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A8GIE8 (GLND_SERP5) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 50. 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:Spro_3792
OrganismSerratia proteamaculans (strain 568) [Complete proteome] [HAMAP]
Taxonomic identifier399741 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Protein attributes

Sequence length892 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 – 892892Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000059226

Regions

Domain470 – 603134HD
Domain711 – 79282ACT 1
Domain818 – 89275ACT 2
Region1 – 351351Uridylyltransferase HAMAP-Rule MF_00277
Region352 – 710359Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
A8GIE8 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 8D6DC4E817EDB145

FASTA892103,200
        10         20         30         40         50         60 
MSENFRQQDT SVISPQAVPV QPEYPNAYGD EEINCIALKQ RLEQFQLWLA AAFNAGSSAE 

        70         80         90        100        110        120 
SLVAARSDFI DRLLRRLWVF YGFEDIPETA LVAVGGYGRG ELHPLSDIDV LVLSQRRLNE 

       130        140        150        160        170        180 
QQSQRVGEFI TLLWDLKLEV GHSVRTLEEC LLEGLADLTV ATNLIESRMI CGDVALFLQM 

       190        200        210        220        230        240 
QKHIFSDGFW PSPQFFHAKV VEQQERHQRY HGTSYNLEPD IKSSPGGLRD IHTLLWVARR 

       250        260        270        280        290        300 
HFGATSLDEM VGFGFLTQAE RNELNECQSF LWRIRFALHL VLPRYDNRLL FDRQLNVAQL 

       310        320        330        340        350        360 
LRYEGEGNEP VERMMKDFYR MTRRVGELNH MLLQLFDEAI LALDATEKPR PLNDDFQLRG 

       370        380        390        400        410        420 
DLIDLRDETL FIRQPESIMR MFYLMVRNRE IKGIYSTTVR QLRHARRHLK QPLCTIPEAR 

       430        440        450        460        470        480 
ELFMAILRHP GAVSRALVPM HRHSVLWAYM PQWGKIVGQM QFDLFHAYTV DEHTIRVLQK 

       490        500        510        520        530        540 
LESFADAETR PRHPLCVELY PRLPNPELLL LAALFHDIAK GRGGDHSILG AQDVLEFAEV 

       550        560        570        580        590        600 
HGLNSREAQL VAWLVRCHLL MSVTAQRRDI QDPTVIQQFS AEVQSETRLR YLVCLTVADI 

       610        620        630        640        650        660 
CATNETLWNS WKQSLLRELY FATEKQLRRG MQNSPDLRER VRHHRLQALA LLRMDNIDEE 

       670        680        690        700        710        720 
ALHRIWSRCR ADYFLRHSPN QLAWHARHLL AHDSTKPLVL VSRQATRGGT EIFIWSPDRP 

       730        740        750        760        770        780 
YLFAAVAGEM DRRNLSVHDA QIFTNRDGMA MDTFIVLEPD GSPLAQDRHT AIRHALLQAI 

       790        800        810        820        830        840 
TQREYQPPRV RRPSSKLRHF SVPTEVSFLP THTDRRSYLE LTALDQPGLL ARVGEVFADL 

       850        860        870        880        890 
NLSLHGARIS TIGERVEDLF ILADSDRRAL NPETRRKLEQ RLTEALNPND KM 

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References

[1]"Complete sequence of chromosome of Serratia proteamaculans 568."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 568.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000826 Genomic DNA. Translation: ABV42888.1.
RefSeqYP_001480016.1. NC_009832.1.

3D structure databases

ProteinModelPortalA8GIE8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399741.Spro_3792.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV42888; ABV42888; Spro_3792.
GeneID5607191.
KEGGspe:Spro_3792.
PATRIC32420400. VBISerPro44537_3852.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycSPRO399741:GI55-3872-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_SERP5
AccessionPrimary (citable) accession number: A8GIE8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: June 11, 2014
This is version 50 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