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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Psychrobacter cryohalolentis (strain K5)
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

  1. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
  2. amino acid binding Source: InterPro
  3. 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

BioCyciPCRY335284:GHE9-456-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 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:Pcryo_0441
OrganismiPsychrobacter cryohalolentis (strain K5)
Taxonomic identifieri335284 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
ProteomesiUP000002425 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 913913Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022352Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi335284.Pcryo_0441.

Structurei

3D structure databases

ProteinModelPortaliQ1QDM9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini479 – 586108HDUniRule annotationAdd
BLAST
Domaini730 – 81586ACT 1UniRule annotationAdd
BLAST
Domaini838 – 91376ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 358358UridylyltransferaseAdd
BLAST
Regioni359 – 729371Uridylyl-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. 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.

Q1QDM9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNCDVTAID LTPMPLFSAD NMTTAFLSTD TSVVEKSLFG IPEWLLQIND
60 70 80 90 100
DISRALERGV NIRQLVSARA CVIDDLLIEL FKCFGLDKTD LALFATGGYG
110 120 130 140 150
RGELSLHSDI DILLLMPHDI NADTSSKIDN LVALLWDIGL EPALSVRSVS
160 170 180 190 200
DCLEAALDHT IASALLEARL LIGNDALQNV PHQIVNNQWS PRSFYDVKID
210 220 230 240 250
EAKARYLQHN ATEYNLEPNI KTAPGGLRDI HIIGWVTKRY FRVSKLYDLV
260 270 280 290 300
QQNFLTEKEF DELSFSENYL WQIRHYLHEL TGRNENKLLF DYQREIAQLM
310 320 330 340 350
GYDTQTDDQP NAAVERFMRD YYRCAMQIST LSEMLTNHYY ETIIEAQLPD
360 370 380 390 400
EERPKKQPIN ARFNQVGDQI AMAHHRVFAQ HPESILEMFL LMGQYGIKNV
410 420 430 440 450
RTHTLRALKI AARGIDQAYR DNPTHQTLFL ANLKEQNYLF HRLRTMNRYG
460 470 480 490 500
VLGNYIPAFA QVTGLMQYDL FHRYTVDAHT LFLIRILHRF TDPHFYEDFP
510 520 530 540 550
LVSSIFQRIE RKEILVLAAM FHDIAKGRGG NHSQLGEIES IEFCLAHGMS
560 570 580 590 600
TADANLVGWL TRYHLLMSMT AQKKDISDPE VVTLFADLVG NVTHLNHLYV
610 620 630 640 650
LTVADMNATN PQLWNSWRAT LMKQLYSQTR RILRADIDAP TNRQDMISAT
660 670 680 690 700
RKQALVMLDN VDNQHMNRDE VLRLWDDLGD EYFLREIAED ILWHTEAILN
710 720 730 740 750
HPPIGRASNA DSPPLVVLRE HRELALDAVQ VFVYTQDQVN LFAVTMAVFD
760 770 780 790 800
QMNLDVLDAR IITATRDFAL DSYVLLDRSG TLLVDSDSQQ ELKQRLIDAF
810 820 830 840 850
KNPTAPKLTH KRIPRQLKHF DVATTINFDF NDASNQHIMS LETLDQPGLL
860 870 880 890 900
ARVGQVFLQQ QIEVHAARIT TLGERAEDMF YISDQNDQAL SADKLKTLKT
910
ALIDSLSVRN DRV
Length:913
Mass (Da):104,638
Last modified:May 16, 2006 - v1
Checksum:i1E1118BBFD987E10
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000323 Genomic DNA. Translation: ABE74224.1.
RefSeqiWP_011512809.1. NC_007969.1.
YP_579708.1. NC_007969.1.

Genome annotation databases

EnsemblBacteriaiABE74224; ABE74224; Pcryo_0441.
KEGGipcr:Pcryo_0441.
PATRICi23060331. VBIPsyCry128170_0505.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000323 Genomic DNA. Translation: ABE74224.1.
RefSeqiWP_011512809.1. NC_007969.1.
YP_579708.1. NC_007969.1.

3D structure databases

ProteinModelPortaliQ1QDM9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi335284.Pcryo_0441.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE74224; ABE74224; Pcryo_0441.
KEGGipcr:Pcryo_0441.
PATRICi23060331. VBIPsyCry128170_0505.

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261778.
KOiK00990.
OMAiSTIGERV.
OrthoDBiEOG6CCH44.

Enzyme and pathway databases

BioCyciPCRY335284:GHE9-456-MONOMER.

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. 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]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J.
    , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K5.

Entry informationi

Entry nameiGLND_PSYCK
AccessioniPrimary (citable) accession number: Q1QDM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: April 29, 2015
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

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.