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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Vibrio fischeri (strain MJ11)
Status
Reviewed-Annotation score: 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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
Short name:
UTase/URUniRule annotation
Alternative name(s):
Bifunctional [protein-PII] modification enzymeUniRule annotation
Bifunctional nitrogen sensor proteinUniRule annotation
Including the following 2 domains:
[Protein-PII] uridylyltransferaseUniRule annotation (EC:2.7.7.59UniRule annotation)
Short name:
PII uridylyltransferaseUniRule annotation
Short name:
UTaseUniRule annotation
[Protein-PII]-UMP uridylyl-removing enzymeUniRule annotation (EC:3.1.4.-UniRule annotation)
Short name:
URUniRule annotation
Gene namesi
Name:glnDUniRule annotation
Ordered Locus Names:VFMJ11_2098
OrganismiVibrio fischeri (strain MJ11)
Taxonomic identifieri388396 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio
ProteomesiUP000001857 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 873873Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000114768Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi388396.VFMJ11_2098.

Structurei

3D structure databases

ProteinModelPortaliB5F9X8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini451 – 584134HDUniRule annotationAdd
BLAST
Domaini693 – 77785ACT 1UniRule annotationAdd
BLAST
Domaini800 – 87374ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 332332UridylyltransferaseAdd
BLAST
Regioni333 – 692360Uridylyl-removingAdd
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.UniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261778.
KOiK00990.
OMAiSTIGERV.
OrthoDBiEOG6CCH44.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
IPR010043. UTase/UR.
[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.

B5F9X8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYLSPLSLS DTQLNITELK QQLTLFSQYQ INAFHQHKAV SDLVFERSHY
60 70 80 90 100
FDQLLSRLWQ FFKFDDIANT SLIAVGGYGR SELHPLSDID ILILTENNTN
110 120 130 140 150
DTFCQKVGEL VTLLWDLKLE IGHSVRSIAE CIEIGQNDLT VATNLQEARY
160 170 180 190 200
ICGNKELSHQ LKLKIHSDSF WPSESFYQAK IDEQKKRHSR YHDTTYNLEP
210 220 230 240 250
DIKSSPGGLR DIHTLSWIAR RHFGATSLLE MSQAGFLTDA EYRELLECQE
260 270 280 290 300
FLWRVRFALH IELKRYDNRL TFGHQASVAE HLGFIGEGNR GVERMMKEFY
310 320 330 340 350
RTLRRVAELN SMLLKIFDQA ILHQGEQDDA IIIDDDFQRR GRLIEARKPA
360 370 380 390 400
LFQARPDTIL DMFLLMANDS TIDGVAPPTM RQLRTARRRL NRFLCEIPEA
410 420 430 440 450
KEKFLQLTQH PNALNNAFSS MHKLGVLSAY LPQWSHIVGQ MQFDLFHAYT
460 470 480 490 500
VDEHSIRLLK HINKFSDTTN RDKHPICCEI FPKIMKKELL IIAAIFHDIA
510 520 530 540 550
KGRGGDHSEL GAVDAYDFCI SHGLSKPEAN LVSWLVKSHL LMSVTAQRRD
560 570 580 590 600
IYDPDVITEF AKQVRDEERL DYLVCLTVAD ICATNPDLWN SWKRSLIADL
610 620 630 640 650
YNATQRALRR GLENPPDLRD RIRHNQQMAS AQLRSEGFTQ WEVDALWRRF
660 670 680 690 700
KADYFLRHTH KQIAWHASHL LRHQDKEKSL ILISKNASRG GTEIFVYSKD
710 720 730 740 750
QPHLFATVAA ELDRRSITIY DAQVMSSKDG YALDTFMVLD QNDDPIDEER
760 770 780 790 800
QQRLIDQLYD VKLNDQATHI KTRRPPRQLQ HFNVKTRMEF LPTKTGKRTL
810 820 830 840 850
MEFVALDTPG LLATVGATFA QLGINLHAAK ITTIGERAED LFILTSDVGG
860 870
RLDDDKQAEL EIALVKNVAR LSS
Length:873
Mass (Da):100,653
Last modified:October 14, 2008 - v1
Checksum:iBD26292DA8B5F8CD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001139 Genomic DNA. Translation: ACH66318.1.
RefSeqiWP_012533646.1. NC_011184.1.
YP_002156792.1. NC_011184.1.

Genome annotation databases

EnsemblBacteriaiACH66318; ACH66318; VFMJ11_2098.
KEGGivfm:VFMJ11_2098.
PATRICi20122660. VBIVibFis37164_2020.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001139 Genomic DNA. Translation: ACH66318.1.
RefSeqiWP_012533646.1. NC_011184.1.
YP_002156792.1. NC_011184.1.

3D structure databases

ProteinModelPortaliB5F9X8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi388396.VFMJ11_2098.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACH66318; ACH66318; VFMJ11_2098.
KEGGivfm:VFMJ11_2098.
PATRICi20122660. VBIVibFis37164_2020.

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261778.
KOiK00990.
OMAiSTIGERV.
OrthoDBiEOG6CCH44.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
IPR010043. UTase/UR.
[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]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of Vibrio fischeri strain MJ11."
    Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.
    Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MJ11.

Entry informationi

Entry nameiGLND_VIBFM
AccessioniPrimary (citable) accession number: B5F9X8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 14, 2008
Last modified: April 29, 2015
This is version 52 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.