Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q89VX9

- GLND_BRADU

UniProt

Q89VX9 - GLND_BRADU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Status
Reviewed - 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 fixation 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

Magnesium.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 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

Enzyme and pathway databases

BioCyciBJAP224911:GJEJ-925-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:bll0916
OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Taxonomic identifieri224911 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
ProteomesiUP000002526: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 929929Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192721Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi224911.bll0916.

Structurei

3D structure databases

ProteinModelPortaliQ89VX9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini524 – 59774HDUniRule annotationAdd
BLAST
Domaini740 – 82283ACT 1UniRule annotationAdd
BLAST
Domaini850 – 92778ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 383383UridylyltransferaseAdd
BLAST
Regioni384 – 739356Uridylyl-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.
HOGENOMiHOG000261779.
InParanoidiQ89VX9.
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.

Q89VX9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDSVTTEHKQ EVDDRFDTAR ITAAVDALAE KHQGREDAFR TAMAQLLKAE
60 70 80 90 100
LIAARAAAQA ILLKDRHGRR CAERLCHVQD EIIRILYSAA TRHLYRSPIP
110 120 130 140 150
SGAERMAVVA TGGYGRGLMA PESDIDLLFI LPYKQTAWGE QVAEAILYCL
160 170 180 190 200
WDMGLKVGHA TRSVDESIRQ ARGDMTIRTA ILETRFLTGD QPLYDELVER
210 220 230 240 250
FDKEVVQGTA SEFVTAKLAE REERHRRGGQ SRYLVEPNVK DGKGALRDLH
260 270 280 290 300
TLFWIAKYVY RVRDTDELVE RGVFDAQEYR TFRRCADFLW SVRCNLHFYS
310 320 330 340 350
GRAEERLSFD LQREIAVRLG YTSHPGMQDV ERFMKHYFLV AKEVGNLTAI
360 370 380 390 400
LCAKLEDQQA KPAPVLSRMM ARLRPTPAKR RVPDSDDFIV DNNRINVAAP
410 420 430 440 450
DVFKHDPVNL IRIFRLAQKH NLAFHPDAMR DVTRSLGLIN AQLRENPEAN
460 470 480 490 500
RLFMEILTSD NAEIVLRRMN ETGVLGHFIR AFGKIVSMMQ FNMYHHYTVD
510 520 530 540 550
EHLIRCVGFL QDIERGGIEE FAVASDLMRK IRPEHRSVIY IATLLHDVAK
560 570 580 590 600
GRPEDHSIAG AKVARRLCPR LGFSPADTEL VAWLIEEHLT MSTVAQSRDL
610 620 630 640 650
SDRKTIENFA AVVQSVEQMK LLTILTTADI RGVGPGVWNG WKAQLLRSLY
660 670 680 690 700
YETEPVLTGG FSEVDRGKRL TAAYAEFRNA FAEWPADELD AYIARHYPAY
710 720 730 740 750
WLKVELPRKI RHARFVRSSE QAGHKLAINV GFDEVRGVTE LTIFAADHPW
760 770 780 790 800
LLSIIAGACA SAGANIVDAQ IYTTTDGRAL DTISISREYD RDEDEGRRAT
810 820 830 840 850
RIGEMIEDVL EGKLRLPEVV ARRTVRSKAR PFVIEPEVTI NNQWSDRYTV
860 870 880 890 900
IEVSGLDRPG LLYELTTAIS KLNLNIASAH VATFGERARD VFYVTDLLGA
910 920
QINAPTRQSA IKSALTHVMA GDKAVQPAA
Length:929
Mass (Da):105,033
Last modified:July 5, 2004 - v2
Checksum:iE4A270C497C26D5E
GO

Sequence cautioni

The sequence BAC46181.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000040 Genomic DNA. Translation: BAC46181.1. Different initiation.
RefSeqiNP_767556.1. NC_004463.1.

Genome annotation databases

EnsemblBacteriaiBAC46181; BAC46181; BAC46181.
GeneIDi1049859.
KEGGibja:bll0916.
PATRICi21185328. VBIBraJap65052_0935.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000040 Genomic DNA. Translation: BAC46181.1 . Different initiation.
RefSeqi NP_767556.1. NC_004463.1.

3D structure databases

ProteinModelPortali Q89VX9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224911.bll0916.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC46181 ; BAC46181 ; BAC46181 .
GeneIDi 1049859.
KEGGi bja:bll0916.
PATRICi 21185328. VBIBraJap65052_0935.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261779.
InParanoidi Q89VX9.
KOi K00990.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci BJAP224911:GJEJ-925-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. 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: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Entry informationi

Entry nameiGLND_BRADU
AccessioniPrimary (citable) accession number: Q89VX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3