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Q1QDM9 (GLND_PSYCK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:Pcryo_0441
OrganismPsychrobacter cryohalolentis (strain K5) [Complete proteome] [HAMAP]
Taxonomic identifier335284 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length913 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 – 913913Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000022352

Regions

Domain479 – 586108HD
Domain730 – 81586ACT 1
Domain838 – 91376ACT 2
Region1 – 358358Uridylyltransferase HAMAP-Rule MF_00277
Region359 – 729371Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q1QDM9 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 1E1118BBFD987E10

FASTA913104,638
        10         20         30         40         50         60 
MFNCDVTAID LTPMPLFSAD NMTTAFLSTD TSVVEKSLFG IPEWLLQIND DISRALERGV 

        70         80         90        100        110        120 
NIRQLVSARA CVIDDLLIEL FKCFGLDKTD LALFATGGYG RGELSLHSDI DILLLMPHDI 

       130        140        150        160        170        180 
NADTSSKIDN LVALLWDIGL EPALSVRSVS DCLEAALDHT IASALLEARL LIGNDALQNV 

       190        200        210        220        230        240 
PHQIVNNQWS PRSFYDVKID EAKARYLQHN ATEYNLEPNI KTAPGGLRDI HIIGWVTKRY 

       250        260        270        280        290        300 
FRVSKLYDLV QQNFLTEKEF DELSFSENYL WQIRHYLHEL TGRNENKLLF DYQREIAQLM 

       310        320        330        340        350        360 
GYDTQTDDQP NAAVERFMRD YYRCAMQIST LSEMLTNHYY ETIIEAQLPD EERPKKQPIN 

       370        380        390        400        410        420 
ARFNQVGDQI AMAHHRVFAQ HPESILEMFL LMGQYGIKNV RTHTLRALKI AARGIDQAYR 

       430        440        450        460        470        480 
DNPTHQTLFL ANLKEQNYLF HRLRTMNRYG VLGNYIPAFA QVTGLMQYDL FHRYTVDAHT 

       490        500        510        520        530        540 
LFLIRILHRF TDPHFYEDFP LVSSIFQRIE RKEILVLAAM FHDIAKGRGG NHSQLGEIES 

       550        560        570        580        590        600 
IEFCLAHGMS TADANLVGWL TRYHLLMSMT AQKKDISDPE VVTLFADLVG NVTHLNHLYV 

       610        620        630        640        650        660 
LTVADMNATN PQLWNSWRAT LMKQLYSQTR RILRADIDAP TNRQDMISAT RKQALVMLDN 

       670        680        690        700        710        720 
VDNQHMNRDE VLRLWDDLGD EYFLREIAED ILWHTEAILN HPPIGRASNA DSPPLVVLRE 

       730        740        750        760        770        780 
HRELALDAVQ VFVYTQDQVN LFAVTMAVFD QMNLDVLDAR IITATRDFAL DSYVLLDRSG 

       790        800        810        820        830        840 
TLLVDSDSQQ ELKQRLIDAF KNPTAPKLTH KRIPRQLKHF DVATTINFDF NDASNQHIMS 

       850        860        870        880        890        900 
LETLDQPGLL ARVGQVFLQQ QIEVHAARIT TLGERAEDMF YISDQNDQAL SADKLKTLKT 

       910 
ALIDSLSVRN DRV 

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References

[1]"Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000323 Genomic DNA. Translation: ABE74224.1.
RefSeqYP_579708.1. NC_007969.1.

3D structure databases

ProteinModelPortalQ1QDM9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335284.Pcryo_0441.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE74224; ABE74224; Pcryo_0441.
GeneID4034059.
KEGGpcr:Pcryo_0441.
PATRIC23060331. VBIPsyCry128170_0505.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBCLSK830629.

Enzyme and pathway databases

BioCycPCRY335284:GHE9-456-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. 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_PSYCK
AccessionPrimary (citable) accession number: Q1QDM9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: February 19, 2014
This is version 60 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