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A1KR65 (GLMU_NEIMF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 56. 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:NMC0015
OrganismNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / FAM18) [Complete proteome] [HAMAP]
Taxonomic identifier272831 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria ›

Protein attributes

Sequence length456 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.

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.

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 – 456456Bifunctional protein GlmU HAMAP-Rule MF_01631
PRO_1000056175

Regions

Region1 – 228228Pyrophosphorylase By similarity
Region11 – 144UDP-GlcNAc binding By similarity
Region80 – 812UDP-GlcNAc binding By similarity
Region102 – 1043UDP-GlcNAc binding By similarity
Region229 – 24921Linker By similarity
Region250 – 456207N-acetyltransferase By similarity
Region385 – 3862Acetyl-CoA binding By similarity

Sites

Active site3621Proton acceptor By similarity
Metal binding1041Magnesium By similarity
Metal binding2261Magnesium By similarity
Binding site251UDP-GlcNAc By similarity
Binding site751UDP-GlcNAc By similarity
Binding site1381UDP-GlcNAc; via amide nitrogen By similarity
Binding site1531UDP-GlcNAc By similarity
Binding site1681UDP-GlcNAc By similarity
Binding site2261UDP-GlcNAc By similarity
Binding site3321Acetyl-CoA; amide nitrogen By similarity
Binding site3501Acetyl-CoA By similarity
Binding site3651Acetyl-CoA By similarity
Binding site3761Acetyl-CoA By similarity
Binding site4041Acetyl-CoA By similarity
Binding site4221Acetyl-CoA; via amide nitrogen By similarity
Binding site4391Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
A1KR65 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: D5A1494FBDD3F59B

FASTA45648,683
        10         20         30         40         50         60 
MPQNTLNIVI LAAGKGTRMY SKMPKVLHRI GGKPMLGRVI DTAAALNPQN ICVVIGHGKD 

        70         80         90        100        110        120 
QVLNAVKRDV VWVEQTEQLG TGHAVKTALP HLSAEGRTLV LYGDVPLIDV KTLKTLLEAA 

       130        140        150        160        170        180 
GNEVGLLTDV PADPTGLGRI IRDGNGSVTA IVEEKDADAA QKAVKEINTG ILVLPNAKLE 

       190        200        210        220        230        240 
NWLNSLSSNN AQGEYYLTDL IAKAVADGIK VHPVQVHTSY LAAGVNNKLQ LAELERIFQT 

       250        260        270        280        290        300 
EQAQELLKAG VTLSDPARFD LRGRLKHGQD VVIDVNCIFE GEVEIGDNVE IGANCVIKNA 

       310        320        330        340        350        360 
KIGANSKIAP FSHLEDCEVG ENNRIGPYAR LRPQAKLAAD VHIGNFVEIK NAAIGKGTKA 

       370        380        390        400        410        420 
NHLTYIGDAE VGSKTNFGAG TIIANYDGVH KHKTVIGNEV RIGSNCVLVA PVTLGNKVTT 

       430        440        450 
GAGSAITRNV EDGKLALARA RQTVIEGWVR PEKDKQ

« Hide

References

[1]"Meningococcal genetic variation mechanisms viewed through comparative analysis of serogroup C strain FAM18."
Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S., Quail M.A., Achtman M. expand/collapse author list , Barrell B.G., Saunders N.J., Parkhill J.
PLoS Genet. 3:230-240(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700532 / FAM18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM421808 Genomic DNA. Translation: CAM09341.1.
RefSeqYP_974160.1. NC_008767.1.

3D structure databases

ProteinModelPortalA1KR65.
SMRA1KR65. Positions 5-450.
ModBaseSearch...

Protein-protein interaction databases

STRING272831.NMC0015.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM09341; CAM09341; NMC0015.
GeneID4676123.
KEGGnmc:NMC0015.
PATRIC20349497. VBINeiMen17609_0022.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHOG000283476.
KOK04042.
OMAEPQTHLR.
ProtClustDBCLSK877361.

Enzyme and pathway databases

BioCycNMEN272831:GJDX-15-MONOMER.
UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PANTHERPTHR22572:SF17. PTHR22572:SF17. 1 hit.
PfamPF00132. Hexapep. 4 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_NEIMF
AccessionPrimary (citable) accession number: A1KR65
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: May 1, 2013
This is version 56 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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