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Q9RAE4

- GLND_RHILV

UniProt

Q9RAE4 - GLND_RHILV

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Rhizobium leguminosarum bv. viciae
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 2 (08 Dec 2000)
      Previous versions | rss
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    Functioni

    Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, 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 likely 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 metabolism.1 Publication

    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 likely activates uridylyl-removing (UR) activity.1 Publication

    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

    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
    OrganismiRhizobium leguminosarum bv. viciae
    Taxonomic identifieri387 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

    Pathology & Biotechi

    Disruption phenotypei

    Deletions in the 5'-region of this gene appear to be lethal. Insertion mutations in the central part of this gene abolishes the ability to use nitrate as a sole nitrogen source but not glutamine. In addition, neither uridylylation of PII nor induction of the ntr-regulated glnII gene (encoding glutamine synthetase II) under ammonium deficiency can be observed in mutant strains.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 944944Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192758Add
    BLAST

    Expressioni

    Inductioni

    Is constitutively expressed, irrespective of the nitrogen content of the medium.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ9RAE4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini488 – 602115HDUniRule annotationAdd
    BLAST
    Domaini728 – 80982ACT 1UniRule annotationAdd
    BLAST
    Domaini839 – 91880ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 371371UridylyltransferaseAdd
    BLAST
    Regioni372 – 727356Uridylyl-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

    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.

    Q9RAE4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRDLDFTNIL DVELLQKQCD AVAEANRNRP DVLRADLLAV LKKASTEGRQ    50
    KAREALMADG GGLNCAYRIS WLQDQITTVL YNFATAHIFP QQKDKFAVTA 100
    VGGYGRDTLA PGSDIDLLFL FLPRPAEETH KAVEFMLYVL WDMGFKVGHA 150
    TRTVEECIAL SKSDMTIRTA ILEMRYICGL QRLETELETR FDKEIVTGTG 200
    PEFIAAKLAE RDERHRKAGD TRYLVEPNVK EGKGGLRDLH TLFWISKYYY 250
    HVRDQAELVK LGVLSKHEYR LLEKADDFLW AVRCHMHFLT GKAEERLSFD 300
    IQREIAEAFG YHTRPGLSAV ERFMKHYFLV AKDVGDLTRI LCAALEDQQA 350
    KSIPGLTGVI SRFTHRNRKI AGSVEFVEDR GRIALADPEV FKRDPVNIIR 400
    LFHVADINGL EFHPDALKRV TRSLALIDNA LRENDEANRL FMSILTSKRD 450
    PALILRRMNE AGVLGRFIPE FGKIVAMMQF NMYHHYTVDE HLIRTVDILS 500
    EIDKGRAEDL HPLANKLMPG IEDREALYVA VLLHDIAKGR QEDHSIAGAR 550
    VARKLCVRFG LSQKQTEIVV WLIEEHLTMS MVAQTRDLTD RKTITDFADR 600
    VQSLDRLKML LILTICDIRA VGPGVWNGWK GQLLRTLYYE TELLLAGGFS 650
    EVSRKERANA AAEALHSALA DWSQKDRNTY TKLHYQPYLL SVPLEDQIRH 700
    AHFIRQADKA GQALATMVRT DSFHAITEIT VLSPDHPRLL AVIAGACAAA 750
    GANIVDAQIF TTSDGRALDT IHVSREFTDD ADELRRAATI GRMIEDVLSG 800
    RKRLPEVIAT RARNRKKSKA FVIPPSVNIT NSLSNKFTVI EVECLDRPGL 850
    LSEITAVLSD LSLDIQSARI TTFGEKVIDT FYVTDLVGQK ISGDSKRANI 900
    TARMKAVMAE EEDELRERMP SGIIAPAATA RTPPASEKKA GSPI 944
    Length:944
    Mass (Da):106,218
    Last modified:December 8, 2000 - v2
    Checksum:iB164E74FF9E6DF2E
    GO

    Sequence cautioni

    The sequence AAF17352.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF155830 Genomic DNA. Translation: AAF17352.1. Different initiation.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF155830 Genomic DNA. Translation: AAF17352.1 . Different initiation.

    3D structure databases

    ProteinModelPortali Q9RAE4.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "The Rhizobium leguminosarum bv. viciae glnD gene, encoding a uridylyltransferase/uridylyl-removing enzyme, is expressed in the root nodule but is not essential for nitrogen fixation."
      Schluter A., Nohlen M., Kramer M., Defez R., Priefer U.B.
      Microbiology 146:2987-2996(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION, INDUCTION, DISRUPTION PHENOTYPE.
      Strain: VF39.

    Entry informationi

    Entry nameiGLND_RHILV
    AccessioniPrimary (citable) accession number: Q9RAE4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: December 8, 2000
    Last modified: October 1, 2014
    This is version 68 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3