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P43889

- GLMU_HAEIN

UniProt

P43889 - GLMU_HAEIN

Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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.
    UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Pathwayi

    Sites

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

    GO - Molecular functioni

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

    GO - Biological processi

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

    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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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 GlmUPRO_0000068703Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.3 Publications

    Protein-protein interaction databases

    STRINGi71421.HI0642.

    Structurei

    Secondary structure

    1
    456
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP43889.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 229229PyrophosphorylaseBy similarityAdd
    BLAST
    Regioni11 – 144UDP-GlcNAc binding
    Regioni81 – 822UDP-GlcNAc binding
    Regioni103 – 1053UDP-GlcNAc binding
    Regioni139 – 1402UDP-GlcNAc binding
    Regioni224 – 2274UDP-GlcNAc binding
    Regioni230 – 25021LinkerBy similarityAdd
    BLAST
    Regioni251 – 456206N-acetyltransferaseBy similarityAdd
    BLAST
    Regioni386 – 3872Acetyl-CoA bindingBy similarity

    Sequence similaritiesi

    In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.Curated
    In the C-terminal section; belongs to the transferase hexapeptide repeat family.Curated

    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

    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: October 1, 2014
    This is version 107 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