Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C6DAI1 (GLND_PECCP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:PC1_0939
OrganismPectobacterium carotovorum subsp. carotovorum (strain PC1) [Complete proteome] [HAMAP]
Taxonomic identifier561230 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

Protein attributes

Sequence length904 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 – 904904Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000204799

Regions

Domain479 – 612134HD
Domain720 – 80182ACT 1
Domain827 – 90478ACT 2
Region1 – 360360Uridylyltransferase HAMAP-Rule MF_00277
Region361 – 719359Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
C6DAI1 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 8B64081DE776F27A

FASTA904104,374
        10         20         30         40         50         60 
MTDNRFSPDS TPPDASSPDS PVDTIASTQL PASPLTYADD MLNCQTLKQQ LELFQLWLGS 

        70         80         90        100        110        120 
EFRSGVSAEK LIDARTLFID RLLQRLWYFY GFENIAQTSL VAVGGYGRGE LHPLSDIDVL 

       130        140        150        160        170        180 
VLSQTALSEE HSQRVGQFIT LLWDLKLEVG HSVRTLEECL QEGRADISVA TNLIESRMIC 

       190        200        210        220        230        240 
GDVALFLTLQ KHVFSDEFWP SSAFFPAKIA EQQERHQRYH STSYNLEPDI KSSPGGLRDI 

       250        260        270        280        290        300 
HTLLWVARRH FGATSLNEMV GFGFLTEAER KELNECQSFL WRIRFALHLI LPRYDNRLLF 

       310        320        330        340        350        360 
DRQLNVAQLL QYQGEGNTPV ERMMKDFYRM TRRVSELNQM LLQLFDEAIL ALDASEKPRP 

       370        380        390        400        410        420 
IDDEFQLRGN LVDLRDENLF IKKPEAIMRM FYLMVRNRDI SGIYSTTLRQ LRHARRHLAS 

       430        440        450        460        470        480 
PLCTIPEARQ LFMNILRHPH AVSRALLPMH RHSVLWAYMP LWGNIVGQMQ FDLFHAYTVD 

       490        500        510        520        530        540 
EHTIRVLLKL ESFADEETRP QHPLCVELYP RLPQPELLLL AALFHDIAKG RGGDHSELGA 

       550        560        570        580        590        600 
QDVLEFAALH GLNSREAQLV SWLVRCHLLM SVTAQRRDIQ DPTVIQQFAT EVQSETRLRY 

       610        620        630        640        650        660 
LVSLTVADIC ATNETLWNSW KQSLLRELYF ATEKQLRRGM QNTPDLRERV RHHRLQALAL 

       670        680        690        700        710        720 
LRMDNIDEEA LHHIWSRCRA DYFLRHSPNQ LAWHARHLLE HDVNKPLVLI SHQASRGGTE 

       730        740        750        760        770        780 
IFIWSPDRPY LFAAVAGELD RRNLSVHDAQ IFTSRDGMAM DTFIVLEPDG SPLAQDRHEM 

       790        800        810        820        830        840 
IRHALEQALT QRHYQHPRVR RPSPKLRHFS VPTEVNFLPT HTDRRSYMEL SALDQPGLLA 

       850        860        870        880        890        900 
RIGEIFADLN LSLHGARIST IGERVEDLFI LADSDRRALK PELRLKLQER LTEALNPNDK 


VPLS 

« Hide

References

[1]"Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Balakrishnan V., Glasner J., Perna N.T.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PC1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001657 Genomic DNA. Translation: ACT11989.1.
RefSeqYP_003016525.1. NC_012917.1.

3D structure databases

ProteinModelPortalC6DAI1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561230.PC1_0939.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT11989; ACT11989; PC1_0939.
GeneID8131868.
KEGGpct:PC1_0939.
PATRIC20486468. VBIPecCar70489_0935.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycPCAR561230:GKCK-969-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. 2 hits.
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_PECCP
AccessionPrimary (citable) accession number: C6DAI1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: June 11, 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