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Q7V8F2

- GLMU_PROMM

UniProt

Q7V8F2 - GLMU_PROMM

Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Prochlorococcus marinus (strain MIT 9313)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      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.UniRule annotation

    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.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei21 – 211UDP-GlcNAcUniRule annotation
    Binding sitei73 – 731UDP-GlcNAcUniRule annotation
    Metal bindingi103 – 1031MagnesiumUniRule annotation
    Binding sitei140 – 1401UDP-GlcNAc; via amide nitrogenUniRule annotation
    Binding sitei155 – 1551UDP-GlcNAcUniRule annotation
    Binding sitei170 – 1701UDP-GlcNAcUniRule annotation
    Metal bindingi224 – 2241MagnesiumUniRule annotation
    Binding sitei224 – 2241UDP-GlcNAcUniRule annotation
    Binding sitei329 – 3291Acetyl-CoA; amide nitrogenUniRule annotation
    Binding sitei347 – 3471Acetyl-CoAUniRule annotation
    Active sitei359 – 3591Proton acceptorUniRule annotation
    Binding sitei362 – 3621Acetyl-CoAUniRule annotation
    Binding sitei373 – 3731Acetyl-CoAUniRule annotation
    Binding sitei419 – 4191Acetyl-CoA; via amide nitrogenUniRule annotation
    Binding sitei436 – 4361Acetyl-CoAUniRule annotation

    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 GlmUUniRule annotation
    Including the following 2 domains:
    UDP-N-acetylglucosamine pyrophosphorylaseUniRule annotation (EC:2.7.7.23UniRule annotation)
    Alternative name(s):
    N-acetylglucosamine-1-phosphate uridyltransferaseUniRule annotation
    Glucosamine-1-phosphate N-acetyltransferaseUniRule annotation (EC:2.3.1.157UniRule annotation)
    Gene namesi
    Name:glmUUniRule annotation
    Ordered Locus Names:PMT_0400
    OrganismiProchlorococcus marinus (strain MIT 9313)
    Taxonomic identifieri74547 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000001423: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 446446Bifunctional protein GlmUPRO_0000233816Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi74547.PMT0400.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7V8F2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 226226PyrophosphorylaseUniRule annotationAdd
    BLAST
    Regioni7 – 104UDP-GlcNAc bindingUniRule annotation
    Regioni78 – 792UDP-GlcNAc bindingUniRule annotation
    Regioni227 – 24721LinkerUniRule annotationAdd
    BLAST
    Regioni248 – 446199N-acetyltransferaseUniRule annotationAdd
    BLAST
    Regioni382 – 3832Acetyl-CoA bindingUniRule annotation

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1207.
    KOiK04042.
    OMAiDCVTNQD.
    OrthoDBiEOG6Z6FQZ.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    HAMAPiMF_01631. GlmU.
    InterProiIPR005882. Bifunctional_GlmU.
    IPR001451. Hexapep_transf.
    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.

    Sequencei

    Sequence statusi: Complete.

    Q7V8F2-1 [UniParc]FASTAAdd to Basket

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    MLAVAILAAG KGTRMKSCLP KVLQPLAGST LVERVLTSCS GLQPQRRLLI    50
    VGHQAQEVQQ QLTDWQGLEF VVQQPQNGTG HAVQQVLPVL EGFDGELLVL 100
    NGDVPLLRPS TIEHLVNEHR SSGADVTLLT ARLADPTGYG RVFSDQQGRV 150
    SSIVEHRDCS DEQRHNNLTN AGIYCFNWKK LAAVLPQLCS DNDQGELYLT 200
    DTVALLPIAM HVEVADPDEV NGINDRCQLA NCEALLQERL RNYWMKEGVT 250
    FTDPASCTLS EDCQFGRDVV IEPQTHLRGC CNIGDGCQLG PGSLIENAEL 300
    GHGVSVLHSV VCDAKVGNEV AIGPFSHLRP GAGIADQCRI GNFVEIKKSQ 350
    IGEGSKVNHL SYIGDAQLGR HVNVGAGTIT ANYDGVRKHL TVVGDNSKTG 400
    ANSVLVAPIV LGSDVTVGAG STLTKDVPNG ALALGRSKQL IKNGWQ 446
    Length:446
    Mass (Da):47,744
    Last modified:October 1, 2003 - v1
    Checksum:iC53372DB8F81E797
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX548175 Genomic DNA. Translation: CAE20575.1.
    RefSeqiNP_894233.1. NC_005071.1.
    WP_011129779.1. NC_005071.1.

    Genome annotation databases

    EnsemblBacteriaiCAE20575; CAE20575; PMT_0400.
    GeneIDi1729380.
    KEGGipmt:PMT0400.
    PATRICi23008645. VBIProMar135351_0480.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX548175 Genomic DNA. Translation: CAE20575.1 .
    RefSeqi NP_894233.1. NC_005071.1.
    WP_011129779.1. NC_005071.1.

    3D structure databases

    ProteinModelPortali Q7V8F2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 74547.PMT0400.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAE20575 ; CAE20575 ; PMT_0400 .
    GeneIDi 1729380.
    KEGGi pmt:PMT0400.
    PATRICi 23008645. VBIProMar135351_0480.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00113 ; UER00532 .
    UPA00113 ; UER00533 .
    UPA00973 .

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    HAMAPi MF_01631. GlmU.
    InterProi IPR005882. Bifunctional_GlmU.
    IPR001451. Hexapep_transf.
    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.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MIT 9313.

    Entry informationi

    Entry nameiGLMU_PROMM
    AccessioniPrimary (citable) accession number: Q7V8F2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 75 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

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3