_002494485.1. NC_011891.1.

3D structure databases

ProteinModelPortalB8J9N1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING455488.A2cp1_4101.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL67419; ACL67419; A2cp1_4101.
GeneID7297526.
KEGGacp:A2cp1_4101.
PATRIC20915156. VBIAnaDeh28364_4136.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHOG000283476.
KOK04042.
OMAIGERAYI.
OrthoDBEOG6Z6FQZ.

Enzyme and pathway databases

BioCycADEH455488:GH35-4157-MONOMER.
UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_ANAD2
AccessionPrimary (citable) accession number: B8J9N1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: June 11, 2014
This is version 37 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