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Q7NTY6 (GLND_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzyme

Short name=UTase/UR
Alternative name(s):
Bifunctional [protein-PII] modification enzyme
Bifunctional nitrogen sensor protein

Including the following 2 domains:

  1. [Protein-PII] uridylyltransferase
    Short name=PII uridylyltransferase
    Short name=UTase
    EC=2.7.7.59
  2. [Protein-PII]-UMP uridylyl-removing enzyme
    Short name=UR
    EC=3.1.4.-
Gene names
Name:glnD
Ordered Locus Names:CV_2917
OrganismChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757) [Complete proteome] [HAMAP]
Taxonomic identifier243365 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeChromobacterium

Protein attributes

Sequence length856 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00277

Catalytic activity

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. HAMAP-Rule MF_00277

Uridylyl-[protein-PII] + H2O = UMP + [protein-PII]. HAMAP-Rule MF_00277

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00277

Enzyme regulation

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity By similarity. HAMAP-Rule MF_00277

Domain

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 By similarity. HAMAP-Rule MF_00277

Sequence similarities

Belongs to the GlnD family.

Contains 2 ACT domains.

Contains 1 HD domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 856856Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192728

Regions

Domain439 – 551113HD
Domain679 – 76082ACT 1
Domain788 – 85669ACT 2
Region1 – 320320Uridylyltransferase HAMAP-Rule MF_00277
Region321 – 678358Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q7NTY6 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: AFA458E7E1D99AB3

FASTA85697,141
        10         20         30         40         50         60 
MTLSAAPLQH WRQTLAEKRQ QLADAYRADR DAPAFLRRYS QAVDQTLAAL WREQGLDGQA 

        70         80         90        100        110        120 
ALAAVGGYGR GQLFPCSDVD ILILLPDPTP AEINDKVSHF IGLMWDIGLE IGHSVRTLDE 

       130        140        150        160        170        180 
CLREAAGDIT IETNLLENRL VAGPAEPWRE LMRRLEAQRD PLAFFEGKTL EQQQRHTRHF 

       190        200        210        220        230        240 
GVSNNLEPNL KESPGGLRDL HTILWISKAA GLGDNWDSLV RRGILTLAEA RLIKHSEEQL 

       250        260        270        280        290        300 
QKLRVDLHLL ARRREDRLIF DLQQQVAQAW GLADTPAKRA SEQLMQLYFR AAKTVNQLNG 

       310        320        330        340        350        360 
ILLPNLRGRI YCQVPRVTQH ISEYFHAVNG MLGIREVNVF DKHPHAILEA FLTLQRHPEL 

       370        380        390        400        410        420 
SGFAPRMLRA LWHGRSQIND RFRSDPRNRA TFMQIFREPS GLTRTLRRMN LYGILGQYLP 

       430        440        450        460        470        480 
NFGQIVGQMQ HDLFHVYTVD EHILMVVRNL RRFAISAYNH EYPFLSRLIN DFERPEVLYL 

       490        500        510        520        530        540 
AGLFHDIAKG RGGDHSQLGI ADADAFCRDH GLAEEDCQLV AWLVGQHLTM SSIAQKQDIY 

       550        560        570        580        590        600 
DPETVQRFAE LVRTPRRLAA LYLLTVADIR GTSPKVWNTW KAKLLEDLYH ATLRVLSRGG 

       610        620        630        640        650        660 
EIDLASELEA RKNQARAQLR LHAIPDAAEA GLWAQLDTVY FLRHEAKEIA WHARVLNRQL 

       670        680        690        700        710        720 
SPDTPQVRAR LADDHEGLQV LIYSPDKPEL FARACAFFGR TNYSIADAKV YTTRHGYALD 

       730        740        750        760        770        780 
TFHVFVPEHH DGDYRDMINF IEFELAAALA TDQPLQLPPQ GRISRHLKHF PITPQVSIRP 

       790        800        810        820        830        840 
DDKDSDFILS IVAGDRPGLL ARIAKVLADY RLNVRSAKIM TLGGRAEDSF QVSGAALKDD 

       850 
KTALALEAAL ITALRI 

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References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016825 Genomic DNA. Translation: AAQ60585.1.
RefSeqNP_902587.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NTY6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243365.CV_2917.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ60585; AAQ60585; CV_2917.
GeneID2548909.
KEGGcvi:CV_2917.
PATRIC21440572. VBIChrVio67196_2837.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK03059.

Enzyme and pathway databases

BioCycCVIO243365:GHUD-2977-MONOMER.

Family and domain databases

Gene3D1.10.3210.10. 1 hit.
HAMAPMF_00277. PII_uridylyl_transf.
InterProIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
PfamPF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFPIRSF006288. PII_uridyltransf. 1 hit.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsTIGR01693. UTase_glnD. 1 hit.
PROSITEPS51671. ACT. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLND_CHRVO
AccessionPrimary (citable) accession number: Q7NTY6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: December 15, 2003
Last modified: February 19, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families