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A9NH16 (GLMU_ACHLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. 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:ACL_1036
OrganismAcholeplasma laidlawii (strain PG-8A) [Complete proteome] [HAMAP]
Taxonomic identifier441768 [NCBI]
Taxonomic lineageBacteria › Tenericutes › Mollicutes › Acholeplasmatales › Acholeplasmataceae › Acholeplasma

Protein attributes

Sequence length460 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 – 460460Bifunctional protein GlmU HAMAP MF_01631
PRO_1000088122

Regions

Region1 – 228228Pyrophosphorylase By similarity
Region8 – 114Substrate binding By similarity
Region77 – 782Substrate binding By similarity
Region229 – 24921Linker By similarity
Region250 – 460211N-acetyltransferase By similarity

Sites

Active site3611Proton acceptor By similarity
Metal binding1021Magnesium By similarity
Metal binding2261Magnesium By similarity
Binding site721Substrate By similarity
Binding site1391Substrate; via amide nitrogen By similarity
Binding site1541Substrate By similarity
Binding site1691Substrate By similarity
Binding site3851Acetyl-CoA By similarity
Binding site4211Acetyl-CoA; via amide nitrogen By similarity
Binding site4381Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
A9NH16 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 0D0F10C4280E2489

FASTA46051,183
        10         20         30         40         50         60 
MKNYALVLAA GKGTRMKSDI PKVAFPILRK PMIEYIVENI EKSSVEEIYL VLGYKREVVE 

        70         80         90        100        110        120 
GIVKDRAKYV YQEEQLGTGH AAMMAAPVLS KLDGNTFIMP GDVPLIWYKS IDRMFAVHED 

       130        140        150        160        170        180 
NGNDFTIVTA HYEDPEGYGR IVRNEQGVIQ RIVEEKDAND FEKEIKEVNT GIYIVNNKKF 

       190        200        210        220        230        240 
FSLLKNLNNN NAKGEYYITD MVELMKKDYK IGSYMIKNNS LAMGVNDLYA ISKAEKYLRE 

       250        260        270        280        290        300 
YINKDHMLNG VSMINPETIT IGHNVIIEPG VTINPNTTIT GDTVIKAGAI VGPNTEIHNS 

       310        320        330        340        350        360 
RIDSHVVVRH SLVYDSIVRE GTTVGPFAHL RDHADIGTHN RIGNFVEVKK SSTGHNTKAS 

       370        380        390        400        410        420 
HLAYIGDSVV GESVNFGCGS VTVNYDGKLK HKTEIGDNVF IGCNTNLIAP IKIGDNVFIA 

       430        440        450        460 
AGSTVTKDIP DNGFAIARSR QVTKEDYSKY LISPKPKKEE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000896 Genomic DNA. Translation: ABX81646.1.
RefSeqYP_001621022.1. NC_010163.1.

3D structure databases

ProteinModelPortalA9NH16.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9NH16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5803686.
GenomeReviewsGene locus ACL_1036 in contig CP000896_GR.
KEGGacl:ACL_1036.
PATRIC20638774. VBIAchLai134690_1004.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG688195.
OMARESIGES.

Enzyme and pathway databases

BioCycALAI441768:ACL_1036-MONOMER.

Family and domain databases

HAMAPMF_01631. GlmU.
[Tree]
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR005835. NTP_transferase.
IPR011004. Trimer_LpxA-like.
[Graphical view]
KOK04042.
PANTHERPTHR22572:SF17. PTHR22572:SF17. 1 hit.
PfamPF00132. Hexapep. 4 hits.
PF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. GlmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_ACHLI
AccessionPrimary (citable) accession number: A9NH16
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 34 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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