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)

Q98C27

- GLND_RHILO

UniProt

Q98C27 - GLND_RHILO

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Rhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Oct 2001)
      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 fixation 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 fixation Source: UniProtKB-HAMAP
    2. regulation of nitrogen utilization Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Nitrogen fixation

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    BioCyciMLOT266835:GJ9L-4157-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:mll5321
    OrganismiRhizobium loti (strain MAFF303099) (Mesorhizobium loti)
    Taxonomic identifieri266835 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium
    ProteomesiUP000000552: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 933933Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192759Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi266835.mll5321.

    Structurei

    3D structure databases

    ProteinModelPortaliQ98C27.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini497 – 596100HDUniRule annotationAdd
    BLAST
    Domaini737 – 81882ACT 1UniRule annotationAdd
    BLAST
    Domaini848 – 92275ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 379379UridylyltransferaseAdd
    BLAST
    Regioni380 – 736357Uridylyl-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.
    HOGENOMiHOG000261779.
    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. 2 hits.
    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.

    Q98C27-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKISLKLDE LIDGEALRRE MTALTTATAG DGSGAAARAG VLQLLKARLA    50
    EGRKIAEAML KEDGGGNACA ERLSHLMDEL IRALYDFAAT HVYRVKNRSS 100
    AERMAVVAVG GYGRGTLAPG SDIDLLFLLP YKQTPWGEQT VEYMLYMLWD 150
    LGLKVGHATR NIDECLRLSR TDITIRTSIL EARFLWGERK LYDELMLRFD 200
    HEVVRTTGPE YVQAKLAERD ERHAKAGESR YLVEPNVKDG KGGLRDLQTL 250
    FWIGKYFYRV RTGEELVEKG VFTEAEYREF QKAEDFLWAV RCHMHFLTGK 300
    AEERLHFDIQ REIAERLGYT THPGLSAVER FMKHYFLVAK DVGDLTRIFC 350
    AALEEEQAKH VPGFNRIFLT FQRRKRKLAG TSDFIVDNHR INIADDQVFE 400
    RDPVNLLRLF WFADKHGLEF HPDALKLLTR SLGLVNKSLR RDEEANRLFL 450
    DILTSDRNAE LNLRRMNEAG LLGRLIPDFG KIVAMMQFSM YHHYTVDEHL 500
    IRCIGVLAEI ERGDGEKVHP LSHSLMPGLK KSREALYVAV LLHDIAKGRP 550
    EDHSEAGARI ARRICPHMGL SAADTETVAW LVENHLAMSM TAQTRDLNDR 600
    KTIEDFASIV QSVERLKLLL VLTVCDIRGV GPGVWNGWKG QLLRTLYYET 650
    ELLLTGGFSE VSRAQRTAAA RERLAEALAD WPDKDRKRYV GLHYENYLLT 700
    VDLPDQLRHA EFVREADAAG KKLATMVKTH QFEAVTEITV LAQDHPRLLS 750
    VIAGACVGAG GNIVDAQIFT TADGRALDTI LISREFDRDE DERRRAERVG 800
    RLIEDVLSGK SWLPEMIEKR TKPKRGAKVF KIPPRAEIRN TLSNRFSVIE 850
    VEGLDRPGLL SEITGTLSDL SLDIASAHIT TFGEKVIDTF YVTDLTGQKI 900
    DSPARIATIR NRLMATLEGI APERGGKAKA AAE 933
    Length:933
    Mass (Da):105,280
    Last modified:October 1, 2001 - v1
    Checksum:i79BF065DAC796FF8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000012 Genomic DNA. Translation: BAB51794.1.
    RefSeqiNP_106008.1. NC_002678.2.
    WP_010913133.1. NC_002678.2.

    Genome annotation databases

    EnsemblBacteriaiBAB51794; BAB51794; BAB51794.
    GeneIDi1228669.
    KEGGimlo:mll5321.
    PATRICi22482678. VBIMesLot2464_4220.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000012 Genomic DNA. Translation: BAB51794.1 .
    RefSeqi NP_106008.1. NC_002678.2.
    WP_010913133.1. NC_002678.2.

    3D structure databases

    ProteinModelPortali Q98C27.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 266835.mll5321.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB51794 ; BAB51794 ; BAB51794 .
    GeneIDi 1228669.
    KEGGi mlo:mll5321.
    PATRICi 22482678. VBIMesLot2464_4220.

    Phylogenomic databases

    eggNOGi COG2844.
    HOGENOMi HOG000261779.
    KOi K00990.
    OMAi LYCLWDM.
    OrthoDBi EOG6CCH44.

    Enzyme and pathway databases

    BioCyci MLOT266835:GJ9L-4157-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. 2 hits.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MAFF303099.

    Entry informationi

    Entry nameiGLND_RHILO
    AccessioniPrimary (citable) accession number: Q98C27
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 2002
    Last sequence update: October 1, 2001
    Last modified: October 1, 2014
    This is version 77 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