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A0KQX6 (GLMU_AERHH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:AHA_4260
OrganismAeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]
Taxonomic identifier380703 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

Protein attributes

Sequence length453 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 – 453453Bifunctional protein GlmU HAMAP MF_01631
PRO_1000056135

Regions

Region1 – 226226Pyrophosphorylase By similarity
Region8 – 114Substrate binding By similarity
Region78 – 792Substrate binding By similarity
Region227 – 24721Linker By similarity
Region248 – 453206N-acetyltransferase By similarity

Sites

Active site3601Proton acceptor By similarity
Metal binding1021Magnesium By similarity
Metal binding2241Magnesium By similarity
Binding site731Substrate By similarity
Binding site1371Substrate; via amide nitrogen By similarity
Binding site1511Substrate By similarity
Binding site1661Substrate By similarity
Binding site3841Acetyl-CoA By similarity
Binding site4021Acetyl-CoA By similarity
Binding site4201Acetyl-CoA; via amide nitrogen By similarity
Binding site4371Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
A0KQX6 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 135D868733BD5685

FASTA45348,788
        10         20         30         40         50         60 
MSLNVVILAA GKGTRMRSSL PKVLHPVANK PMVSHVIETA RKVGAEQLHL VYGHGAELLK 

        70         80         90        100        110        120 
ERIQASDLNW VLQAQQLGTG HAVAQAIPFW QDEDDVLVLY GDTPLIQPET LQRLLAAKAS 

       130        140        150        160        170        180 
DGMALLTVVL DNPTGYGRIV RSNGQVVGIV EQKDANAEQL AIREVNTGVL VANGGQLRSW 

       190        200        210        220        230        240 
LSRLDNKNAQ GEFYLTDVIA MAHADNCPIA AVHPDDAMEV EGANNRVQLA QLERSYQKMQ 

       250        260        270        280        290        300 
AERLMIAGAT LIDPARFDLR GTLEIGEEVV IDVNVIIEGK VVLGNHVRIG AGSVLKDCVI 

       310        320        330        340        350        360 
GDHSEVKPYS VIEGAQIADQ CSVGPFTRLR PGTVLEQDAH VGNFVEMKKA RLGVGSKCGH 

       370        380        390        400        410        420 
LTYLGDAEVG AKVNIGAGTI TCNYDGVNKF QTIIEDDVFV GSDTQLVAPV RIGKGATLGA 

       430        440        450 
GSTITKDVAE NELVITRVPQ RHIQNWARPV KKK

« Hide

References

[1]"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."
Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.
J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 7966 / NCIB 9240.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000462 Genomic DNA. Translation: ABK38010.1.
RefSeqYP_858677.1. NC_008570.1.

3D structure databases

ProteinModelPortalA0KQX6.
SMRA0KQX6. Positions 2-450.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0KQX6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4487364.
GenomeReviewsGene locus AHA_4260 in contig CP000462_GR.
KEGGaha:AHA_4260.
PATRIC20786196. VBIAerHyd135212_4210.
TIGRAHA_4260.

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHBG688195.
OMAGSKVNHL.
PhylomeDBA0KQX6.
ProtClustDBCLSK729539.

Enzyme and pathway databases

BioCycAHYD196024:AHA_4260-MONOMER.

Family and domain databases

HAMAPMF_01631. GlmU.
[Tree]
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR011004. Trimer_LpxA-like.
[Graphical view]
KOK04042.
PANTHERPTHR22572:SF17. PTHR22572:SF17. 1 hit.
PfamPF00132. Hexapep. 2 hits.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. GlmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_AERHH
AccessionPrimary (citable) accession number: A0KQX6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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