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B5F8S8

- GLND_SALA4

UniProt

B5F8S8 - GLND_SALA4

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, SeAg_B0253
Organism
Salmonella agona (strain SL483)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].UniRule annotation
Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

Enzyme regulationi

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity By similarity.UniRule annotation

GO - Molecular functioni

  1. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
  2. amino acid binding Source: InterPro
  3. metal ion binding Source: InterPro
  4. phosphoric diester hydrolase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. nitrogen compound metabolic process Source: InterPro
  2. regulation of nitrogen utilization Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciSENT454166:GHBA-248-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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:
[Protein-PII] uridylyltransferase (EC:2.7.7.59)
Short name:
PII uridylyltransferase
Short name:
UTase
[Protein-PII]-UMP uridylyl-removing enzyme (EC:3.1.4.-)
Short name:
UR
Gene namesi
Name:glnD
Ordered Locus Names:SeAg_B0253
OrganismiSalmonella agona (strain SL483)
Taxonomic identifieri454166 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000008819: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 890890Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_1000114759Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi454166.SeAg_B0253.

Structurei

3D structure databases

ProteinModelPortaliB5F8S8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini468 – 601134HD
Add
BLAST
Domaini709 – 78476ACT 1
Add
BLAST
Domaini816 – 89075ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 349349UridylyltransferaseUniRule annotation
Add
BLAST
Regioni350 – 708359Uridylyl-removingUniRule annotation
Add
BLAST

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the GlnD family.
Contains 2 ACT domains.
Contains 1 HD domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261778.
OMAiHHLLMSV.
OrthoDBiEOG6CCH44.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamiPF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF006288. PII_uridyltransf. 1 hit.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01693. UTase_glnD. 1 hit.
PROSITEiPS51671. ACT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B5F8S8-1 [UniParc]FASTAAdd to Basket

« Hide

MNTLPEQHAN TALPTLPDQP QNPGVWPRAE LTVAGIKARI DIFQHWLGEA    50
FDSGICAEQL IEARTEFIDQ LLQRLWIEAG FGQIADLALV AVGGYGRGEL 100
HPLSDIDLLI LSRKKLPDEQ AQKVGELLTL LWDVKLDVGH SVRTLEECLL 150
EGLSDLTVAT NLIETRLLIG DVALFLALQK HIFSEGFWPS DKFYAAKVEE 200
QNQRHQRYHG TSYNLEPDIK SSPGGLRDIH TLQWVARRHF GATSLDEMVG 250
FGFLTPAERA ELNECLHILW RIRFALHLVV SRYDNRLLFD RQLSVAQRLN 300
YSGEGNDPVE RMMKDYFRVT RRVSELNQML LQLFDEAILA LPADEKPRPV 350
DDEFQLRGTL IDLRDDTLFI REPQAILRMF YMMVRNSAIT GIYSTTLRHL 400
RHARRHLSQP LCYIPEARTL FLSMLRHPGA VSRGLLPMHR HSVLWAYMPQ 450
WSHIVGQMQF DLFHAYTVDE HTIRVMLKLE SFAKEETRQR HPLCVDLWPR 500
LPHPELILIA ALFHDIAKGR GGDHSVLGAQ DVLTFAELHG LNSRETQLVA 550
WLVRQHLLMS VTAQRRDIQD PEVIKQFAEE VQTETRLRFL VCLTVADICA 600
TNETLWNSWK QSLLRELYFA TEKQLRRGMQ NTPDMRERVR HHQLQALALL 650
RMDNIDEAAL HKIWTRCRAN YFVRHSPNQL AWHARHLLQH DLSQPLVLLS 700
PQATRGGTEI FIWSPDRPYL FAAVCAELDR RNLSVHDAQI FTTRDGMAMD 750
TFIVLEPDGN PLAADRHDVI RTGLEQTITQ RSWQPPQPRR QPAKLRHFTV 800
ETEVNFLPTH TDRKSFMELI ALDQPGLLAR VGQIFADLGI SLHGARITTI 850
GERVEDLFII ATADRRALNN VLQLEVQQRL TAALNPNDKG 890
Length:890
Mass (Da):102,222
Last modified:October 14, 2008 - v1
Checksum:i313D763DCCF77460
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001138 Genomic DNA. Translation: ACH49835.1.
RefSeqiYP_002145219.1. NC_011149.1.

Genome annotation databases

EnsemblBacteriaiACH49835; ACH49835; SeAg_B0253.
PATRICi18478870. VBISalEnt65316_0278.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001138 Genomic DNA. Translation: ACH49835.1 .
RefSeqi YP_002145219.1. NC_011149.1.

3D structure databases

ProteinModelPortali B5F8S8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 454166.SeAg_B0253.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACH49835 ; ACH49835 ; SeAg_B0253 .
PATRICi 18478870. VBISalEnt65316_0278.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261778.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci SENT454166:GHBA-248-MONOMER.

Family and domain databases

Gene3Di 1.10.3210.10. 1 hit.
HAMAPi MF_00277. PII_uridylyl_transf.
InterProi IPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view ]
Pfami PF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF006288. PII_uridyltransf. 1 hit.
SMARTi SM00471. HDc. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01693. UTase_glnD. 1 hit.
PROSITEi PS51671. ACT. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
    Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
    J. Bacteriol. 193:3556-3568(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SL483.

Entry informationi

Entry nameiGLND_SALA4
AccessioniPrimary (citable) accession number: B5F8S8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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