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P23679 (GLND_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 108. 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:STM0214
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length890 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 caution

The sequence CAA39299.1 differs from that shown. Reason: Frameshift at position 88.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 890890Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192766

Regions

Domain468 – 601134HD
Domain709 – 78476ACT 1
Domain816 – 89075ACT 2
Region1 – 349349Uridylyltransferase HAMAP-Rule MF_00277
Region350 – 708359Uridylyl-removing HAMAP-Rule MF_00277

Experimental info

Sequence conflict1011H → D Ref.2

Sequences

Sequence LengthMass (Da)Tools
P23679 [UniParc].

Last modified December 13, 2001. Version 3.
Checksum: B4BF92D1DC4280D0

FASTA890102,264
        10         20         30         40         50         60 
MNTLPEQHAN TALPTLPDQP QNPGVWPRAE LTVAGIKARI DIFQHWLGEA FDSGICAEQL 

        70         80         90        100        110        120 
IEARTEFIDQ LLQRLWIEAG FGQIADLALV AVGGYGRGEL HPLSDIDLLI LSRKKLPDEQ 

       130        140        150        160        170        180 
AQKVGELLTL LWDVKLDVGH SVRTLEECLL EGLSDLTVAT NLIETRLLIG DVALFLALQK 

       190        200        210        220        230        240 
HIFSEGFWPS DKFYAAKVEE QNQRHQRYHG TSYNLEPDIK SSPGGLRDIH TLQWVARRHF 

       250        260        270        280        290        300 
GATSLDEMVG FGFLTPAERA ELNECLHILW RIRFALHLVV SRYDNRLLFD RQLSVAQRLN 

       310        320        330        340        350        360 
YSGEGNDPVE RMMKDYFRVT RRVSELNQML LQLFDEAILA LPADEKPRPV DDEFQLRGTL 

       370        380        390        400        410        420 
IDLRDDTLFI REPQAILRMF YMMVRNSAIT GIYSTTLRHL RHARRHLSQP LCYIPEARTL 

       430        440        450        460        470        480 
FLSMLRHPGA VSRGLLPMHR HSVLWAYMPQ WSHIVGQMQF DLFHAYTVDE HTIRVMLKLE 

       490        500        510        520        530        540 
SFAKEETRQR HPLCVDLWPR LPHPELILIA ALFHDIAKGR GGDHSVLGAQ DVLTFAELHG 

       550        560        570        580        590        600 
LNSRETQLVA WLVRQHLLMS VTAQRRDIQD PEVIKQFAEE VQTETRLRFL VCLTVADICA 

       610        620        630        640        650        660 
TNETLWNSWK QSLLRELYFA TEKQLRRGMQ NTPDMRERVR HHQLQALALL RMDNIDEAAL 

       670        680        690        700        710        720 
HKIWTRCRAN YFVRHSPNQL AWHARHLLQH DLRQPLVLLS PQATRGGTEI FIWSPDRPYL 

       730        740        750        760        770        780 
FAAVCAELDR RNLSVHDAQI FTTRDGMAMD TFIVLEPDGS PLAADRHDVI RTGLEQTITQ 

       790        800        810        820        830        840 
RSWQPPQPRR QPAKLRHFTV ETEVNFLPTH TDRKSFMELI ALDQPGLLAR VGQIFADLGI 

       850        860        870        880        890 
SLHGARITTI GERVEDLFII ATADRRALNN VLQLEVQQRL TAALNPNDKG 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[2]"Cloning and nucleotide sequence of the Salmonella typhimurium pepM gene."
Movva N.R., Semon D., Meyer C., Kawashima E., Wingfield P., Miller J.L., Miller C.G.
Mol. Gen. Genet. 223:345-348(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201.
Strain: LT2.
[3]Robison K.
Unpublished observations (OCT-1992)
Cited for: IDENTIFICATION OF PROTEIN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL19178.1.
X55778 Genomic DNA. Translation: CAA39299.1. Frameshift.
PIRS12028.
RefSeqNP_459219.1. NC_003197.1.

3D structure databases

ProteinModelPortalP23679.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM0214.

Proteomic databases

PRIDEP23679.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL19178; AAL19178; STM0214.
GeneID1251732.
KEGGstm:STM0214.
PATRIC32378715. VBISalEnt20916_0227.

Phylogenomic databases

HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK05007.

Enzyme and pathway databases

BioCycSENT99287:GCTI-213-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_SALTY
AccessionPrimary (citable) accession number: P23679
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: December 13, 2001
Last modified: February 19, 2014
This is version 108 of the entry and version 3 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