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Reviewed, UniProtKB/Swiss-Prot Q3MC88 (GLMU_ANAVT)

Last modified February 9, 2010. Version 34. 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: Ava_1776
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length451 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-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. HAMAP MF_01631

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. HAMAP 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 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 MF_01631

Subcellular location

Cytoplasm By similarity HAMAP 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 – 451451Bifunctional protein glmU HAMAP MF_01631
PRO_0000244287

Regions

Region1 – 225225Pyrophosphorylase By similarity
Region7 – 104Substrate binding By similarity
Region77 – 782Substrate binding By similarity
Region226 – 24621Linker By similarity
Region247 – 451205N-acetyltransferase By similarity

Sites

Active site3581Proton acceptor By similarity
Metal binding1021Magnesium By similarity
Metal binding2231Magnesium By similarity
Binding site721Substrate By similarity
Binding site1391Substrate; via amide nitrogen By similarity
Binding site1541Substrate By similarity
Binding site1691Substrate By similarity
Binding site3821Acetyl-CoA By similarity
Binding site4001Acetyl-CoA By similarity
Binding site4181Acetyl-CoA; via amide nitrogen By similarity
Binding site4351Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3MC88-1 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 0216286BAA42FA62

FASTA45149,191
        10         20         30         40         50         60 
MVVVAILAAG RGTRMKSDLP KVLHPLGGRS LVERVIDSVE PLSPSRRLVI VGYQAEQVKT 

        70         80         90        100        110        120 
GLQSLHLEFV EQTVQLGTGH AIQQLLPHLE GYTGDLLVLN GDVPLLRTQT LEQLLQTHQT 

       130        140        150        160        170        180 
NQNAATILTS HLPNPKGYGR VFCNGNNIVQ QIVEDKDCSP AQRQNHRINA GIYCFRWENL 

       190        200        210        220        230        240 
AQVLPHLEAN NAQKEYYLTD AVTQVGQVMA VDVEDYQEIL GINDRLQLAT AYEILQRRVK 

       250        260        270        280        290        300 
EQWMMAGVTL IDPNSITIDD TVDLQPDVII EPQTHLRGNT FIQTGSRIGP GSLIENSQLG 

       310        320        330        340        350        360 
ANVTVQYSVI TDSTIQNGAK IGPYAHLRGH AQVGANCRIG NFVELKNTEL GDRTNVAHLS 

       370        380        390        400        410        420 
YLGDATAGTQ VNIGAGTITA NYDGVKKHRT KIGDRTKTGS NSVLVAPVTL GDDVYVAAGS 

       430        440        450 
TITEDVPNDS LVIARTRQVV KPGWRKKSGE S 

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References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000117 Genomic DNA. Translation: ABA21398.1.
RefSeqYP_322293.1.

3D structure databases

SMRQ3MC88. Positions 5-447.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3MC88.

Genome annotation databases

GeneID3682060.
GenomeReviewsGene locus Ava_1776 in contig CP000117_GR.
KEGGava:Ava_1776.
NMPDRfig|240292.3.peg.2856.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHBG688195.
OMAGSKVNHL.
PhylomeDBQ3MC88.

Enzyme and pathway databases

BioCycAVAR240292:AVA_1776-MONOMER.

Family and domain databases

HAMAPMF_01631. GlmU.
[Tree]
InterProIPR005882. Bifunctional_GlmU.
IPR005835. NTP_transferase.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00483. NTP_transferase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_ANAVT
AccessionPrimary (citable) accession number: Q3MC88
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 25, 2005
Last modified: February 9, 2010
This is version 34 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