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Reviewed, UniProtKB/Swiss-Prot Q2IGL4 (GLMU_ANADE)

Last modified June 16, 2009. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional protein glmU
Including the following 2 domains:
    1- Recommended name:
            UDP-N-acetylglucosamine pyrophosphorylase
              EC=2.7.7.23
        Alternative name(s):
            N-acetylglucosamine-1-phosphate uridyltransferase
    2- Recommended name:
            Glucosamine-1-phosphate N-acetyltransferase
              EC=2.3.1.157
Gene names
Name: glmU
Ordered Locus Names: Adeh_3958
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Pathway

Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from D-glucosamine 6-phosphate (route II): step 2/2. HAMAP MF_01631

Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine biosynthesis; UDP-N-acetyl-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.

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 MF_01631
PRO_0000244288

Regions

Region1 – 237237Pyrophosphorylase By similarity
Region13 – 164Substrate binding By similarity
Region87 – 882Substrate binding By similarity
Region238 – 25821Linker By similarity
Region259 – 488230N-acetyltransferase By similarity

Sites

Active site3711Proton acceptor By similarity
Metal binding1121Magnesium By similarity
Metal binding2351Magnesium By similarity
Binding site821Substrate By similarity
Binding site1491Substrate; via amide nitrogen By similarity
Binding site1641Substrate By similarity
Binding site1791Substrate By similarity
Binding site3951Acetyl-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
Q2IGL4-1 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 5BDFBDBF8AF6E784

FASTA48850,939
        10         20         30         40         50         60 
MPRTRTPLAA IVLAAGKGTR MKSNKAKVLH EVAGRPLAYY PVKRAVELGA SPVVVVVGHQ 

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

       130        140        150        160        170        180 
LEAVVSARRR ARAAVSLATM TLEAPRGYGR VVRDARGRPA RIVEEKDATD AERAVREVNA 

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

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

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

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

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


RPAARRAS 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000251 Genomic DNA. Translation: ABC83722.1.
RefSeqYP_467159.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3887770.
GenomeReviewsGene locus Adeh_3958 in contig CP000251_GR.
KEGGade:Adeh_3958.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2IGL4.
OMAQ2IGL4. TRMKSKL.

Enzyme and pathway databases

BioCycADEH290397:ADEH_3958-MON.

Family and domain databases

HAMAPMF_01631.
[Tree]
InterProIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR005835. NTP_transferase.
IPR005882. UDP_GlcNAc_PyrPase.
[Graphical view]
PfamPF00132. Hexapep. 7 hits.
PF00483. NTP_transferase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_ANADE
AccessionPrimary (citable) accession number: Q2IGL4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 7, 2006
Last modified: June 16, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents