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Q3JCX7 (GLND_NITOC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 62. 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:Noc_0806
OrganismNitrosococcus oceani (strain ATCC 19707 / NCIMB 11848) [Complete proteome] [HAMAP]
Taxonomic identifier323261 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeNitrosococcus

Protein attributes

Sequence length892 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 – 892892Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231683

Regions

Domain486 – 598113HD
Domain711 – 78676ACT 1
Domain822 – 89271ACT 2
Region1 – 348348Uridylyltransferase HAMAP-Rule MF_00277
Region349 – 710362Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q3JCX7 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 01DF936D6F5B286B

FASTA892103,332
        10         20         30         40         50         60 
MPNFTGNTRP DPTLFEPAAF AKWIDTSEAP LLLLRSFLKE GIENLKQRFL TGTSAAELLP 

        70         80         90        100        110        120 
LHAWLVDQIL VQACRLHTKK CPERVALVAV GGYGRGTLHP YSDIDILLLL TEETDSILQN 

       130        140        150        160        170        180 
SIGHFISFLW DTGLEMGHSV RTVAECQQAA RDDLSFITSL MEARLLFGPE LLFKNLQTAI 

       190        200        210        220        230        240 
APEQIWNSRQ FFLAKQAEQI TRHHKYHDTA YNLEPNLKEG PGGLRDIQMI QWVSKRYFNT 

       250        260        270        280        290        300 
WSFDSLLQHD FLTVSERKEL LESQSFLWQL RYGLHTLTGR REDRLLFDHQ IALAKQLGYH 

       310        320        330        340        350        360 
DQGPHLAVEQ LMKDYYRTAE NTGRLNEMLL QLLEERILLV DAKVHVRPIN ERFQARNGFL 

       370        380        390        400        410        420 
EVINPSVFKH TPSALLEVFL LLQQHPEIKG VRASTIRLIR EHRHLIDDNF RADSFNRALF 

       430        440        450        460        470        480 
MEIMRQSRGI TRELRRMNKY GILGAYLPVF GKIVGQMQYD MFHAYTVDEH TLFLIHNLRR 

       490        500        510        520        530        540 
FALPKYAQEL PLCSEIFQRI SKPELLYLAG LFHDIAKGRG GDHSKLGAKD ALRFCLYHGL 

       550        560        570        580        590        600 
SRDDSRLVAW LVAHHLLMSM TAQRRDINDP KVIQRFAREV GDERRLNHLY LLTAADIRAT 

       610        620        630        640        650        660 
NPNLWNSWKD ALLNKLYTAT QQALRQGLEY PVDKKEHIRD IQNEARQALL KDGWTEQKLD 

       670        680        690        700        710        720 
ILWSQIDADY FLRHTPNEIR WHIKALAQKE PHDGAPRILV RIHNQEPGTM EVFIYARAHA 

       730        740        750        760        770        780 
LIFTVTTRTM AQLDLDVLDA RIITTGHGFV LESFVVREAA TIRAEADLEF RLQEIQEVLT 

       790        800        810        820        830        840 
QRLTQPDRAP PYRPGFIPRK LKLFKFPTTI TFTKDRRNQC TVMELTTNNW PGLLSRVCRA 

       850        860        870        880        890 
LASCQVRLVN AKITTLGTQV VDVFFICNQQ DKPLTPEQQQ QLKEAIYTYL ER 

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References

[1]"Complete genome sequence of the marine, chemolithoautotrophic, ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707."
Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J., Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T., Vergez L.M., Ward B.B.
Appl. Environ. Microbiol. 72:6299-6315(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19707 / NCIMB 11848.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000127 Genomic DNA. Translation: ABA57319.1.
RefSeqYP_342849.1. NC_007484.1.

3D structure databases

ProteinModelPortalQ3JCX7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323261.Noc_0806.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA57319; ABA57319; Noc_0806.
GeneID3707072.
KEGGnoc:Noc_0806.
PATRIC22705462. VBINitOce57959_0972.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycNOCE323261:GCI3-813-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]
PfamPF08335. 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_NITOC
AccessionPrimary (citable) accession number: Q3JCX7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 8, 2005
Last modified: June 11, 2014
This is version 62 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