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Q9KGJ6 (GLMU_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. 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:BH0065
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length455 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 – 455455Bifunctional protein GlmU HAMAP MF_01631
PRO_0000233731

Regions

Region1 – 230230Pyrophosphorylase By similarity
Region9 – 124Substrate binding By similarity
Region78 – 792Substrate binding By similarity
Region231 – 25121Linker By similarity
Region252 – 455204N-acetyltransferase By similarity

Sites

Active site3631Proton acceptor By similarity
Metal binding1031Magnesium By similarity
Metal binding2281Magnesium By similarity
Binding site731Substrate By similarity
Binding site1401Substrate; via amide nitrogen By similarity
Binding site1551Substrate By similarity
Binding site1701Substrate By similarity
Binding site3871Acetyl-CoA By similarity
Binding site4231Acetyl-CoA; via amide nitrogen By similarity
Binding site4401Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KGJ6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 9D36C1052A97436C

FASTA45549,282
        10         20         30         40         50         60 
MSNRFAVILA AGQGTRMKSK LYKVLHSVCG KPMVQHVVDQ VSALGFDEIV TIIGHGADAV 

        70         80         90        100        110        120 
KSQLGERVSY ALQEEQLGTG HAVLQAESAL GGRRGVTIVL CGDTPLLTAE TIDHVMSYHE 

       130        140        150        160        170        180 
EEQAKATVLT AELADPTGYG RIVRNDKGLV ERIVEHKDAT SEEKQITEVN TGTYCFDNEA 

       190        200        210        220        230        240 
LFQALKEVGN NNAQGEYYLP DVIQILQTKG EKVAAYKTAH VEETLGVNDR VALAQAEQVM 

       250        260        270        280        290        300 
KRRINEAWMR KGVTFIDPEQ TYVSPDATIG QDTVIYPGTM VLGQTTIGEG CVLGPHTELK 

       310        320        330        340        350        360 
DSKIGNKTAV KQSVVHNSEV GERVSIGPFS HIRPASMIHD DVRIGNFVEV KKSTIGKESK 

       370        380        390        400        410        420 
ASHLSYIGDA EVGERVNFSC GSITVNYDGK NKFLTKIEDD AFIGCNSNLI APVTIGKGAL 

       430        440        450 
IAAGSTITED VPSDALSIAR ARQTNKEHYV TKKNN

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000004 Genomic DNA. Translation: BAB03784.1.
PIRA83658.
RefSeqNP_240931.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KGJ6.
SMRQ9KGJ6. Positions 3-452.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000051920; EBBACP00000050559; EBBACG00000051911.
GeneID892269.
GenomeReviewsGene locus BH0065 in contig BA000004_GR.
KEGGbha:BH0065.
NMPDRfig|272558.1.peg.65.
PATRIC18936960. VBIBacHal18977_0070.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000000560.
HOGENOMHBG688195.
OMAGSKVNHL.
PhylomeDBQ9KGJ6.
ProtClustDBCLSK2748798.

Enzyme and pathway databases

BioCycBHAL272558:BH0065-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. 3 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_BACHD
AccessionPrimary (citable) accession number: Q9KGJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 67 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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