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Q53245

- GLND_RHITR

UniProt

Q53245 - GLND_RHITR

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Rhizobium tropici
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    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-KW
    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

    BioCyciRETL1328306-WGS:GSTH-393-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
    OrganismiRhizobium tropici
    Taxonomic identifieri398 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 948948Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192761Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ53245.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini490 – 603114HDUniRule annotationAdd
    BLAST
    Domaini729 – 81082ACT 1UniRule annotationAdd
    BLAST
    Domaini840 – 92182ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 372372UridylyltransferaseAdd
    BLAST
    Regioni373 – 728356Uridylyl-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.

    Q53245-1 [UniParc]FASTAAdd to Basket

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    METHHIDFST VLDVSALKAE CEALAKRGLD KNEERSALLA LLKKASQDGR    50
    EEARRLLIAD GSGLNCAHRI SWLQDQIITV LYDLTVHHAY PKQAGVFSVT 100
    AVGGYGRDTL APGSDIDLLF LFQPKPASET HKAVEFILYM LWDMGFKVGH 150
    ATRSVEECIR EAKSDMTVRT AILETRYICG NVALERELQA RFDKEIVTNT 200
    GPEFIAAKLA ERDERHRKAG DTRYLVEPNV KEGKGGLRDL HTLFWISKYY 250
    YHVRDPAELV KLGVLSKQEY RLFEKAEDFL WAVRCHMHFL TGKAEERLSF 300
    DIQRDIAAAL DYNARPGLSA VERFMKHYFL VAKDVGDLTR ILCAALEDQQ 350
    AKATPGLTGV ISRFANRSRK IPGTVEFVED RGRIALANPD VFKRDPVSLI 400
    RLFFVADING LEFHPDALKR VTRSLSLIDN DLRENEEANR LFLSILTSKR 450
    DPALILRRMN EAGVLGRFIP EFGKIVSMMQ FNMYHHYTVD EHLIRAVEVL 500
    SEIDKGRAED IHPLTNKLMP NIEDRDALYV AVLLHDIAKG REEDHSEAGA 550
    AVARKLCPRF GLSPKQTELV VWLIAEHLTM SMVAQTRDLT DRKTIIDFAD 600
    RVQSLDRLKM LLILTVCDIR AVGPGVWNGW KGQLLRTLYY ETELLLSGGF 650
    SEVSRKERAE AAAEALEHAL ADWSQKERKA YVKLHYQPYL LSVPLEDQIR 700
    HTQFMRESDK AGKVLATMVR TDSFHAITEI TVLSPDHPRL LTVIAGACAA 750
    AGANIADAQI FTTSDGRALD TIHVSREFPD DADELRRAAT IGKMIEDVLA 800
    GRKRLPEVIA TRTKNRRKNK AFVIPPSVII TNSLSNKFTV IEVECLDRPG 850
    LLSEITAVLS DLSLDIQSAR ITTFGEKVID TFYVADLVGQ KISNENRRAY 900
    ITARLKAVMA GEEDEMRERM PSGIIAPAAT RGVAVEKSDT EKKAGSAA 948
    Length:948
    Mass (Da):106,423
    Last modified:May 30, 2000 - v2
    Checksum:i9CCE1A43545213BD
    GO

    Sequence cautioni

    The sequence AAC32290.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U47030 Genomic DNA. Translation: AAC32290.1. Different initiation.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U47030 Genomic DNA. Translation: AAC32290.1 . Different initiation.

    3D structure databases

    ProteinModelPortali Q53245.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci RETL1328306-WGS:GSTH-393-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. O'Connell K.P., Raffel S.J., Saville B.J., Handelsman J.
      Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CIAT899.

    Entry informationi

    Entry nameiGLND_RHITR
    AccessioniPrimary (citable) accession number: Q53245
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 76 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