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P43889 (GLMU_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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:HI_0642
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.2

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. HAMAP-Rule 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-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. Ref.2 Ref.3

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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 – 456456Bifunctional protein GlmU HAMAP-Rule MF_01631
PRO_0000068703

Regions

Region1 – 229229Pyrophosphorylase By similarity
Region11 – 144UDP-GlcNAc binding HAMAP-Rule MF_01631
Region81 – 822UDP-GlcNAc binding HAMAP-Rule MF_01631
Region103 – 1053UDP-GlcNAc binding HAMAP-Rule MF_01631
Region139 – 1402UDP-GlcNAc binding HAMAP-Rule MF_01631
Region224 – 2274UDP-GlcNAc binding HAMAP-Rule MF_01631
Region230 – 25021Linker By similarity
Region251 – 456206N-acetyltransferase By similarity
Region386 – 3872Acetyl-CoA binding By similarity

Sites

Active site3631Proton acceptor By similarity
Metal binding1051Magnesium By similarity
Metal binding2271Magnesium By similarity
Binding site251UDP-GlcNAc By similarity
Binding site761UDP-GlcNAc
Binding site1401UDP-GlcNAc; via amide nitrogen By similarity
Binding site1541UDP-GlcNAc
Binding site1691UDP-GlcNAc
Binding site2271UDP-GlcNAc By similarity
Binding site3331Acetyl-CoA; amide nitrogen By similarity
Binding site3511Acetyl-CoA By similarity
Binding site3661Acetyl-CoA By similarity
Binding site3771Acetyl-CoA By similarity
Binding site4051Acetyl-CoA By similarity
Binding site4231Acetyl-CoA; via amide nitrogen By similarity
Binding site4401Acetyl-CoA By similarity

Experimental info

Mutagenesis251K → A: No pyrophosphorylase activity. Ref.2
Mutagenesis761Q → A: No pyrophosphorylase activity. Ref.2
Mutagenesis1031Y → A: Reduces the pyrophosphorylase activity. Ref.2
Mutagenesis1051D → A: No pyrophosphorylase activity. Ref.2
Mutagenesis2231V → A: Reduces slightly the pyrophosphorylase activity. Ref.2
Mutagenesis2241E → A: Reduces the pyrophosphorylase activity. Ref.2

Secondary structure

........................................................................... 456
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43889 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 93B76552A8F9BD36

FASTA45649,287
        10         20         30         40         50         60 
MTKKALSAVI LAAGKGTRMY SDLPKVLHTI AGKPMVKHVI DTAHQLGSEN IHLIYGHGGD 

        70         80         90        100        110        120 
LMRTHLANEQ VNWVLQTEQL GTAHAVQQAA PFFKDNENIV VLYGDAPLIT KETLEKLIEA 

       130        140        150        160        170        180 
KPENGIALLT VNLDNPTGYG RIIRENGNVV AIVEQKDANA EQLNIKEVNT GVMVSDGASF 

       190        200        210        220        230        240 
KKWLARVGNN NAQGEYYLTD LIALANQDNC QVVAVQATDV MEVEGANNRL QLAALERYFQ 

       250        260        270        280        290        300 
NKQASKLLLE GVMIYDPARF DLRGTLEHGK DVEIDVNVII EGNVKLGDRV KIGTGCVLKN 

       310        320        330        340        350        360 
VVIGNDVEIK PYSVLEDSIV GEKAAIGPFS RLRPGAELAA ETHVGNFVEI KKSTVGKGSK 

       370        380        390        400        410        420 
VNHLTYVGDS EIGSNCNIGA GVITCNYDGA NKFKTIIGDD VFVGSDTQLV APVKVANGAT 

       430        440        450 
IGAGTTITRD VGENELVITR VAQRHIQGWQ RPIKKK 

« Hide

References

« Hide 'large scale' references
[1]"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. expand/collapse author list , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.
Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]"Characterization of substrate binding and catalysis in the potential antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase (GlmU)."
Mochalkin I., Lightle S., Zhu Y., Ohren J.F., Spessard C., Chirgadze N.Y., Banotai C., Melnick M., McDowell L.
Protein Sci. 16:2657-2666(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, MUTAGENESIS OF LYS-25; GLN-76; TYR-103; ASP-105; VAL-223 AND GLU-224, REACTION MECHANSIM, SUBUNIT.
[3]"Structure of a small-molecule inhibitor complexed with GlmU from Haemophilus influenzae reveals an allosteric binding site."
Mochalkin I., Lightle S., Narasimhan L., Bornemeier D., Melnick M., Vanderroest S., McDowell L.
Protein Sci. 17:577-582(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.
[4]"Discovery and initial sar of quinazoline inhibitors of GlmU from Haemophilus influenzae."
Melnick M., Mochalkin I., Lightle S., Narasimhan L., Mcdowell L., Sarver R.
Submitted (OCT-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC22302.1.
PIRG64083.
RefSeqNP_438802.1. NC_000907.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V0HX-ray1.79A1-456[»]
2V0IX-ray1.89A1-456[»]
2V0JX-ray2.00A1-456[»]
2V0KX-ray2.30A1-456[»]
2V0LX-ray2.20A1-456[»]
2VD4X-ray1.90A1-456[»]
2W0VX-ray1.99A1-456[»]
2W0WX-ray2.59A1-456[»]
4E1KX-ray2.00A1-456[»]
ProteinModelPortalP43889.
SMRP43889. Positions 4-453.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI0642.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC22302; AAC22302; HI_0642.
GeneID949691.
KEGGhin:HI0642.
PATRIC20189891. VBIHaeInf48452_0670.

Phylogenomic databases

eggNOGCOG1207.
KOK04042.
OMADCVTNQD.
OrthoDBEOG6Z6FQZ.
PhylomeDBP43889.

Enzyme and pathway databases

UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00132. Hexapep. 4 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP43889.

Entry information

Entry nameGLMU_HAEIN
AccessionPrimary (citable) accession number: P43889
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names