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P43889

- GLMU_HAEIN

UniProt

P43889 - GLMU_HAEIN

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Protein
Bifunctional protein GlmU
Gene
glmU, HI_0642
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotation
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine.UniRule annotation

Cofactori

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei25 – 251UDP-GlcNAc By similarity
Binding sitei76 – 761UDP-GlcNAc
Metal bindingi105 – 1051Magnesium By similarity
Binding sitei140 – 1401UDP-GlcNAc; via amide nitrogen By similarity
Binding sitei154 – 1541UDP-GlcNAc
Binding sitei169 – 1691UDP-GlcNAc
Metal bindingi227 – 2271Magnesium By similarity
Binding sitei227 – 2271UDP-GlcNAc By similarity
Binding sitei333 – 3331Acetyl-CoA; amide nitrogen By similarity
Binding sitei351 – 3511Acetyl-CoA By similarity
Active sitei363 – 3631Proton acceptor By similarity
Binding sitei366 – 3661Acetyl-CoA By similarity
Binding sitei377 – 3771Acetyl-CoA By similarity
Binding sitei405 – 4051Acetyl-CoA By similarity
Binding sitei423 – 4231Acetyl-CoA; via amide nitrogen By similarity
Binding sitei440 – 4401Acetyl-CoA By similarity

GO - Molecular functioni

  1. UDP-N-acetylglucosamine diphosphorylase activity Source: UniProtKB-HAMAP
  2. glucosamine-1-phosphate N-acetyltransferase activity Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. UDP-N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway
  2. cell morphogenesis Source: UniProtKB-HAMAP
  3. lipid A biosynthetic process Source: UniProtKB-UniPathway
  4. lipopolysaccharide biosynthetic process Source: InterPro
  5. peptidoglycan biosynthetic process Source: UniProtKB-HAMAP
  6. regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein GlmU
Including the following 2 domains:
UDP-N-acetylglucosamine pyrophosphorylase (EC:2.7.7.23)
Alternative name(s):
N-acetylglucosamine-1-phosphate uridyltransferase
Glucosamine-1-phosphate N-acetyltransferase (EC:2.3.1.157)
Gene namesi
Name:glmU
Ordered Locus Names:HI_0642
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251K → A: No pyrophosphorylase activity. 1 Publication
Mutagenesisi76 – 761Q → A: No pyrophosphorylase activity. 1 Publication
Mutagenesisi103 – 1031Y → A: Reduces the pyrophosphorylase activity. 1 Publication
Mutagenesisi105 – 1051D → A: No pyrophosphorylase activity. 1 Publication
Mutagenesisi223 – 2231V → A: Reduces slightly the pyrophosphorylase activity. 1 Publication
Mutagenesisi224 – 2241E → A: Reduces the pyrophosphorylase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Bifunctional protein GlmUUniRule annotation
PRO_0000068703Add
BLAST

Interactioni

Subunit structurei

Homotrimer.2 Publications

Protein-protein interaction databases

STRINGi71421.HI0642.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116
Helixi17 – 193
Beta strandi21 – 233
Helixi25 – 273
Beta strandi28 – 303
Helixi35 – 4511
Beta strandi51 – 555
Helixi59 – 657
Turni66 – 683
Beta strandi72 – 754
Helixi82 – 898
Helixi90 – 923
Beta strandi97 – 1037
Helixi111 – 12010
Beta strandi125 – 1328
Beta strandi141 – 1455
Beta strandi148 – 1536
Turni155 – 1573
Helixi160 – 1634
Beta strandi167 – 17610
Helixi177 – 1848
Helixi198 – 2003
Helixi201 – 2077
Beta strandi212 – 2165
Helixi221 – 2233
Helixi229 – 24921
Beta strandi253 – 2553
Helixi257 – 2593
Beta strandi260 – 2689
Beta strandi276 – 28611
Beta strandi297 – 3037
Beta strandi314 – 3207
Beta strandi328 – 3325
Beta strandi336 – 3383
Beta strandi343 – 35210
Beta strandi360 – 37213
Beta strandi383 – 3864
Beta strandi388 – 3914
Beta strandi395 – 3973
Beta strandi408 – 4158

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP43889.
SMRiP43889. Positions 4-453.

Miscellaneous databases

EvolutionaryTraceiP43889.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 229229Pyrophosphorylase By similarity
Add
BLAST
Regioni11 – 144UDP-GlcNAc bindingUniRule annotation
Regioni81 – 822UDP-GlcNAc bindingUniRule annotation
Regioni103 – 1053UDP-GlcNAc bindingUniRule annotation
Regioni139 – 1402UDP-GlcNAc bindingUniRule annotation
Regioni224 – 2274UDP-GlcNAc bindingUniRule annotation
Regioni230 – 25021Linker By similarity
Add
BLAST
Regioni251 – 456206N-acetyltransferase By similarity
Add
BLAST
Regioni386 – 3872Acetyl-CoA binding By similarity

Sequence similaritiesi

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.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1207.
KOiK04042.
OMAiDCVTNQD.
OrthoDBiEOG6Z6FQZ.
PhylomeDBiP43889.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU.
InterProiIPR005882. 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]
PfamiPF00132. Hexapep. 4 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01173. glmU. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P43889-1 [UniParc]FASTAAdd to Basket

« Hide

MTKKALSAVI LAAGKGTRMY SDLPKVLHTI AGKPMVKHVI DTAHQLGSEN    50
IHLIYGHGGD LMRTHLANEQ VNWVLQTEQL GTAHAVQQAA PFFKDNENIV 100
VLYGDAPLIT KETLEKLIEA KPENGIALLT VNLDNPTGYG RIIRENGNVV 150
AIVEQKDANA EQLNIKEVNT GVMVSDGASF KKWLARVGNN NAQGEYYLTD 200
LIALANQDNC QVVAVQATDV MEVEGANNRL QLAALERYFQ NKQASKLLLE 250
GVMIYDPARF DLRGTLEHGK DVEIDVNVII EGNVKLGDRV KIGTGCVLKN 300
VVIGNDVEIK PYSVLEDSIV GEKAAIGPFS RLRPGAELAA ETHVGNFVEI 350
KKSTVGKGSK VNHLTYVGDS EIGSNCNIGA GVITCNYDGA NKFKTIIGDD 400
VFVGSDTQLV APVKVANGAT IGAGTTITRD VGENELVITR VAQRHIQGWQ 450
RPIKKK 456
Length:456
Mass (Da):49,287
Last modified:November 1, 1995 - v1
Checksum:i93B76552A8F9BD36
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC22302.1.
PIRiG64083.
RefSeqiNP_438802.1. NC_000907.1.
WP_005694502.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22302; AAC22302; HI_0642.
GeneIDi949691.
KEGGihin:HI0642.
PATRICi20189891. VBIHaeInf48452_0670.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC22302.1 .
PIRi G64083.
RefSeqi NP_438802.1. NC_000907.1.
WP_005694502.1. NC_000907.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V0H X-ray 1.79 A 1-456 [» ]
2V0I X-ray 1.89 A 1-456 [» ]
2V0J X-ray 2.00 A 1-456 [» ]
2V0K X-ray 2.30 A 1-456 [» ]
2V0L X-ray 2.20 A 1-456 [» ]
2VD4 X-ray 1.90 A 1-456 [» ]
2W0V X-ray 1.99 A 1-456 [» ]
2W0W X-ray 2.59 A 1-456 [» ]
4E1K X-ray 2.00 A 1-456 [» ]
ProteinModelPortali P43889.
SMRi P43889. Positions 4-453.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 71421.HI0642.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC22302 ; AAC22302 ; HI_0642 .
GeneIDi 949691.
KEGGi hin:HI0642.
PATRICi 20189891. VBIHaeInf48452_0670.

Phylogenomic databases

eggNOGi COG1207.
KOi K04042.
OMAi DCVTNQD.
OrthoDBi EOG6Z6FQZ.
PhylomeDBi P43889.

Enzyme and pathway databases

UniPathwayi UPA00113 ; UER00532 .
UPA00113 ; UER00533 .
UPA00973 .

Miscellaneous databases

EvolutionaryTracei P43889.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
HAMAPi MF_01631. GlmU.
InterProi IPR005882. 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 ]
Pfami PF00132. Hexapep. 4 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view ]
SUPFAMi SSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsi TIGR01173. glmU. 1 hit.
PROSITEi PS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiGLMU_HAEIN
AccessioniPrimary (citable) accession number: P43889
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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