Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q485H4 (GLND_COLP3) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:CPS_1549
OrganismColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) [Complete proteome] [HAMAP]
Taxonomic identifier167879 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia

Protein attributes

Sequence length878 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 – 878878Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192729

Regions

Domain460 – 567108HD
Domain701 – 77979ACT 1
Domain809 – 87870ACT 2
Region1 – 342342Uridylyltransferase HAMAP-Rule MF_00277
Region343 – 700358Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q485H4 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 90026DD7C373EF21

FASTA878101,844
        10         20         30         40         50         60 
MTSHPVSVHI VPSHFINQLA ISADFLSTRD ICQLSQSFNT WLKDVFIEND INDLLSARAV 

        70         80         90        100        110        120 
FVDAILKKLW CQHHLDEFQI TLIAVGGYGR GELHPQSDVD ILLLTQEEVD LELEEKISSF 

       130        140        150        160        170        180 
ITQLWDIKLD IGHSVRSIKE CLKQAVKEVT VATNLMEMRQ VAGNETLTQQ LTPLLSEDVF 

       190        200        210        220        230        240 
WTSEKFFIAK CKEQEARHQQ YRGAAYTLEP NLKANPGGLR DIQTIAWVAK RHFSADSLEE 

       250        260        270        280        290        300 
LVEHDYLYPN EFFELLESQD YLWRMRFALH FVAGRSENRL LFDYQADVAK MMGFGDEGKA 

       310        320        330        340        350        360 
PVERMMKRFF RIIARVTELN TMLLQHFEQA IIKKPELSNI SIINQDFELV DKLINTRNDR 

       370        380        390        400        410        420 
IFMRPVKMIE MFLIIAQEPG IKGIHSHTMR LMRNARRRLI SGLIDYAECR RMFMAIIRHP 

       430        440        450        460        470        480 
RGLGLALTLM HRHSILSSYL PLWRNIAGQM QFDLFHAYSV DEHSYRVIKN LHQFSQKEHN 

       490        500        510        520        530        540 
HKFPLCSKIV QKIRKPEVLY LAGFFHDIGK GRGGDHAKLG AVDALTFCLS HQLSKHDSNM 

       550        560        570        580        590        600 
VAWLVEHHLL MSVTAQRRDI NDENVIRTFG EIVRDEAHLN YLYCLTVADM RGTNESLWNN 

       610        620        630        640        650        660 
WKANLLEELY FNTLSAFRHG LEKPVEVRSK IRENQQQALA LLNENNVDEQ SIKALWREFR 

       670        680        690        700        710        720 
IDYFLRYSPE QIARQCQNIV EHDREKPLVL ISPIPYRGGT EVFIFTKEKN NTFASTVSFL 

       730        740        750        760        770        780 
VTKKLSIHDA KIITTKTGYT VNTFVVLDSR NKPLRERFYT KEMSQALVDR LQQVNICELP 

       790        800        810        820        830        840 
EPKLARHMKK FKVPLRVNFI KIHAKNRTMI EIIALDRPGL LSNISQVFLE ARVNIHSAKI 

       850        860        870 
TTFGEKADDV FTISTEEDDA LTTQEKEALA LRLTQEID 

« Hide

References

[1]"The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses."
Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., Zhou L., Davidsen T.M. expand/collapse author list , Wu M., Huston A.L., Lewis M., Weaver B., Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 34H / ATCC BAA-681.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000083 Genomic DNA. Translation: AAZ26298.1.
RefSeqYP_268291.1. NC_003910.7.

3D structure databases

ProteinModelPortalQ485H4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167879.CPS_1549.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ26298; AAZ26298; CPS_1549.
GeneID3520548.
KEGGcps:CPS_1549.
PATRIC21466307. VBIColPsy94388_1405.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycCPSY167879:GI48-1549-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]
PfamPF01842. ACT. 1 hit.
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_COLP3
AccessionPrimary (citable) accession number: Q485H4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: September 13, 2005
Last modified: June 11, 2014
This is version 64 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