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P36223 (GLND_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 72. 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
Synonyms:nfrX
OrganismAzotobacter vinelandii
Taxonomic identifier354 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length899 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Modifies, by uridylylation and deuridylylation, the PII regulatory protein GlnK, 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 protein 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 protein, and plays an important role in the regulation of nitrogen fixation and metabolism. Ref.1 Ref.2

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

Disruption phenotype

Cells lacking this gene are not viable unless a second mutation occurs, either spontaneously or by design, resulting in the inability of glutamine synthetase (GS) to be adenylylated. Ref.2

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_0000192717

Regions

Domain486 – 590105HD
Domain706 – 78984ACT 1
Domain816 – 89984ACT 2
Region1 – 342342Uridylyltransferase HAMAP-Rule MF_00277
Region343 – 705363Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
P36223 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 96AF63BC5EDE3C9D

FASTA899102,580
        10         20         30         40         50         60 
MPQVDPDLFD PGQFQAELAL KSSPIPAYKK ALRCAREVLD ARFQEGRDIR RLIEDRAWFV 

        70         80         90        100        110        120 
DQILALAWNR FDWSEDADIA LIAVGGYGRG ELHPYSDIDL LILMDGADHE VFREPIEGFL 

       130        140        150        160        170        180 
TLLWDIGLEV GQSVRSLAEC AEEAQADLTV ITNLMESRTI AGPEHLRQRM QEVTSAQRMW 

       190        200        210        220        230        240 
PSRAFFLAKR DEQKTRHARY NDTEYNLEPN VKGSPGGLRD IQTLLWIARR QFGTINLHAM 

       250        260        270        280        290        300 
VGQGFLLESE YTLLASSQEF LWKVRYALHM LAGRAEDRLL FDLQRQIAGL LGYEDSDAKL 

       310        320        330        340        350        360 
AVERFMQKYY RVVLGIAELT ELVFQHFEEV ILPGDAAGRV EPLNERFQVR DGYLEVTHAG 

       370        380        390        400        410        420 
VFQETPSALL EIFVLLARRP EIRGVRADTI RLLRDHRYLI DDAFRRDPHN TGLFIELFKS 

       430        440        450        460        470        480 
RQGIHRNLRR MNRYGILGRY LPEFGHIVGQ MQHDLFHIYT VDAHTLNLIK NLRKLFWPEL 

       490        500        510        520        530        540 
AEKYPLASKL IEKLPKPELI YLAGLYHDIG KGRGGDHSEL GAADALAFCQ RHDLPAMDTQ 

       550        560        570        580        590        600 
LIVWLVRNHL LMSTTAQRKD LSDPQVIFDF AQKVRDQTYL DYLYVLTVAD INATNPTLWN 

       610        620        630        640        650        660 
SWRASLLRQL YTETKHALRR GLEQPVGREE QIRQTQKAAL DILVRSGTDP DDAEHLWTQL 

       670        680        690        700        710        720 
GDDYFLRHTS SDIAWHTEAI LQHPSSGGPL VLIKETTQRE FEGATQIFIY APDQHDFFAV 

       730        740        750        760        770        780 
TVAAMDQLNL SIHDARVITS TSQFTLDTYI VLDADGGSIG NNPARIQEIR QGLVEALRNP 

       790        800        810        820        830        840 
ADYPTIIQRR VPRQLKHFAF APQVTIQNDA LRPVTILEII APDRPGLLAR IGKIFLDFDL 

       850        860        870        880        890 
SLQNAKIATL GERVEDVFFV TDAHNQPLSD PELCARLQLA IAEQLADGDS YIQPSRISI 

« Hide

References

[1]"The product of the nitrogen fixation regulatory gene nfrX of Azotobacter vinelandii is functionally and structurally homologous to the uridylyltransferase encoded by glnD in enteric bacteria."
Contreras A., Drummond M., Bali A., Blanco G., Garcia E., Bush G., Kennedy C., Merrick M.
J. Bacteriol. 173:7741-7749(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COMPLEMENTATION OF E.COLI GLND MUTANT, ROLE IN NITROGEN FIXATION.
Strain: OP / UW136.
[2]"Lethality of glnD null mutations in Azotobacter vinelandii is suppressible by prevention of glutamine synthetase adenylylation."
Colnaghi R., Rudnick P., He L., Green A., Yan D., Larson E., Kennedy C.
Microbiology 147:1267-1276(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PII URIDYLYLTRANSFERASE, DISRUPTION PHENOTYPE.
Strain: OP / UW136.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59610 Genomic DNA. Translation: CAA42173.1.
PIRS24223.

3D structure databases

ProteinModelPortalP36223.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_AZOVI
AccessionPrimary (citable) accession number: P36223
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 11, 2014
This is version 72 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