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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Agrobacterium sp. (strain H13-3) (Rhizobium lupini (strain H13-3))
Status
Unreviewed-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 annotationSAAS annotation
Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].UniRule annotationSAAS annotation

Cofactori

Mg2+UniRule annotationSAAS annotation

Enzyme regulationi

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotationSAAS annotation, NucleotidyltransferaseUniRule annotationSAAS annotation, Transferase

Keywords - Ligandi

MagnesiumUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciASP861208:GH59-335-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationSAAS annotation
Short name:
UTase/URUniRule annotation
Alternative name(s):
Bifunctional [protein-PII] modification enzymeUniRule annotation
Bifunctional nitrogen sensor proteinUniRule annotation
Gene namesi
Name:glnDUniRule annotationImported
Ordered Locus Names:AGROH133_03522Imported
OrganismiAgrobacterium sp. (strain H13-3) (Rhizobium lupini (strain H13-3))Imported
Taxonomic identifieri861208 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium
ProteomesiUP000007455 Componenti: Chromosome circular

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini523 – 60684HDUniRule annotationAdd
BLAST
Domaini730 – 81182ACT 1UniRule annotationAdd
BLAST
Domaini841 – 92080ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 373373UridylyltransferaseUniRule annotationAdd
BLAST
Regioni374 – 729356Uridylyl-removingUniRule annotationAdd
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 1 HD domain.UniRule annotation
Contains 2 ACT domains.UniRule annotation

Keywords - Domaini

RepeatUniRule annotationSAAS annotation

Phylogenomic databases

KOiK00990.
OMAiSTIGERV.

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. 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.

F0L5E2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIKDLDFSE ILDVSALKRE CDIIFKNDGK RIADVRSDLL PIFRKASTEG
60 70 80 90 100
REKARELLKS DGSGIDCARR ISWLQDRLIE ILYDLACQYV YPKDAPQIAV
110 120 130 140 150
AAVGGYGRGT LAPGSDIDLL FLLPAKNTPD MHKAVEFVLY LLWDLGFKVG
160 170 180 190 200
HATRTVDECV RLSKSDMTIR TAILEVRAIC GKKSLTDDLE KRFESEVVTG
210 220 230 240 250
TGPEFIAAKL AERDQRHRKA GDTRYLVEPN VKEGKGGLRD LHTLFWIAKY
260 270 280 290 300
YYHVRDTADL VKLGVLSKRE LRLFEKADDF LWAVRCQMHF ITNKAEERLS
310 320 330 340 350
FDIQREIADA LGYQPRPGLS AVERFMKHYF LVAKDVGDLT RIVCAALEDR
360 370 380 390 400
QAKDVPGLSG VLSRFAHRVR KIPGSVEFVE DRGRIALAKP DVFKNDPVNL
410 420 430 440 450
IRLFHIADIN NLELHPDALR VVTRSLSLIN DGLRENEEAN RLFLAILTSR
460 470 480 490 500
RDPALTLRRM NEAGVLGKFI PEFGKIVAMM QFNMYHHYTV DEHLIRSVGV
510 520 530 540 550
LSEVDKGTAV DAHPLANQLM PGVEEREALY VAVLLHDVAK GRQEDHSIAG
560 570 580 590 600
ARVARKLCQR FRLTGKQTEM VVWLIEQHLL MSMVAQTRDL HDRKTITDFA
610 620 630 640 650
DKVQSMERLK MLLILTVCDI RAVGPGVWNG WKGQLLRSLY YETELLLSGG
660 670 680 690 700
FSEVSRKERA HIARQALYDA LEDWGQKARR KYTKLHYEPY LLTVALEDQV
710 720 730 740 750
RHTRFIREAD KQEKALSTMV RTHSFHAITE ITVLAPDHPR LLSIITGACA
760 770 780 790 800
AAGANIADAQ IFTTSDGRAL DTILINREFP IDEDETRRGN NVGKLIEEVL
810 820 830 840 850
SGRQRLPEMI ATRTKSRRKK SAFTIPPSVI ISNGLSNKFT VIEVECLDRP
860 870 880 890 900
GLLADMTAVI ADLSLDIHSA RITTFGEKVI DTFYVTDLFG QKVTNDNRQA
910 920 930 940
SIATRLKAVM SEQEDELRDR MPNGIIAHPD VAALPATRTA KA
Length:942
Mass (Da):106,259
Last modified:May 3, 2011 - v1
Checksum:i9C1AC9C8AB73259B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002248 Genomic DNA. Translation: ADY63324.1.
RefSeqiWP_003514778.1. NC_015183.1.
YP_004277644.1. NC_015183.1.

Genome annotation databases

EnsemblBacteriaiADY63324; ADY63324; AGROH133_03522.
KEGGiagr:AGROH133_03522.
PATRICi46845387. VBIAgrSp164909_0335.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002248 Genomic DNA. Translation: ADY63324.1.
RefSeqiWP_003514778.1. NC_015183.1.
YP_004277644.1. NC_015183.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADY63324; ADY63324; AGROH133_03522.
KEGGiagr:AGROH133_03522.
PATRICi46845387. VBIAgrSp164909_0335.

Phylogenomic databases

KOiK00990.
OMAiSTIGERV.

Enzyme and pathway databases

BioCyciASP861208:GH59-335-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. 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]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequencing of Agrobacterium sp H13-3, the former Rhizobium lupini H13-3, reveals a tripartite genome consisting of a circular and a linear chromosome and an accessory plasmid but lacking a tumor-inducing Ti-plasmid."
    Wibberg D., Blom J., Jaenicke S., Kollin F., Rupp O., Scharf B., Schneiker-Bekel S., Sczcepanowski R., Goesmann A., Setubal J.C., Schmitt R., Puhler A., Schluter A.
    J. Biotechnol. 155:50-62(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: H13-3Imported.

Entry informationi

Entry nameiF0L5E2_AGRSH
AccessioniPrimary (citable) accession number: F0L5E2
Entry historyi
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: May 27, 2015
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported, Multifunctional enzymeUniRule annotationSAAS annotation

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.