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Reviewed, UniProtKB/Swiss-Prot Q7NTY6 (GLND_CHRVO)

Last modified February 9, 2010. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    [Protein-PII] uridylyltransferase
      Short name=PII uridylyl-transferase
    EC=2.7.7.59
Alternative name(s):
    Uridylyl-removing enzyme
    UTase
Gene names
Name: glnD
Ordered Locus Names: CV_2917
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeChromobacterium

Protein attributes

Sequence length856 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Modifies, by uridylylation or deuridylylation the PII (glnB) regulatory protein By similarity. HAMAP MF_00277

Catalytic activity

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

Sequence similarities

Belongs to the glnD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 856856[Protein-PII] uridylyltransferase HAMAP MF_00277
PRO_0000192728

Sequences

Sequence LengthMass (Da)Tools
Q7NTY6-1 [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: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

Cross-references

Sequence databases

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

3D structure databases

SMRQ7NTY6. Positions 59-297, 474-566, 677-850.
ModBaseSearch...

Genome annotation databases

GeneID2548909.
GenomeReviewsGene locus CV_2917 in contig AE016825_GR.
KEGGcvi:CV_2917.
NMPDRfig|243365.1.peg.2917.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG687872.
OMAMQHDLFH.
PhylomeDBQ7NTY6.

Enzyme and pathway databases

BioCycCVIO243365:CV_2917-MONOMER.
BRENDA2.7.7.59. 415.

Family and domain databases

HAMAPMF_00277. PII_uridylyl-transf.
[Tree]
InterProIPR002912. ACT_bd.
IPR010043. GlnD_Uridyltrans.
IPR003607. Metal-dep_PHydrolase_HD_dom.
IPR006674. Metal-dep_PHydrolase_HD_sub.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PANTHERPTHR13734:SF1. GlnD_Uridyltrans. 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.
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 9, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents