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Q5FPT6

- GLND_GLUOX

UniProt

Q5FPT6 - GLND_GLUOX

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, GOX1872
Organism
Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
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

Enzyme and pathway databases

BioCyciGOXY290633:GHB3-1870-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:GOX1872
OrganismiGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
Taxonomic identifieri290633 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconobacter
ProteomesiUP000006375: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 949949Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_0000192735Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi290633.GOX1872.

Structurei

3D structure databases

ProteinModelPortaliQ5FPT6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini541 – 62989HD
Add
BLAST
Domaini757 – 83478ACT 1
Add
BLAST
Domaini870 – 94980ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 395395UridylyltransferaseUniRule annotation
Add
BLAST
Regioni396 – 756361Uridylyl-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.
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.

Q5FPT6-1 [UniParc]FASTAAdd to Basket

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MKETSFWGET PSLSFADDTD KPLSDRTASP PCDPASSLQT ALDTAAAQGQ    50
TTRENVLSIL RRHLGSGNAT VRREFEKRRM SGIDAARALA RQADDMVCAL 100
AELAAQKHES PGETLCLCAT GGYGAGLLAP FSDIDILFLI PGDPTPAMTA 150
RIEFILYALW DLGLRVGHAT RSIAECVRDA DSDLTIRTAL LDLRFLHGER 200
GLARDLRCAL GADLQNDRLC EFVMGKIAER EQRHRRFGDN PYMVEPNIKE 250
GRGGLRDLQT LNWMGRAALG CAVSTPDRSG QPAEAPQTPS FASFGLLTDR 300
ESLRARRSWD FLWTVRLHLH YITGRAEERL TFDVQPVIGG RMGYATHGRQ 350
RGVERFMRHY FLTARDVMRL TSVLQPVVLM HLQDQTTGEP PKVVPGPEEF 400
QTIAGRICPI EPVTFAAQPR EMFRLLDCGR RHDLPLHPIA MQQIIRNERH 450
AVTLRDDPET AKIFLDLLCE PSADETKAVP FWLPILNETG LLGRLLPDWS 500
RVVGQMQFDS YHIYTVDEHI VEAVRMMGQI EAGRMADEIP LAYTLASDLR 550
SRRALYVAVL LHDIGKGRGG DHSEIGADLA LTICPQLGLD PEETDTVSWL 600
VLHHLLLSQT AFTRDIDDPR TILDLADTIQ SPERLRLLLL LTIADMRAVS 650
PKVWNAWKAT LLRELFSRVA EVLEGGLAAT ERDSRVNHAR ELARDGLTGI 700
LPESSIDRFL DLGYPSYWLG FDTDTQMRHA RMVHDSDRYR SPVTVEAYPI 750
PERGVTELTV LCADHPGLFS QIAGALAVSG ASIVDARIHT LSDGMALDTF 800
WVQDGEGCSF EEPHQLGRLN HLVEQALSGR LDIRKGIEDA SHHSTSRRMR 850
AIHVPPRVVI DNTASDRHTV IEVNGRDRPG LLHDVTSALS SASLQISSAH 900
ITTYGMRAVD VFYVRDLLGM KITDPVRLAR LRETLLASLT SAPVTTPAS 949
Length:949
Mass (Da):105,398
Last modified:March 1, 2005 - v1
Checksum:i79BEEE7485522A9B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000009 Genomic DNA. Translation: AAW61610.1.
RefSeqiYP_192266.1. NC_006677.1.

Genome annotation databases

EnsemblBacteriaiAAW61610; AAW61610; GOX1872.
GeneIDi3250631.
KEGGigox:GOX1872.
PATRICi32611646. VBIGluOxy81109_2161.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000009 Genomic DNA. Translation: AAW61610.1 .
RefSeqi YP_192266.1. NC_006677.1.

3D structure databases

ProteinModelPortali Q5FPT6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 290633.GOX1872.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAW61610 ; AAW61610 ; GOX1872 .
GeneIDi 3250631.
KEGGi gox:GOX1872.
PATRICi 32611646. VBIGluOxy81109_2161.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci GOXY290633:GHB3-1870-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. "Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
    Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
    Nat. Biotechnol. 23:195-200(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 621H.

Entry informationi

Entry nameiGLND_GLUOX
AccessioniPrimary (citable) accession number: Q5FPT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: March 1, 2005
Last modified: June 11, 2014
This is version 68 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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