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Q4FUP5

- GLND_PSYA2

UniProt

Q4FUP5 - GLND_PSYA2

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, Psyc_0395
Organism
Psychrobacter arcticus (strain DSM 17307 / 273-4)
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
Complete GO annotation...

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

BioCyciPARC259536:GI3A-410-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:Psyc_0395
OrganismiPsychrobacter arcticus (strain DSM 17307 / 273-4)
Taxonomic identifieri259536 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
ProteomesiUP000000546: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 915915Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_0000231688Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi259536.Psyc_0395.

Structurei

3D structure databases

ProteinModelPortaliQ4FUP5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini498 – 58891HD
Add
BLAST
Domaini732 – 81786ACT 1
Add
BLAST
Domaini840 – 91576ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 360360UridylyltransferaseUniRule annotation
Add
BLAST
Regioni361 – 731371Uridylyl-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. 1 hit.
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.

Q4FUP5-1 [UniParc]FASTAAdd to Basket

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MFNCAVTAID LTPMPLLSTD NMTTAPLSLS TDTSLIEKSL FGIPEWLLQI    50
NDDISRALER GVNIRQLVSA RACVIDDLLI GLFKWFELDK TDLALFATGG 100
YGRGELSLHS DIDILLLMPH EIDADTSSKI DNLVALLWDI GLEPALSVRS 150
VSECLEAALD HTIASALLEA RLLIGNETLQ DVPHQIVNNQ WSPRAFYDVK 200
IDEAKARYLQ HNATEYNLEP NIKTAPGGLR DIHIVGWVTK RYFRVSKLYD 250
LVQQNFLTEK EFDELSFSEG YLWQIRHYLH ELTGRNENKL LFDYQREIAQ 300
LMGYDTQPDD QPNAAVERFM RDYYRCAMQI STLSEMLTNH YYETIIEPQL 350
PDEERPKKQP INARFNQVGE QIAMAHHRVF AQHPESILEM FLLMGQYGIK 400
NVRTHTLRAL KIAARGIDQA YRDNPTHQTL FLANLKEQNY LFHRLRTMNR 450
YGVLGNYIPA FAQVTGLMQY DLFHRYTVDA HTLFLIRILH RFIDPHFYED 500
FPLVSSIFQR IERKEILVLA AMFHDIAKGR GGNHSQLGEI ESIEFCLAHG 550
MSNADANLVG WLTRYHLLMS MTAQKKDISD PEVVTLFADL VGNVTHLNHL 600
YVLTVADMNA TNPQLWNSWR ATLMKQLYSQ TRRILRADID APTNRQDMIS 650
ATRKQALMML DNVDNQHMNR DEVLSLWDDL GDEYFLREIA EDILWHTEAI 700
LNHPPIGRAS NADSPPLVVL REHRELALDA VQVFVYTQDQ VNLFAVTMAV 750
FDQMNLDVLD ARIITATRDF ALDSYVLLDR SGTLLVDSDS QQELKQRLID 800
AFKNPTAPKL THKRIPRQLK HFDVETTINF EFNDASSQHI MSLETLDQPG 850
LLARVGQVFL QQQIEVHAAR ITTLGERAED MFYISDQNDQ ALSANKLKTL 900
KTALIESLSV HNDSI 915
Length:915
Mass (Da):104,846
Last modified:August 30, 2005 - v1
Checksum:i68837CAE3D605366
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000082 Genomic DNA. Translation: AAZ18263.1.
RefSeqiYP_263697.1. NC_007204.1.

Genome annotation databases

EnsemblBacteriaiAAZ18263; AAZ18263; Psyc_0395.
GeneIDi3514133.
KEGGipar:Psyc_0395.
PATRICi23055115. VBIPsyArc98534_0490.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000082 Genomic DNA. Translation: AAZ18263.1 .
RefSeqi YP_263697.1. NC_007204.1.

3D structure databases

ProteinModelPortali Q4FUP5.
ModBasei Search...

Protein-protein interaction databases

STRINGi 259536.Psyc_0395.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ18263 ; AAZ18263 ; Psyc_0395 .
GeneIDi 3514133.
KEGGi par:Psyc_0395.
PATRICi 23055115. VBIPsyArc98534_0490.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci PARC259536:GI3A-410-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. 1 hit.
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. "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
    Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
    Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 17307 / 273-4.

Entry informationi

Entry nameiGLND_PSYA2
AccessioniPrimary (citable) accession number: Q4FUP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: August 30, 2005
Last modified: June 11, 2014
This is version 63 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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