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Q4FUP5 (GLND_PSYA2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:Psyc_0395
OrganismPsychrobacter arcticus (strain DSM 17307 / 273-4) [Complete proteome] [HAMAP]
Taxonomic identifier259536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length915 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 – 915915Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231688

Regions

Domain498 – 58891HD
Domain732 – 81786ACT 1
Domain840 – 91576ACT 2
Region1 – 360360Uridylyltransferase HAMAP-Rule MF_00277
Region361 – 731371Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q4FUP5 [UniParc].

Last modified August 30, 2005. Version 1.
Checksum: 68837CAE3D605366

FASTA915104,846
        10         20         30         40         50         60 
MFNCAVTAID LTPMPLLSTD NMTTAPLSLS TDTSLIEKSL FGIPEWLLQI NDDISRALER 

        70         80         90        100        110        120 
GVNIRQLVSA RACVIDDLLI GLFKWFELDK TDLALFATGG YGRGELSLHS DIDILLLMPH 

       130        140        150        160        170        180 
EIDADTSSKI DNLVALLWDI GLEPALSVRS VSECLEAALD HTIASALLEA RLLIGNETLQ 

       190        200        210        220        230        240 
DVPHQIVNNQ WSPRAFYDVK IDEAKARYLQ HNATEYNLEP NIKTAPGGLR DIHIVGWVTK 

       250        260        270        280        290        300 
RYFRVSKLYD LVQQNFLTEK EFDELSFSEG YLWQIRHYLH ELTGRNENKL LFDYQREIAQ 

       310        320        330        340        350        360 
LMGYDTQPDD QPNAAVERFM RDYYRCAMQI STLSEMLTNH YYETIIEPQL PDEERPKKQP 

       370        380        390        400        410        420 
INARFNQVGE QIAMAHHRVF AQHPESILEM FLLMGQYGIK NVRTHTLRAL KIAARGIDQA 

       430        440        450        460        470        480 
YRDNPTHQTL FLANLKEQNY LFHRLRTMNR YGVLGNYIPA FAQVTGLMQY DLFHRYTVDA 

       490        500        510        520        530        540 
HTLFLIRILH RFIDPHFYED FPLVSSIFQR IERKEILVLA AMFHDIAKGR GGNHSQLGEI 

       550        560        570        580        590        600 
ESIEFCLAHG MSNADANLVG WLTRYHLLMS MTAQKKDISD PEVVTLFADL VGNVTHLNHL 

       610        620        630        640        650        660 
YVLTVADMNA TNPQLWNSWR ATLMKQLYSQ TRRILRADID APTNRQDMIS ATRKQALMML 

       670        680        690        700        710        720 
DNVDNQHMNR DEVLSLWDDL GDEYFLREIA EDILWHTEAI LNHPPIGRAS NADSPPLVVL 

       730        740        750        760        770        780 
REHRELALDA VQVFVYTQDQ VNLFAVTMAV FDQMNLDVLD ARIITATRDF ALDSYVLLDR 

       790        800        810        820        830        840 
SGTLLVDSDS QQELKQRLID AFKNPTAPKL THKRIPRQLK HFDVETTINF EFNDASSQHI 

       850        860        870        880        890        900 
MSLETLDQPG LLARVGQVFL QQQIEVHAAR ITTLGERAED MFYISDQNDQ ALSANKLKTL 

       910 
KTALIESLSV HNDSI 

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References

[1]"The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17307 / 273-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000082 Genomic DNA. Translation: AAZ18263.1.
RefSeqYP_263697.1. NC_007204.1.

3D structure databases

ProteinModelPortalQ4FUP5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING259536.Psyc_0395.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ18263; AAZ18263; Psyc_0395.
GeneID3514133.
KEGGpar:Psyc_0395.
PATRIC23055115. VBIPsyArc98534_0490.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPARC259536:GI3A-410-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_PSYA2
AccessionPrimary (citable) accession number: Q4FUP5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: August 30, 2005
Last modified: February 19, 2014
This is version 61 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