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Q3IIZ7 (GLND_PSEHT) 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
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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:PSHAa2038
OrganismPseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]
Taxonomic identifier326442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length872 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 – 872872Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231685

Regions

Domain452 – 582131HD
Domain692 – 77382ACT 1
Domain799 – 87274ACT 2
Region1 – 332332Uridylyltransferase HAMAP-Rule MF_00277
Region333 – 691359Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q3IIZ7 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 473147E4F7F35DA0

FASTA872101,049
        10         20         30         40         50         60 
MALPNKVKKL LSDAEQLSDY RDCSSYFYKW LFNEFSKQPV GNLINARAEF IDRLLIKLFH 

        70         80         90        100        110        120 
VYDLAHEPDL ALIAVGGYGR GELHPYSDID FLLLVTQQPN AEISEKIGQF VTMLWDLNLE 

       130        140        150        160        170        180 
IGHSVRTIAQ AIEQKREDVT FATSLLESRL IFGNHIEFEK LKNHIIDTPV WRSNEFFLAK 

       190        200        210        220        230        240 
VQEQHLRHRK CHGTAYNLEP NIKENPGGLR DLQTIIWVAK KHFRAETLQE LISHGYLTHE 

       250        260        270        280        290        300 
EFQELSECLE NLWNIRFALH LAAGRSENRL LFDHQPQAAE ILGFGSDGKS SVERMMKRLF 

       310        320        330        340        350        360 
RIMSRVRELN LMLLAYFEQS ISPKHHQPII QELDRNFERI GNQIKVKSPS VFFRRDQLFM 

       370        380        390        400        410        420 
LFEHIADNPE ITHIYPSTIR TIRQVRRRLL GDLQDYAACR EAFLRLIKHP NGMGRAFTLM 

       430        440        450        460        470        480 
HKHGMLAAYL PQWRNIFGQM QFDLFHAYTV DEHTHRLINN IYQYFDKTGV SEFPICSEIV 

       490        500        510        520        530        540 
TRMDKPELLY LAGIFHDIAK GRGGDHSELG AVDALAFAKL HAFSVADGKL IAWLVSNHLL 

       550        560        570        580        590        600 
MSVTAQRKDI NDPGVIKDFA TRVKTERQLD YLYCLTVADI RATNDNLWND WKNTLLRELY 

       610        620        630        640        650        660 
LHTQHALRLG LENPMDQRDQ IRDKKHQAKQ RLLNLGYMED QIDLIWSRFK ANYFTAFSEQ 

       670        680        690        700        710        720 
QISWHSQHLV NSEDLSQPSV IVSNKAMHGG TQVFVYSPYS GPLFARLVSV IGSKKAQIQH 

       730        740        750        760        770        780 
AQVLTTKDGY VLFNFVILEV NGEPIASGRA QSIKRALEQA LFEPRKKIRF KKNRSQRFKD 

       790        800        810        820        830        840 
FNIKPKIVLR PHPRKDRSLI EIQAIDIPGL LTKIAEVFQA HLLHIHAARI TTVGQRAEDF 

       850        860        870 
FVVSNNEYQA LTDEEQAKIH QALRKKLNAE TE 

« Hide

References

[1]"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125."
Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. expand/collapse author list , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.
Genome Res. 15:1325-1335(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TAC 125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR954246 Genomic DNA. Translation: CAI87094.1.
RefSeqYP_340537.1. NC_007481.1.

3D structure databases

ProteinModelPortalQ3IIZ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326442.PSHAa2038.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI87094; CAI87094; PSHAa2038.
GeneID3708244.
KEGGpha:PSHAa2038.
PATRIC32297675. VBIPseHal105694_1966.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycPHAL326442:GJIU-2090-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_PSEHT
AccessionPrimary (citable) accession number: Q3IIZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 8, 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