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P62223

- GLND_RHOPA

UniProt

P62223 - GLND_RHOPA

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, RPA0591
Organism
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
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 fixation 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 fixation Source: UniProtKB-HAMAP
  2. regulation of nitrogen utilization Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Nitrogen fixation

Keywords - Ligandi

Magnesium

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:RPA0591
OrganismiRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Taxonomic identifieri258594 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
ProteomesiUP000001426: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 929929Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_0000192762Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiP62223. 1 interaction.
MINTiMINT-6732844.
STRINGi258594.RPA0591.

Structurei

3D structure databases

ProteinModelPortaliP62223.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini497 – 59296HD
Add
BLAST
Domaini736 – 81883ACT 1
Add
BLAST
Domaini849 – 92981ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 379379UridylyltransferaseUniRule annotation
Add
BLAST
Regioni380 – 735356Uridylyl-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.
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. 2 hits.
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.

P62223-1 [UniParc]FASTAAdd to Basket

« Hide

MSPSRPAADE RFDSARVAAE IATLAEKHTG NDAAFRTALA MLMKAELAKA    50
RTEAEAQLLR DRHGRRCAER LCYVQDAIIR LLFNAATEYL YNTPTPSSSE 100
RMTVVATGGY GRGLMAPESD IDLLFILPYK QTAWGEQVAE VILYCLWDIG 150
LKVGHATRSV DECIRQARAD MTIRTAILET RFLAGDEALY AELVERFDKE 200
VVEGTAAEFV AAKLAEREER HRRSGQSRYL VEPNVKDGKG GLRDLHTLFW 250
IAKYVYRVRE ASELSERGVF DPAEFRTFRR CEDFLWSVRC NIHFVTKRAE 300
DRLSFDLQRE IGVRLGYTSH PGMQDVERFM KHYFLIAKEV GNLTAILCAK 350
LEDQQAKAAP ALTRMMARLR PAAKRRRVPE SDDFVIDNNR INLAVPDVFK 400
HDPVNLIRIF RLAQKNNLAF HPDAMRSVTR SLSLITPQLR DNPEANRLFV 450
EILTSDNAEP VLRRMNETGV LGRFIRAFGR IVSMMQFNMY HSYTVDEHLI 500
RCVGNLQEIE RGGNDEFALS SELIRKIRPD HRAVLYAAVL LHDIAKGQPE 550
DHSTAGAKVA RRLCPRFGFS TADTELVAWL IEKHLVMSTV AQSRDLSDRK 600
TIENFAAVVE TVEQMKMLTI LTTADIRGVG PGVWNGWKAQ LIRTLYYETE 650
PVLTGGFSEV NRAERIRAAQ AEFRAAFTEW PEADLNAYVA RHYPAYWLKV 700
DLQRKIRHAR FLRASEQAGH KLAINVGFDE ARAVTELTIL AVDHPWLLSV 750
IAGACASAGA NIVDAQIYTT TDGRALDTIS ISREYDRDED EGRRATRIGE 800
TIEEVLEGKL RLPEAVARRA SSGSKAKLRA FVVEPEVEIN NNWSDRYTVI 850
EVSGLDRPGL LYQLTTAISK LNLNIASAHV ATFGERARDV FYVTDLLGAQ 900
ITAPTRQAAI KRALVHLLAN GDAAEKPAA 929
Length:929
Mass (Da):104,542
Last modified:July 5, 2004 - v1
Checksum:iBC13BFA4845F8785
GO

Sequence cautioni

The sequence CAE26035.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX572594 Genomic DNA. Translation: CAE26035.1. Different initiation.
RefSeqiNP_945944.1. NC_005296.1.

Genome annotation databases

EnsemblBacteriaiCAE26035; CAE26035; RPA0591.
GeneIDi2692917.
KEGGirpa:RPA0591.
PATRICi23285359. VBIRhoPal84835_0625.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX572594 Genomic DNA. Translation: CAE26035.1 . Different initiation.
RefSeqi NP_945944.1. NC_005296.1.

3D structure databases

ProteinModelPortali P62223.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P62223. 1 interaction.
MINTi MINT-6732844.
STRINGi 258594.RPA0591.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE26035 ; CAE26035 ; RPA0591 .
GeneIDi 2692917.
KEGGi rpa:RPA0591.
PATRICi 23285359. VBIRhoPal84835_0625.

Phylogenomic databases

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

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. 2 hits.
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: ATCC BAA-98 / CGA009.

Entry informationi

Entry nameiGLND_RHOPA
AccessioniPrimary (citable) accession number: P62223
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: June 11, 2014
This is version 69 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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