SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q0BV39

- Q0BV39_GRABC

UniProt

Q0BV39 - Q0BV39_GRABC

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, GbCGDNIH1_0415
Organism
Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1)
Status
Unreviewed - 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 annotationSAAS annotations
Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].UniRule annotationSAAS annotations

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

HydrolaseUniRule annotationSAAS annotations, NucleotidyltransferaseUniRule annotationSAAS annotationsImported, Transferase

Keywords - Ligandi

MagnesiumUniRule annotationSAAS annotations

Enzyme and pathway databases

BioCyciGBET391165:GHON-426-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
Short name:
UTase/URUniRule annotation
Alternative name(s):
Bifunctional [protein-PII] modification enzyme
Bifunctional nitrogen sensor protein
Gene namesi
Name:glnDUniRule annotation
Ordered Locus Names:GbCGDNIH1_0415Imported
OrganismiGranulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1)Imported
Taxonomic identifieri391165 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGranulibacter
ProteomesiUP000001963: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi391165.GbCGDNIH1_0415.

Structurei

3D structure databases

ProteinModelPortaliQ0BV39.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini520 – 631112HD By similarityUniRule annotationAdd
BLAST
Domaini756 – 83782ACT 1 By similarityUniRule annotationAdd
BLAST
Domaini869 – 95183ACT 2 By similarityUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 390390Uridylyltransferase By similarityUniRule annotationAdd
BLAST
Regioni391 – 755365Uridylyl-removing By similarityUniRule annotationAdd
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.UniRule annotation
Contains 1 HD domain.UniRule annotation
Contains 2 ACT domains.UniRule annotation
Contains ACT domains.SAAS annotations
Contains HD domain.SAAS annotations

Keywords - Domaini

RepeatUniRule annotationSAAS annotations

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261779.
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.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamiPF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 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.

Q0BV39-1 [UniParc]FASTAAdd to Basket

« Hide

MVTSSSPGLA QKAPRQTASE LAALELDRAL TALEEEFGPG PRKGPLSQLE    50
RNAALGVFRR HLARIQGRVR DTFEQGRLAG LTAAHLLSDL TDGLVAALYQ 100
YTDSIAIPAS ATQQTEPVTV AATGGYGRQE LAPFSDIDLL FITADTPSAR 150
TLAVVEFMLY FLWDLGLKVG HATRSISQSL QAATEDTTVR TTLLDTRHLA 200
GNQPLFDAFI TAFREACTEA GEHDFIAAKQ AERHARHLRY GESPFFVEPN 250
IKEGRGGLRD LQTLYWLSRY VFGTRKLVDL VGTGAPGGGL ITENEARLAK 300
RSWNFLWTLR FHLHYVAGRA EERLTFDVQP VIGARMGYTR HGRQNGVERF 350
MRHYFLTARE VLRLTRVLEP ALIRAALGPP AIAAETDIAL INAGFVLAEG 400
KLLPAPSHDF EREPIQMLRI MKLARDRDLQ IHPLGIRSLI RNERGAIALR 450
DDQRAAALFL DLLCGNTVPD GVQRPTQRPS GARWMSILNE TGFLGRFIPE 500
WARIVGQMQF DTYHVFTVDE HTIEAIRVLN QLEHGDLADI APVATGVVDH 550
LQSRRALYVA MLTHDIAKGR GGDHSELGAE LALEIGPALG LDSEETEMVS 600
WLVLHHLLLS QTAFRRDIDD PKTILDLADT IQSPERLKLL LVLTVADMRA 650
VSSKVWNGWK ATLLRELYAR VAEVLAGGLA TTERDTRVAR AKEAAAELLY 700
DWPEEQREAF LTLGYPGYWL SFDPETHARH ARMIRAAGTQ LLTVDTQPLP 750
ARAVTEVTVY VADTPGLVGK IAGALAVAGA SIVDARIHTM TNGMAMDTFW 800
VQDTSGEAFD QPNRLAKIAV LIEQALSGQL DIDEEIRKAS NPLLGTRMRA 850
IHVPPRVVVD NHASHTHTVL EVNGRDRPGL MHDIAAAIAQ QGLQIASAHI 900
TTYGVRAVDV FYVKDVFGLK VENERKLAKL RQALLGALTS PDDTGPMPLP 950
PPMRRTHATG DDF 963
Length:963
Mass (Da):106,130
Last modified:October 17, 2006 - v1
Checksum:iFACD7A2CBB1E00F1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000394 Genomic DNA. Translation: ABI61313.1.
RefSeqiYP_744236.1. NC_008343.1.

Genome annotation databases

EnsemblBacteriaiABI61313; ABI61313; GbCGDNIH1_0415.
GeneIDi4275199.
KEGGigbe:GbCGDNIH1_0415.
PATRICi22076889. VBIGraBet83793_0436.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000394 Genomic DNA. Translation: ABI61313.1 .
RefSeqi YP_744236.1. NC_008343.1.

3D structure databases

ProteinModelPortali Q0BV39.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 391165.GbCGDNIH1_0415.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABI61313 ; ABI61313 ; GbCGDNIH1_0415 .
GeneIDi 4275199.
KEGGi gbe:GbCGDNIH1_0415.
PATRICi 22076889. VBIGraBet83793_0436.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261779.
KOi K00990.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci GBET391165:GHON-426-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.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view ]
Pfami PF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 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. "Genome sequence analysis of the emerging human pathogenic acetic acid bacterium Granulibacter bethesdensis."
    Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E., Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.
    J. Bacteriol. 189:8727-8736(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-1260 / CGDNIH1.

Entry informationi

Entry nameiQ0BV39_GRABC
AccessioniPrimary (citable) accession number: Q0BV39
Entry historyi
Integrated into UniProtKB/TrEMBL: October 17, 2006
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzymeUniRule annotationSAAS annotations

External Data

Dasty 3

Similar proteinsi