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Q6D8E5 (GLND_PECAS) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 70. 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:ECA1029
OrganismPectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica) [Complete proteome] [HAMAP]
Taxonomic identifier218491 [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 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 – 904904Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192731

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
Q6D8E5 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 1A6A4DEF5361ED32

FASTA904104,412
        10         20         30         40         50         60 
MTDKRFSPDN TPPDASSPDS PIDTIAAAQP PVSPLTYADD MLNCQALKQQ LELFQLWLGS 

        70         80         90        100        110        120 
EFRSGVSAEK LIDARTLFID RLLQRLWYCH GFENIAQTAL VAVGGYGRGE LHPLSDIDVL 

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

       190        200        210        220        230        240 
GDVALFLTLQ KHVFSDEFWP SPTFFPAKIT 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 LFMNILRHPY AVSRALLPMH RHSVLWAYMP LWGNIVGQMQ FDLFHAYTVD 

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

       550        560        570        580        590        600 
LDVLEFAALH 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 IAWHARHLLE HDTNKPLVLI SHQASRGGTE 

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

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

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


VPLS 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX950851 Genomic DNA. Translation: CAG73940.1.
RefSeqYP_049136.1. NC_004547.2.

3D structure databases

ProteinModelPortalQ6D8E5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218491.ECA1029.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG73940; CAG73940; ECA1029.
GeneID2881763.
KEGGeca:ECA1029.
PATRIC20477274. VBIPecAtr54885_1037.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycPATR218491:GJNB-1059-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_PECAS
AccessionPrimary (citable) accession number: Q6D8E5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: August 16, 2004
Last modified: June 11, 2014
This is version 70 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