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C1DSU8 (GLND_AZOVD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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:Avin_39010
OrganismAzotobacter vinelandii (strain DJ / ATCC BAA-1303) [Complete proteome] [HAMAP]
Taxonomic identifier322710 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

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 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 – 899899Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000204797

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
C1DSU8 [UniParc].

Last modified May 26, 2009. 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001157 Genomic DNA. Translation: ACO80041.1.
RefSeqYP_002801016.1. NC_012560.1.

3D structure databases

ProteinModelPortalC1DSU8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING322710.Avin_39010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO80041; ACO80041; Avin_39010.
GeneID7762790.
KEGGavn:Avin_39010.
PATRIC21033848. VBIAzoVin72790_3666.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK00275.

Enzyme and pathway databases

BioCycAVIN322710:GJ0M-3907-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_AZOVD
AccessionPrimary (citable) accession number: C1DSU8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 40 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