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A5UBF9

- GLND_HAEIE

UniProt

A5UBF9 - GLND_HAEIE

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Haemophilus influenzae (strain PittEE)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (10 Jul 2007)
      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 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

    BioCyciHINF374930:GJDD-668-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:CGSHiEE_03445
    OrganismiHaemophilus influenzae (strain PittEE)
    Taxonomic identifieri374930 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000006555: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 863863Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022344Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi374930.CGSHiEE_03445.

    Structurei

    3D structure databases

    ProteinModelPortaliA5UBF9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini446 – 579134HDUniRule annotationAdd
    BLAST
    Domaini688 – 77285ACT 1UniRule annotationAdd
    BLAST
    Domaini794 – 86370ACT 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 328328UridylyltransferaseAdd
    BLAST
    Regioni329 – 687359Uridylyl-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.
    OMAiHHLLMSV.
    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.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view]
    PfamiPF01842. ACT. 2 hits.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 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.

    A5UBF9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLFPLSLSSP LTPSAVKIER ENLKQFELEN FSRYSIFELV ENRSDFYDAL    50
    LIQLWQEMGL SEQLGISLIA VGGYGRREMF PLSDLDFLIL VEQTPIPEIE 100
    EKITQFIQFL WDCGFEVGHS VRTLQQCESE GKQDITIATN LLEARFLIGN 150
    RPHFDALNEL VKRADFWSKE GFFNAKVQEQ IERYQRYHNT AYNLEPDIKY 200
    SPGGLRDLHL LYWVALHHSG AQTLEDILQS GFIYPQEYQQ LQESRAFLFK 250
    VRFALHLILT RYDNRLLFDR QIKVSELLGF RGEGNQAVEK MMKCFFQALH 300
    RISLISNLLI QHYRENVLSS NQATVIEQLD DDFQLINQCL CLRNSLVFQE 350
    KPARILDLFF YLTQYEQANI HSDTLRQLQI SLEQLPQKLC EIPEAREKFL 400
    RLFNQPNSIK RAFMPMHQYG VLTAYLPQWQ AIEGLMQFDL FHIYTVDEHT 450
    LRVMLKLESF LSQESAQEHP IAHRIFSQLS DRTLLYIAAL FHDIAKGRGG 500
    DHAELGAKDV ANFARLHGLD RREIDTLAWL VQSHLLMSIT AQRRDIHDPE 550
    VVMNFAEAVQ NQVRLDYLTC LTVADICATN GNLWNSWKRS LFASLYEFTE 600
    QQFAQGMKEL LDYSEKSAEN RKLAQQILTQ DYSDIMPISI DQLWERCPED 650
    YFVRNTPKQI AWHTSLLVDL VEALLVKISN RFSLGGTEVF IYCQDQPHLF 700
    NKVVSTIGAK KFSIHDAQII TTQDGYVFDS FIITELNGEL VEFDRRRELE 750
    QALTLALQSE KLSALSITPN RQLQHFTVQT DVRFLHENKK EHTEMELVAL 800
    DKAGLLAQVS QIFSELNLNL LNAKITTVGE KAEDFFILTN QFGQALDSQQ 850
    REILRNVLYR NIG 863
    Length:863
    Mass (Da):100,197
    Last modified:July 10, 2007 - v1
    Checksum:iFBC5A42D0FFB0B92
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000671 Genomic DNA. Translation: ABQ98110.1.
    RefSeqiYP_001290493.1. NC_009566.1.

    Genome annotation databases

    EnsemblBacteriaiABQ98110; ABQ98110; CGSHiEE_03445.
    GeneIDi5225241.
    KEGGihip:CGSHiEE_03445.
    PATRICi20277493. VBIHaeInf81350_0696.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000671 Genomic DNA. Translation: ABQ98110.1 .
    RefSeqi YP_001290493.1. NC_009566.1.

    3D structure databases

    ProteinModelPortali A5UBF9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 374930.CGSHiEE_03445.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ98110 ; ABQ98110 ; CGSHiEE_03445 .
    GeneIDi 5225241.
    KEGGi hip:CGSHiEE_03445.
    PATRICi 20277493. VBIHaeInf81350_0696.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci HINF374930:GJDD-668-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.
    IPR013546. PII_UdlTrfase/GS_AdlTrfase.
    [Graphical view ]
    Pfami PF01842. ACT. 2 hits.
    PF08335. GlnD_UR_UTase. 1 hit.
    PF01966. HD. 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. "Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
      Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
      Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PittEE.

    Entry informationi

    Entry nameiGLND_HAEIE
    AccessioniPrimary (citable) accession number: A5UBF9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 55 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3