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A4XWU3 (GLND_PSEMY) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 54. 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:Pmen_3055
OrganismPseudomonas mendocina (strain ymp) [Complete proteome] [HAMAP]
Taxonomic identifier399739 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length899 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 – 899899Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000059224

Regions

Domain488 – 56881HD
Domain706 – 78479ACT 1
Domain816 – 89782ACT 2
Region1 – 342342Uridylyltransferase HAMAP-Rule MF_00277
Region343 – 705363Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
A4XWU3 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 6154CE68B882E4DF

FASTA899102,887
        10         20         30         40         50         60 
MPQMDPELFD RGQFQAELAL KSSPIAAFKK AIRHAREVLD ARFKGGRDIR RLVEDRAWFV 

        70         80         90        100        110        120 
DQILQEAWKR FAWSEDADIA LLAVGGYGRG ELHPYSDIDL LILLDSSDHE IFREPIEGFL 

       130        140        150        160        170        180 
TLLWDIGLEV GQSVRSVDEC AEEARADLTV ITNLMESRTI AGPEHLRQRM QQVTSSEQMW 

       190        200        210        220        230        240 
PSKHFYLAKR EERKARHAKY NDTEYNLEPN VKGSPGGLRD IQTVLWVARR QFGTLNLQAL 

       250        260        270        280        290        300 
VGQGFLLESE YALLSSSQEF LWKVRYALHM LAGRAEDRLL FDYQARIAAL FGYQDGDGKR 

       310        320        330        340        350        360 
SIEHFMQKYY RVVMGISELS DLINQHFEEV ILRAGESGPA TPLNSRFQVR DGYIEVTHPN 

       370        380        390        400        410        420 
VFKRTPFAIL EVFVLMAQNP EIKGVRADSI RLLRDSRHLI DDDFRKDIRN TSLFIELFKC 

       430        440        450        460        470        480 
KEGIHRNLRR MNRYGILGRY LPEFGHIVGQ MQHDLFHIYT VDAHTLNLIK HLRKFRWPEL 

       490        500        510        520        530        540 
AEKFPLASKL IDRLPKPELI YLAGLYHDIG KGRGGDHSEL GAVDAEAFAR RHQLPAWDSA 

       550        560        570        580        590        600 
LIVWLVQHHL VMSTTAQRKD LSDPQVIHDF AQFVGDQTHL DYLYVLTVAD INATNPSLWN 

       610        620        630        640        650        660 
SWRASLLRQL YTETKRALRR GLENPLDREE QIRQTQSAAL DILVRGGTDP DDAEQLWSQL 

       670        680        690        700        710        720 
GDDYFLRHTA NDVAWHTEAI LQHPADSGPL VLIKETTQRE FEGGTQIFIY APDQHDFFAV 

       730        740        750        760        770        780 
TVAAMSQLNL NIHDARIITS TSQFTLDTYV VLDADGGSIG DNPARIKQIR EGLIEALKNP 

       790        800        810        820        830        840 
DEYPTIIQRR VPRQLKHFAF APQVTIHNDA QRPVTILELT APDRPGLLAR IGRIFLEYDL 

       850        860        870        880        890 
SLQNAKIATL GERVEDVFFV TDANNQPLSD PELCARLQET IVRRLSEPSA QPQSLQIDI 

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References

[1]"Complete sequence of Pseudomonas mendocina ymp."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Hersman L., Dubois J., Maurice P., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ymp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000680 Genomic DNA. Translation: ABP85809.1.
RefSeqYP_001188541.1. NC_009439.1.

3D structure databases

ProteinModelPortalA4XWU3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399739.Pmen_3055.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP85809; ABP85809; Pmen_3055.
GeneID5107535.
KEGGpmy:Pmen_3055.
PATRIC19912722. VBIPseMen131592_3101.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycPMEN399739:GHR6-3114-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_PSEMY
AccessionPrimary (citable) accession number: A4XWU3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: June 11, 2014
This is version 54 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