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B5F9X8

- GLND_VIBFM

UniProt

B5F9X8 - GLND_VIBFM

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, VFMJ11_2098
Organism
Vibrio fischeri (strain MJ11)
Status
Reviewed - Annotation score: 4 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

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:VFMJ11_2098
OrganismiVibrio fischeri (strain MJ11)
Taxonomic identifieri388396 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio
ProteomesiUP000001857: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 873873Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_1000114768Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi388396.VFMJ11_2098.

Structurei

3D structure databases

ProteinModelPortaliB5F9X8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini451 – 584134HD
Add
BLAST
Domaini693 – 77785ACT 1
Add
BLAST
Domaini800 – 87374ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 332332UridylyltransferaseUniRule annotation
Add
BLAST
Regioni333 – 692360Uridylyl-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.
KOiK00990.
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.

B5F9X8-1 [UniParc]FASTAAdd to Basket

« Hide

MKYLSPLSLS DTQLNITELK QQLTLFSQYQ INAFHQHKAV SDLVFERSHY    50
FDQLLSRLWQ FFKFDDIANT SLIAVGGYGR SELHPLSDID ILILTENNTN 100
DTFCQKVGEL VTLLWDLKLE IGHSVRSIAE CIEIGQNDLT VATNLQEARY 150
ICGNKELSHQ LKLKIHSDSF WPSESFYQAK IDEQKKRHSR YHDTTYNLEP 200
DIKSSPGGLR DIHTLSWIAR RHFGATSLLE MSQAGFLTDA EYRELLECQE 250
FLWRVRFALH IELKRYDNRL TFGHQASVAE HLGFIGEGNR GVERMMKEFY 300
RTLRRVAELN SMLLKIFDQA ILHQGEQDDA IIIDDDFQRR GRLIEARKPA 350
LFQARPDTIL DMFLLMANDS TIDGVAPPTM RQLRTARRRL NRFLCEIPEA 400
KEKFLQLTQH PNALNNAFSS MHKLGVLSAY LPQWSHIVGQ MQFDLFHAYT 450
VDEHSIRLLK HINKFSDTTN RDKHPICCEI FPKIMKKELL IIAAIFHDIA 500
KGRGGDHSEL GAVDAYDFCI SHGLSKPEAN LVSWLVKSHL LMSVTAQRRD 550
IYDPDVITEF AKQVRDEERL DYLVCLTVAD ICATNPDLWN SWKRSLIADL 600
YNATQRALRR GLENPPDLRD RIRHNQQMAS AQLRSEGFTQ WEVDALWRRF 650
KADYFLRHTH KQIAWHASHL LRHQDKEKSL ILISKNASRG GTEIFVYSKD 700
QPHLFATVAA ELDRRSITIY DAQVMSSKDG YALDTFMVLD QNDDPIDEER 750
QQRLIDQLYD VKLNDQATHI KTRRPPRQLQ HFNVKTRMEF LPTKTGKRTL 800
MEFVALDTPG LLATVGATFA QLGINLHAAK ITTIGERAED LFILTSDVGG 850
RLDDDKQAEL EIALVKNVAR LSS 873
Length:873
Mass (Da):100,653
Last modified:October 14, 2008 - v1
Checksum:iBD26292DA8B5F8CD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi6806687.
KEGGivfm:VFMJ11_2098.
PATRICi20122660. VBIVibFis37164_2020.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001139 Genomic DNA. Translation: ACH66318.1 .
RefSeqi WP_012533646.1. NC_011184.1.
YP_002156792.1. NC_011184.1.

3D structure databases

ProteinModelPortali B5F9X8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 388396.VFMJ11_2098.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACH66318 ; ACH66318 ; VFMJ11_2098 .
GeneIDi 6806687.
KEGGi vfm:VFMJ11_2098.
PATRICi 20122660. VBIVibFis37164_2020.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261778.
KOi K00990.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.

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. "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: September 3, 2014
This is version 45 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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