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Q485H4

- GLND_COLP3

UniProt

Q485H4 - GLND_COLP3

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, CPS_1549
Organism
Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus)
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

BioCyciCPSY167879:GI48-1549-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:CPS_1549
OrganismiColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus)
Taxonomic identifieri167879 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia
ProteomesiUP000000547: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 878878Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_0000192729Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi167879.CPS_1549.

Structurei

3D structure databases

ProteinModelPortaliQ485H4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini460 – 567108HD
Add
BLAST
Domaini701 – 77979ACT 1
Add
BLAST
Domaini809 – 87870ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 342342UridylyltransferaseUniRule annotation
Add
BLAST
Regioni343 – 700358Uridylyl-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.

Q485H4-1 [UniParc]FASTAAdd to Basket

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MTSHPVSVHI VPSHFINQLA ISADFLSTRD ICQLSQSFNT WLKDVFIEND    50
INDLLSARAV FVDAILKKLW CQHHLDEFQI TLIAVGGYGR GELHPQSDVD 100
ILLLTQEEVD LELEEKISSF ITQLWDIKLD IGHSVRSIKE CLKQAVKEVT 150
VATNLMEMRQ VAGNETLTQQ LTPLLSEDVF WTSEKFFIAK CKEQEARHQQ 200
YRGAAYTLEP NLKANPGGLR DIQTIAWVAK RHFSADSLEE LVEHDYLYPN 250
EFFELLESQD YLWRMRFALH FVAGRSENRL LFDYQADVAK MMGFGDEGKA 300
PVERMMKRFF RIIARVTELN TMLLQHFEQA IIKKPELSNI SIINQDFELV 350
DKLINTRNDR IFMRPVKMIE MFLIIAQEPG IKGIHSHTMR LMRNARRRLI 400
SGLIDYAECR RMFMAIIRHP RGLGLALTLM HRHSILSSYL PLWRNIAGQM 450
QFDLFHAYSV DEHSYRVIKN LHQFSQKEHN HKFPLCSKIV QKIRKPEVLY 500
LAGFFHDIGK GRGGDHAKLG AVDALTFCLS HQLSKHDSNM VAWLVEHHLL 550
MSVTAQRRDI NDENVIRTFG EIVRDEAHLN YLYCLTVADM RGTNESLWNN 600
WKANLLEELY FNTLSAFRHG LEKPVEVRSK IRENQQQALA LLNENNVDEQ 650
SIKALWREFR IDYFLRYSPE QIARQCQNIV EHDREKPLVL ISPIPYRGGT 700
EVFIFTKEKN NTFASTVSFL VTKKLSIHDA KIITTKTGYT VNTFVVLDSR 750
NKPLRERFYT KEMSQALVDR LQQVNICELP EPKLARHMKK FKVPLRVNFI 800
KIHAKNRTMI EIIALDRPGL LSNISQVFLE ARVNIHSAKI TTFGEKADDV 850
FTISTEEDDA LTTQEKEALA LRLTQEID 878
Length:878
Mass (Da):101,844
Last modified:September 13, 2005 - v1
Checksum:i90026DD7C373EF21
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000083 Genomic DNA. Translation: AAZ26298.1.
RefSeqiYP_268291.1. NC_003910.7.

Genome annotation databases

EnsemblBacteriaiAAZ26298; AAZ26298; CPS_1549.
GeneIDi3520548.
KEGGicps:CPS_1549.
PATRICi21466307. VBIColPsy94388_1405.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000083 Genomic DNA. Translation: AAZ26298.1 .
RefSeqi YP_268291.1. NC_003910.7.

3D structure databases

ProteinModelPortali Q485H4.
ModBasei Search...

Protein-protein interaction databases

STRINGi 167879.CPS_1549.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ26298 ; AAZ26298 ; CPS_1549 .
GeneIDi 3520548.
KEGGi cps:CPS_1549.
PATRICi 21466307. VBIColPsy94388_1405.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci CPSY167879:GI48-1549-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 34H / ATCC BAA-681.

Entry informationi

Entry nameiGLND_COLP3
AccessioniPrimary (citable) accession number: Q485H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: September 13, 2005
Last modified: June 11, 2014
This is version 64 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