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)

Q5NZH8

- GLND_AROAE

UniProt

Q5NZH8 - GLND_AROAE

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (04 Jan 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.UniRule annotation

    Catalytic activityi

    UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].UniRule annotation
    Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].UniRule annotation

    Cofactori

    Magnesium.UniRule annotation

    Enzyme regulationi

    Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity.UniRule annotation

    GO - Molecular functioni

    1. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
    2. amino acid binding Source: InterPro
    3. metal ion binding Source: InterPro
    4. phosphoric diester hydrolase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. nitrogen compound metabolic process Source: InterPro
    2. regulation of nitrogen utilization Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase, Nucleotidyltransferase, Transferase

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    BioCyciAARO76114:GJTA-3463-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
    Short name:
    UTase/URUniRule annotation
    Alternative name(s):
    Bifunctional [protein-PII] modification enzymeUniRule annotation
    Bifunctional nitrogen sensor proteinUniRule annotation
    Including the following 2 domains:
    [Protein-PII] uridylyltransferaseUniRule annotation (EC:2.7.7.59UniRule annotation)
    Short name:
    PII uridylyltransferaseUniRule annotation
    Short name:
    UTaseUniRule annotation
    [Protein-PII]-UMP uridylyl-removing enzymeUniRule annotation (EC:3.1.4.-UniRule annotation)
    Short name:
    URUniRule annotation
    Gene namesi
    Name:glnDUniRule annotation
    Ordered Locus Names:AZOSEA34110
    ORF Names:ebA5982
    OrganismiAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1))
    Taxonomic identifieri76114 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum
    ProteomesiUP000006552: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 862862Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192715Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi76114.ebA5982.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5NZH8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini448 – 553106HDUniRule annotationAdd
    BLAST
    Domaini686 – 76580ACT 1UniRule annotationAdd
    BLAST
    Domaini794 – 86269ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 328328UridylyltransferaseAdd
    BLAST
    Regioni329 – 685357Uridylyl-removingAdd
    BLAST

    Domaini

    Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.UniRule annotation

    Sequence similaritiesi

    Belongs to the GlnD family.UniRule annotation
    Contains 2 ACT domains.UniRule annotation
    Contains 1 HD domain.UniRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG2844.
    HOGENOMiHOG000261778.
    KOiK00990.
    OMAiLYCLWDM.
    OrthoDBiEOG6CCH44.

    Family and domain databases

    Gene3Di1.10.3210.10. 1 hit.
    HAMAPiMF_00277. PII_uridylyl_transf.
    InterProiIPR002912. ACT_dom.
    IPR010043. GlnD_Uridyltrans.
    IPR003607. HD/PDEase_dom.
    IPR006674. HD_domain.
    IPR002934. Nucleotidyltransferase.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view]
    PfamiPF01842. ACT. 1 hit.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 1 hit.
    PF01909. NTP_transf_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006288. PII_uridyltransf. 1 hit.
    SMARTiSM00471. HDc. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01693. UTase_glnD. 1 hit.
    PROSITEiPS51671. ACT. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5NZH8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTAAIPTDA AVQAAIAEAR ARLADGSMRI RMAYEGHPAT STVLKGRAHL    50
    VDETIHRLWR ACAMPADVAL LAVGGYGRGE LFPCSDVDLM VLLPDTADDA 100
    MQARLSVLLG ALWDVGLEIG HSARTVAEAI DAAEQDITVQ TNLLESRLLE 150
    GNRPLFEEFC RRYRALLDVR VFFKAKQLEQ EKRYARYNDT PYALEPNCKE 200
    SPGGLRDLQM LGWIARAAGL GRNWRDLARR RLITGAEARD LRSIERFLQH 250
    VRIRLHYLTG RSEDRLLFDY QERLASALGI EATAAKRASE VFMQRYYVNA 300
    KKVTQTNTIL LQNYGVEIFP RRAGAAIVIN ERFQAVRELL DMREDDTFAR 350
    HPSALLECFL ILQQRSELKG MTARTLRALW LNRKRINAAF RADPHNRELF 400
    VAILQQKRGI VHEFRRMNQY GILSGYLPSW RRIVGQMQHD LFHVYTVDQH 450
    IMMVLRNMRR FTMGEHAHEY PLMAQLIMAF DRHWLLYVAA LFHDIAKGRG 500
    GDHSKLGTID AREFCEHHHL AREDADLVVW LVEHHLTMSH VAQKEDTSDP 550
    AVIGRFADTV GTERRLTALY LLTHADIRGT SPKVWNGWKG KLLEDLFFAT 600
    RRLLRGATPQ EALGLDDRQE NARALLRYHG LRPGVEDALW AQLDAVYFMR 650
    HSAEEIAWHS RTLYYRPDAL EPVVKARVSD ADQGVQVMVF TRDQKDLFVR 700
    LTGFFGRLGF SILDAKVHTT RHGYALDSFM LQDPGNAEHY RDVITLIEHE 750
    LTERLKKSAP PDRPSAGRLS RQVKHFPITP RVSILPDESG RHYILSLTAA 800
    DRRGLLFAVA EVLAQNGIVL HTAKIATLGE RVEDTFLLSG NGLSQDARVV 850
    KIERELLQRL HI 862
    Length:862
    Mass (Da):98,195
    Last modified:January 4, 2005 - v1
    Checksum:iFA31DCA7E434257E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR555306 Genomic DNA. Translation: CAI09536.1.
    RefSeqiYP_160437.1. NC_006513.1.

    Genome annotation databases

    EnsemblBacteriaiCAI09536; CAI09536; ebA5982.
    GeneIDi3179129.
    KEGGieba:ebA5982.
    PATRICi20973043. VBIAroAro98752_3439.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR555306 Genomic DNA. Translation: CAI09536.1 .
    RefSeqi YP_160437.1. NC_006513.1.

    3D structure databases

    ProteinModelPortali Q5NZH8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 76114.ebA5982.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAI09536 ; CAI09536 ; ebA5982 .
    GeneIDi 3179129.
    KEGGi eba:ebA5982.
    PATRICi 20973043. VBIAroAro98752_3439.

    Phylogenomic databases

    eggNOGi COG2844.
    HOGENOMi HOG000261778.
    KOi K00990.
    OMAi LYCLWDM.
    OrthoDBi EOG6CCH44.

    Enzyme and pathway databases

    BioCyci AARO76114:GJTA-3463-MONOMER.

    Family and domain databases

    Gene3Di 1.10.3210.10. 1 hit.
    HAMAPi MF_00277. PII_uridylyl_transf.
    InterProi IPR002912. ACT_dom.
    IPR010043. GlnD_Uridyltrans.
    IPR003607. HD/PDEase_dom.
    IPR006674. HD_domain.
    IPR002934. Nucleotidyltransferase.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view ]
    Pfami PF01842. ACT. 1 hit.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 1 hit.
    PF01909. NTP_transf_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006288. PII_uridyltransf. 1 hit.
    SMARTi SM00471. HDc. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01693. UTase_glnD. 1 hit.
    PROSITEi PS51671. ACT. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
      Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
      Arch. Microbiol. 183:27-36(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: EbN1.

    Entry informationi

    Entry nameiGLND_AROAE
    AccessioniPrimary (citable) accession number: Q5NZH8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 71 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3