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A7MGS0 (GLND_CROS8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:ESA_03176
OrganismCronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii) [Complete proteome] [HAMAP]
Taxonomic identifier290339 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter

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_1000022342

Regions

Domain470 – 603134HD
Domain711 – 79080ACT 1
Domain818 – 89275ACT 2
Region1 – 351351Uridylyltransferase HAMAP-Rule MF_00277
Region352 – 710359Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
A7MGS0 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 99E2B1D75E7F6B4E

FASTA892103,003
        10         20         30         40         50         60 
MMSNTLPEQS VNTTLAPLPG QPDYPATWPA DALNCAQIKQ HLDAFQQWLG AAFDDGYTAE 

        70         80         90        100        110        120 
QLIEARTEFI DQLLQRLWIA AGFGDTPDTA LVAVGGYGRG ELHPLSDIDL LILSRKRLSE 

       130        140        150        160        170        180 
AQAQKVGELL TLLWDVKLEV GHSVRTLEEC LLEGLSDLTV ATNLIESRLL IGDVALFLEL 

       190        200        210        220        230        240 
QKHIFSDGFW PSEKFFAAKV EEQNERHQRY HGTSYNLEPD IKSSPGGLRD IHTLQWVARR 

       250        260        270        280        290        300 
HFGATSLREM VGFGFLTEAE RNELDECQHL LWRIRFALHL ELNRYDNRLL FDRQLSVAQR 

       310        320        330        340        350        360 
LRYEGEGNEP VEHMMKDFYR VTRRVGELNQ MLLQLFDEAI LALTTDEKPR VLDDDFQLRG 

       370        380        390        400        410        420 
TLIDLRDETL FIREPQAILR MFYMMVRNRD ITGIYSTTLR HLRHARRHLK QPLCYIPEAR 

       430        440        450        460        470        480 
SLFLAMLRHP GAVSRGLLPM HRHSVLWAYM PQWSHIVGQM QFDLFHAYTV DEHTIRVLLK 

       490        500        510        520        530        540 
LESFAKEETR AKHPLCVDLW PRLSHPELIL IAALFHDIAK GRGGDHSVLG AQDILKFAEL 

       550        560        570        580        590        600 
HGLNSRETQL VAWLVRHHLL MSVTAQRRDI QDPEVIKQFA EEVQTENRLR FLVCLTVADI 

       610        620        630        640        650        660 
CATNETLWNS WKQSLLRELY FATEKQLRRG MQSTPDMRER VRHHQLQALA LLRMENIDEE 

       670        680        690        700        710        720 
ALHHIWGRCR ANYFVRHSPN QLAWHARHLL RHDLSKPLIL LSPQATRGGT EIFIWSPDRP 

       730        740        750        760        770        780 
YLFAAVCAEL DRRNLSVHDA QIFTTRDDMA MDTFIVLEPD GSPLSPDRHE AIRHGLEQAI 

       790        800        810        820        830        840 
TQRTWQPPQP RRQPAKLRHF TVETEVNFLP THTDRKSFLE LIALDQPGLL ARVGQVFADL 

       850        860        870        880        890 
GISLHGARIS TIGERVEDLF IIATADRRGL NNLLQQEVRQ RLTEDLNPND KV 

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References

[1]"Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic hybridization analysis with other Cronobacter species."
Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., McClelland M., Forsythe S.J.
PLoS ONE 5:E9556-E9556(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-894.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000783 Genomic DNA. Translation: ABU78398.1.
RefSeqYP_001439234.1. NC_009778.1.

3D structure databases

ProteinModelPortalA7MGS0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290339.ESA_03176.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABU78398; ABU78398; ESA_03176.
GeneID5549477.
KEGGesa:ESA_03176.
PATRIC20398085. VBICroSak107175_2807.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK05007.

Enzyme and pathway databases

BioCycCSAK290339:GJ80-3166-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. 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_CROS8
AccessionPrimary (citable) accession number: A7MGS0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 2, 2007
Last modified: February 19, 2014
This is version 47 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