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A4VJR9 (GLND_PSEU5) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 55. 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:PST_1535
OrganismPseudomonas stutzeri (strain A1501) [Complete proteome] [HAMAP]
Taxonomic identifier379731 [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 fixation 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_1000078809

Regions

Domain462 – 590129HD
Domain706 – 78984ACT 1
Domain816 – 89681ACT 2
Region1 – 342342Uridylyltransferase HAMAP-Rule MF_00277
Region343 – 705363Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
A4VJR9 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 71172F92D9FFEF11

FASTA900102,974
        10         20         30         40         50         60 
MPQVDPELFD RSQFQAELAL KASPIAAYKK AIRQARQVLD ERFRAGRDIR RLIEDRAWFV 

        70         80         90        100        110        120 
DQILRSAWSR FDWDKGADIA LVAVGGYGRG ELHPYSDIDL LILLDENDQE IFREPIEGFL 

       130        140        150        160        170        180 
TLLWDIGLEV GQAVRSVAEC ADEARADLTV ITNLMESRTI AGPERLRQAM LQVTSTQQMW 

       190        200        210        220        230        240 
PSKEFFLAKR NEQRARHAKY NNTEYNLEPN VKGSPGGLRD IQTILWIARR EFGTLNLQAM 

       250        260        270        280        290        300 
VDQGFITEGE HSLLTAAQEF LWKVRYGLHM LAGRAEDRLL FDHQRSLAAL LGYEDSDAKL 

       310        320        330        340        350        360 
AIERFMQKYY RVVMSIAELS DLVGQHFAEV ILWEGESGPI VPLNSRFQVR DGYLEVSNPA 

       370        380        390        400        410        420 
IFKRTPFAIL ETFVLLAQHP DIQGVRSDTI RLLRDHRYLI DDTFRQDLRN TSLFIELFKC 

       430        440        450        460        470        480 
KEGIHRNLRR MNRYGILGRY LPEFGHIVGQ MQHDLFHIYT VDAHTLNVIK YLRKLTKPGV 

       490        500        510        520        530        540 
AEKYPLASKL VEKLPKPELI YIAGLYHDIA KGRGGDHSEL GAVDAEQFCR RHKLPAWDTR 

       550        560        570        580        590        600 
LVVWLVENHL VMSTTAQRKD LSDPQVINDF AQRVGDETHL DYLYVLTVAD INATNPTLWN 

       610        620        630        640        650        660 
SWRASLLRQL YTETKRALKR GLENPLGREE QIRQTQRAAL DDLVRHGTDP DDAEQLWAQL 

       670        680        690        700        710        720 
GDDYFLRHTA TDVAWHTDAI IEHPANGGPL VLIKETTQRE FEGGTQIFIY APDQHDFFAV 

       730        740        750        760        770        780 
TVAAMDQLNL NIHDARILTS SSQFTLDTYI VLEADGSPIG NNPERIEEIR SGLIAALRNP 

       790        800        810        820        830        840 
DDYLTIIQRR VPRQLKHFAF PPQVTIHNDT QRPQTILEII APDRPGLLAR VGQLFLDFDL 

       850        860        870        880        890        900 
SVQNAKIATL GERVEDVFFV TDADNQPLSD PQLCLRLQQA IIKELQQENE QQPSPSSIVI 

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References

[1]"Complete genome sequence of the metabolically versatile and root-associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501."
Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W., Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D., Lin Z., Wang Y. expand/collapse author list , Elmerich C., Lin M., Jin Q.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A1501.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000304 Genomic DNA. Translation: ABP79220.1.
RefSeqYP_001172062.1. NC_009434.1.

3D structure databases

ProteinModelPortalA4VJR9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING379731.PST_1535.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP79220; ABP79220; PST_1535.
GeneID5097620.
KEGGpsa:PST_1535.
PATRIC19963513. VBIPseStu31643_1536.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycPSTU379731:GJER-1534-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_PSEU5
AccessionPrimary (citable) accession number: A4VJR9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 29, 2007
Last modified: June 11, 2014
This is version 55 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