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Q9RAE4

- GLND_RHILV

UniProt

Q9RAE4 - GLND_RHILV

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Rhizobium leguminosarum bv. viciae
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, 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 likely 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 metabolism.1 Publication

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 likely activates uridylyl-removing (UR) activity.1 Publication

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

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
OrganismiRhizobium leguminosarum bv. viciae
Taxonomic identifieri387 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Pathology & Biotechi

Disruption phenotypei

Deletions in the 5'-region of this gene appear to be lethal. Insertion mutations in the central part of this gene abolishes the ability to use nitrate as a sole nitrogen source but not glutamine. In addition, neither uridylylation of PII nor induction of the ntr-regulated glnII gene (encoding glutamine synthetase II) under ammonium deficiency can be observed in mutant strains.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 944944Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192758Add
BLAST

Expressioni

Inductioni

Is constitutively expressed, irrespective of the nitrogen content of the medium.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9RAE4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini488 – 602115HDUniRule annotationAdd
BLAST
Domaini728 – 80982ACT 1UniRule annotationAdd
BLAST
Domaini839 – 91880ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 371371UridylyltransferaseAdd
BLAST
Regioni372 – 727356Uridylyl-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

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.

Q9RAE4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRDLDFTNIL DVELLQKQCD AVAEANRNRP DVLRADLLAV LKKASTEGRQ
60 70 80 90 100
KAREALMADG GGLNCAYRIS WLQDQITTVL YNFATAHIFP QQKDKFAVTA
110 120 130 140 150
VGGYGRDTLA PGSDIDLLFL FLPRPAEETH KAVEFMLYVL WDMGFKVGHA
160 170 180 190 200
TRTVEECIAL SKSDMTIRTA ILEMRYICGL QRLETELETR FDKEIVTGTG
210 220 230 240 250
PEFIAAKLAE RDERHRKAGD TRYLVEPNVK EGKGGLRDLH TLFWISKYYY
260 270 280 290 300
HVRDQAELVK LGVLSKHEYR LLEKADDFLW AVRCHMHFLT GKAEERLSFD
310 320 330 340 350
IQREIAEAFG YHTRPGLSAV ERFMKHYFLV AKDVGDLTRI LCAALEDQQA
360 370 380 390 400
KSIPGLTGVI SRFTHRNRKI AGSVEFVEDR GRIALADPEV FKRDPVNIIR
410 420 430 440 450
LFHVADINGL EFHPDALKRV TRSLALIDNA LRENDEANRL FMSILTSKRD
460 470 480 490 500
PALILRRMNE AGVLGRFIPE FGKIVAMMQF NMYHHYTVDE HLIRTVDILS
510 520 530 540 550
EIDKGRAEDL HPLANKLMPG IEDREALYVA VLLHDIAKGR QEDHSIAGAR
560 570 580 590 600
VARKLCVRFG LSQKQTEIVV WLIEEHLTMS MVAQTRDLTD RKTITDFADR
610 620 630 640 650
VQSLDRLKML LILTICDIRA VGPGVWNGWK GQLLRTLYYE TELLLAGGFS
660 670 680 690 700
EVSRKERANA AAEALHSALA DWSQKDRNTY TKLHYQPYLL SVPLEDQIRH
710 720 730 740 750
AHFIRQADKA GQALATMVRT DSFHAITEIT VLSPDHPRLL AVIAGACAAA
760 770 780 790 800
GANIVDAQIF TTSDGRALDT IHVSREFTDD ADELRRAATI GRMIEDVLSG
810 820 830 840 850
RKRLPEVIAT RARNRKKSKA FVIPPSVNIT NSLSNKFTVI EVECLDRPGL
860 870 880 890 900
LSEITAVLSD LSLDIQSARI TTFGEKVIDT FYVTDLVGQK ISGDSKRANI
910 920 930 940
TARMKAVMAE EEDELRERMP SGIIAPAATA RTPPASEKKA GSPI
Length:944
Mass (Da):106,218
Last modified:December 8, 2000 - v2
Checksum:iB164E74FF9E6DF2E
GO

Sequence cautioni

The sequence AAF17352.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155830 Genomic DNA. Translation: AAF17352.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155830 Genomic DNA. Translation: AAF17352.1 . Different initiation.

3D structure databases

ProteinModelPortali Q9RAE4.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "The Rhizobium leguminosarum bv. viciae glnD gene, encoding a uridylyltransferase/uridylyl-removing enzyme, is expressed in the root nodule but is not essential for nitrogen fixation."
    Schluter A., Nohlen M., Kramer M., Defez R., Priefer U.B.
    Microbiology 146:2987-2996(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION, INDUCTION, DISRUPTION PHENOTYPE.
    Strain: VF39.

Entry informationi

Entry nameiGLND_RHILV
AccessioniPrimary (citable) accession number: Q9RAE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: December 8, 2000
Last modified: November 26, 2014
This is version 70 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

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3