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B1MKE4

- B1MKE4_MYCA9

UniProt

B1MKE4 - B1MKE4_MYCA9

Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196)
Status
Unreviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (29 Apr 2008)
      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 annotationSAAS annotation

    Catalytic activityi

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

    Cofactori

    Binds 1 magnesium ion per subunit.UniRule annotationSAAS annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei27 – 271UDP-GlcNAcUniRule annotation
    Binding sitei84 – 841UDP-GlcNAcUniRule annotation
    Metal bindingi115 – 1151MagnesiumUniRule annotation
    Binding sitei152 – 1521UDP-GlcNAc; via amide nitrogenUniRule annotation
    Binding sitei167 – 1671UDP-GlcNAcUniRule annotation
    Binding sitei182 – 1821UDP-GlcNAcUniRule annotation
    Metal bindingi240 – 2401MagnesiumUniRule annotation
    Binding sitei240 – 2401UDP-GlcNAcUniRule annotation
    Binding sitei345 – 3451Acetyl-CoA; amide nitrogenUniRule annotation
    Binding sitei363 – 3631Acetyl-CoAUniRule annotation
    Active sitei375 – 3751Proton acceptorUniRule annotation
    Binding sitei378 – 3781Acetyl-CoAUniRule annotation
    Binding sitei389 – 3891Acetyl-CoAUniRule annotation
    Binding sitei417 – 4171Acetyl-CoAUniRule annotation
    Binding sitei435 – 4351Acetyl-CoA; via amide nitrogenUniRule 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

    AcyltransferaseUniRule annotationSAAS annotation, NucleotidyltransferaseUniRule annotationSAAS annotation, Transferase

    Keywords - Biological processi

    Cell shape, Cell wall biogenesis/degradationUniRule annotationSAAS annotation, Peptidoglycan synthesisUniRule annotationSAAS annotation

    Keywords - Ligandi

    MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation

    Enzyme and pathway databases

    BioCyciMABS36809-WGS:GSQO-1150-MONOMER.
    MABS561007:GJTG-1150-MONOMER.
    UniPathwayiUPA00113; UER00532.
    UPA00113; UER00533.
    UPA00973.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional protein GlmUUniRule annotation
    Gene namesi
    Name:glmUUniRule annotation
    Ordered Locus Names:MAB_1148cImported
    OrganismiMycobacterium abscessus (strain ATCC 19977 / DSM 44196)Imported
    Taxonomic identifieri561007 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium abscessus
    ProteomesiUP000007137: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotationSAAS annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    CytoplasmUniRule annotationSAAS annotation

    Interactioni

    Subunit structurei

    Homotrimer.UniRule annotationSAAS annotation

    Protein-protein interaction databases

    STRINGi561007.MAB_1148c.

    Structurei

    3D structure databases

    ProteinModelPortaliB1MKE4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 242242PyrophosphorylaseUniRule annotationAdd
    BLAST
    Regioni13 – 164UDP-GlcNAc bindingUniRule annotation
    Regioni89 – 902UDP-GlcNAc bindingUniRule annotation
    Regioni113 – 1153UDP-GlcNAc bindingUniRule annotation
    Regioni243 – 26321LinkerUniRule annotationAdd
    BLAST
    Regioni264 – 482219N-acetyltransferaseUniRule annotationAdd
    BLAST
    Regioni398 – 3992Acetyl-CoA bindingUniRule annotation

    Sequence similaritiesi

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

    Keywords - Domaini

    RepeatUniRule annotationSAAS annotation

    Phylogenomic databases

    eggNOGiCOG1207.
    HOGENOMiHOG000283476.
    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. 3 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.

    B1MKE4-1 [UniParc]FASTAAdd to Basket

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    MPGNTAGTAV IVLAAGAGTR MCSDIPKVLH TLGGRSMLAH AVYAAASVNP    50
    EHLVIVLGHE RERIATAVDI LAESLGRRIE IAVQEQQLGT GHAVACGLQA 100
    LPAGFAGTVV VTSGDIPLLD GGTLAGLIGS HTSEPAAATL LTTTLTDPTG 150
    YGRILRTQDR EVIAIVEQTD ATESQRAIGE VNAGVYAFDI EPLHAALSRL 200
    RSNNAQHELY LTDAVSIIRE SGKVVHANHV DDSALVAGVN DRVQLSELGA 250
    ELNRRIIRHH QRNGVTIIDP SSTWIDVDVH IGQDATIAPG TQLHSATVIG 300
    GHCHIGPDTT LIDVTVGDSA TVIRTHGQGS TIGARSVIGP FTYLRPGTVT 350
    GESAKLGAFV EVKNSTVGRG TKVPHLTYVG DADIGEHSNI GASSVFVNYD 400
    GETKRRTVIG SHVKTGSDTM FVAPVTVGDG AYTGAGTVIR EDVPPGALAV 450
    SAGRQRNIEG WVAQKRPGSD AAKAAEEASK GS 482
    Length:482
    Mass (Da):50,002
    Last modified:April 29, 2008 - v1
    Checksum:iDCDD8EB6FB512C09
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU458896 Genomic DNA. Translation: CAM61236.1.
    RefSeqiYP_001701890.1. NC_010397.1.

    Genome annotation databases

    EnsemblBacteriaiCAM61236; CAM61236; MAB_1148c.
    GeneIDi5963672.
    KEGGimab:MAB_1148c.
    PATRICi17973977. VBIMycAbs55940_1185.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU458896 Genomic DNA. Translation: CAM61236.1 .
    RefSeqi YP_001701890.1. NC_010397.1.

    3D structure databases

    ProteinModelPortali B1MKE4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 561007.MAB_1148c.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAM61236 ; CAM61236 ; MAB_1148c .
    GeneIDi 5963672.
    KEGGi mab:MAB_1148c.
    PATRICi 17973977. VBIMycAbs55940_1185.

    Phylogenomic databases

    eggNOGi COG1207.
    HOGENOMi HOG000283476.
    KOi K04042.
    OMAi DCVTNQD.
    OrthoDBi EOG6Z6FQZ.

    Enzyme and pathway databases

    UniPathwayi UPA00113 ; UER00532 .
    UPA00113 ; UER00533 .
    UPA00973 .
    BioCyci MABS36809-WGS:GSQO-1150-MONOMER.
    MABS561007:GJTG-1150-MONOMER.

    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. 3 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. "Acquisition of foreign virulence genes by the cystic fibrosis pathogen Mycobacterium abscessus."
      Genoscope
      Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., Gaillard J.L.
      Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 19977 / DSM 44196Imported.

    Entry informationi

    Entry nameiB1MKE4_MYCA9
    AccessioniPrimary (citable) accession number: B1MKE4
    Entry historyi
    Integrated into UniProtKB/TrEMBL: April 29, 2008
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 51 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzymeUniRule annotationSAAS annotation, Reference proteomeImported

    External Data

    Dasty 3