Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A1KR65

- GLMU_NEIMF

UniProt

A1KR65 - GLMU_NEIMF

Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei25 – 251UDP-GlcNAcUniRule annotation
    Binding sitei75 – 751UDP-GlcNAcUniRule annotation
    Metal bindingi104 – 1041MagnesiumUniRule annotation
    Binding sitei138 – 1381UDP-GlcNAc; via amide nitrogenUniRule annotation
    Binding sitei153 – 1531UDP-GlcNAcUniRule annotation
    Binding sitei168 – 1681UDP-GlcNAcUniRule annotation
    Metal bindingi226 – 2261MagnesiumUniRule annotation
    Binding sitei226 – 2261UDP-GlcNAcUniRule annotation
    Binding sitei332 – 3321Acetyl-CoA; amide nitrogenUniRule annotation
    Binding sitei350 – 3501Acetyl-CoAUniRule annotation
    Active sitei362 – 3621Proton acceptorUniRule annotation
    Binding sitei365 – 3651Acetyl-CoAUniRule annotation
    Binding sitei376 – 3761Acetyl-CoAUniRule annotation
    Binding sitei404 – 4041Acetyl-CoAUniRule annotation
    Binding sitei422 – 4221Acetyl-CoA; via amide nitrogenUniRule annotation
    Binding sitei439 – 4391Acetyl-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

    BioCyciNMEN272831:GJDX-15-MONOMER.
    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:NMC0015
    OrganismiNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
    Taxonomic identifieri272831 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
    ProteomesiUP000002286: 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 – 456456Bifunctional protein GlmUPRO_1000056175Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272831.NMC0015.

    Structurei

    3D structure databases

    ProteinModelPortaliA1KR65.
    SMRiA1KR65. Positions 5-450.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 228228PyrophosphorylaseUniRule annotationAdd
    BLAST
    Regioni11 – 144UDP-GlcNAc bindingUniRule annotation
    Regioni80 – 812UDP-GlcNAc bindingUniRule annotation
    Regioni102 – 1043UDP-GlcNAc bindingUniRule annotation
    Regioni229 – 24921LinkerUniRule annotationAdd
    BLAST
    Regioni250 – 456207N-acetyltransferaseUniRule annotationAdd
    BLAST
    Regioni385 – 3862Acetyl-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.
    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. 2 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.

    A1KR65-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPQNTLNIVI LAAGKGTRMY SKMPKVLHRI GGKPMLGRVI DTAAALNPQN    50
    ICVVIGHGKD QVLNAVKRDV VWVEQTEQLG TGHAVKTALP HLSAEGRTLV 100
    LYGDVPLIDV KTLKTLLEAA GNEVGLLTDV PADPTGLGRI IRDGNGSVTA 150
    IVEEKDADAA QKAVKEINTG ILVLPNAKLE NWLNSLSSNN AQGEYYLTDL 200
    IAKAVADGIK VHPVQVHTSY LAAGVNNKLQ LAELERIFQT EQAQELLKAG 250
    VTLSDPARFD LRGRLKHGQD VVIDVNCIFE GEVEIGDNVE IGANCVIKNA 300
    KIGANSKIAP FSHLEDCEVG ENNRIGPYAR LRPQAKLAAD VHIGNFVEIK 350
    NAAIGKGTKA NHLTYIGDAE VGSKTNFGAG TIIANYDGVH KHKTVIGNEV 400
    RIGSNCVLVA PVTLGNKVTT GAGSAITRNV EDGKLALARA RQTVIEGWVR 450
    PEKDKQ 456
    Length:456
    Mass (Da):48,683
    Last modified:February 6, 2007 - v1
    Checksum:iD5A1494FBDD3F59B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM421808 Genomic DNA. Translation: CAM09341.1.
    RefSeqiYP_974160.1. NC_008767.1.

    Genome annotation databases

    EnsemblBacteriaiCAM09341; CAM09341; NMC0015.
    GeneIDi4676123.
    KEGGinmc:NMC0015.
    PATRICi20349497. VBINeiMen17609_0022.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM421808 Genomic DNA. Translation: CAM09341.1 .
    RefSeqi YP_974160.1. NC_008767.1.

    3D structure databases

    ProteinModelPortali A1KR65.
    SMRi A1KR65. Positions 5-450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272831.NMC0015.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAM09341 ; CAM09341 ; NMC0015 .
    GeneIDi 4676123.
    KEGGi nmc:NMC0015.
    PATRICi 20349497. VBINeiMen17609_0022.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00113 ; UER00532 .
    UPA00113 ; UER00533 .
    UPA00973 .
    BioCyci NMEN272831:GJDX-15-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. 2 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: ATCC 700532 / DSM 15464 / FAM18.

    Entry informationi

    Entry nameiGLMU_NEIMF
    AccessioniPrimary (citable) accession number: A1KR65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 63 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

    Documents

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

    External Data

    Dasty 3