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B1JBR2 (GLND_PSEPW) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 46. 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:PputW619_4084
OrganismPseudomonas putida (strain W619) [Complete proteome] [HAMAP]
Taxonomic identifier390235 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length900 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 – 900900Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000114758

Regions

Domain481 – 590110HD
Domain706 – 78479ACT 1
Domain816 – 90085ACT 2
Region1 – 342342Uridylyltransferase HAMAP-Rule MF_00277
Region343 – 705363Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
B1JBR2 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: E6F3451AFEC02E74

FASTA900102,914
        10         20         30         40         50         60 
MPQVDPELFD RGQFQAELAL KASPIAAFKK AIRQAGEVLD RRFRDGRDIR RLIEDRAWLV 

        70         80         90        100        110        120 
DNILQQAWKQ FDWGDADGIA LVAVGGYGRG ELHPHSDIDL LILLRDAEHE QYRDAIERFL 

       130        140        150        160        170        180 
TLLWDIGLEV GQSVRTVDEC AEQARADLTV ITNMMESRTI AGREALRQRM LEVTSTAHMW 

       190        200        210        220        230        240 
PSKEFFLAKR AELKARHHKY NDTEYNLEPN VKGSPGGLRD IQTVLWVARR QYGTLNLHAL 

       250        260        270        280        290        300 
AGEGFLLESE NELLASSQDF LWKVRYALHM LAGRAEDRLL FDHQRSIAAL LGYSDENPKR 

       310        320        330        340        350        360 
AIEQFMQQYY RVVMSISQLC DLIIQHFEEV ILADDDSGTT QPLNARFRLH DGYIEAVNAN 

       370        380        390        400        410        420 
VFKRTPFAML EIFVLMAQHP EIKGVRADTV RLLREHRHLI DDTFRNDIRN TSLFIELFKC 

       430        440        450        460        470        480 
EIGIHRNLRR MNRYGILGRY LPEFGLIVGQ MQHDLFHIYT VDAHTLNLIK HLRKLQYTPV 

       490        500        510        520        530        540 
SEKFPLASKL MGRLPKPELI YLAGLYHDIG KGRQGDHSEL GAVDAKKFCE RHQLPAWDSR 

       550        560        570        580        590        600 
LIVWLVQNHL VMSTTAQRKD LSDPQVINDF ALHVGDETRL DYLYVLTVAD INATNPSLWN 

       610        620        630        640        650        660 
SWRASLLRQL YSETKRALRR GLENPLDREE QIRQTQSAAL DILVREGTDP DDVEQLWSQL 

       670        680        690        700        710        720 
GDDYFLKHNA ADVAWHSDAI LQQPADGGPL VLIKETTQRE FEGGTQIFIY APDQHDFFAV 

       730        740        750        760        770        780 
TVAAMSQLNL NIHDARIITS SSQFTLDTYI VLDNDGGSIG DNPQRVKQIR DGLTEALRNP 

       790        800        810        820        830        840 
EDYPTIIQRR VPRQLKHFNF PPQVTILNDA QRAVTILEIT APDRPGLLAR IGRIFLEFDL 

       850        860        870        880        890        900 
SLQNAKIATL GERVEDVFFI TDADNQPLSD PQLCSRLQEA IVQQLQAGQA SDASPTRVTF 

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References

[1]"Complete sequence of Pseudomonas putida W619."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Taghavi S., Vangronsveld D., van der Lelie D., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: W619.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000949 Genomic DNA. Translation: ACA74564.1.
RefSeqYP_001750933.1. NC_010501.1.

3D structure databases

ProteinModelPortalB1JBR2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390235.PputW619_4084.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA74564; ACA74564; PputW619_4084.
GeneID6113053.
KEGGppw:PputW619_4084.
PATRIC19958059. VBIPsePut93764_4107.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycPPUT390235:GHHJ-4146-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_PSEPW
AccessionPrimary (citable) accession number: B1JBR2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: June 11, 2014
This is version 46 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