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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Rhizobium tropici
Status
Reviewed-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 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

Mg2+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-KW
  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

BioCyciRETL1328306-WGS:GSTH-393-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
OrganismiRhizobium tropici
Taxonomic identifieri398 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 948948Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192761Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ53245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini490 – 603114HDUniRule annotationAdd
BLAST
Domaini729 – 81082ACT 1UniRule annotationAdd
BLAST
Domaini840 – 92182ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 372372UridylyltransferaseAdd
BLAST
Regioni373 – 728356Uridylyl-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.

Q53245-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METHHIDFST VLDVSALKAE CEALAKRGLD KNEERSALLA LLKKASQDGR
60 70 80 90 100
EEARRLLIAD GSGLNCAHRI SWLQDQIITV LYDLTVHHAY PKQAGVFSVT
110 120 130 140 150
AVGGYGRDTL APGSDIDLLF LFQPKPASET HKAVEFILYM LWDMGFKVGH
160 170 180 190 200
ATRSVEECIR EAKSDMTVRT AILETRYICG NVALERELQA RFDKEIVTNT
210 220 230 240 250
GPEFIAAKLA ERDERHRKAG DTRYLVEPNV KEGKGGLRDL HTLFWISKYY
260 270 280 290 300
YHVRDPAELV KLGVLSKQEY RLFEKAEDFL WAVRCHMHFL TGKAEERLSF
310 320 330 340 350
DIQRDIAAAL DYNARPGLSA VERFMKHYFL VAKDVGDLTR ILCAALEDQQ
360 370 380 390 400
AKATPGLTGV ISRFANRSRK IPGTVEFVED RGRIALANPD VFKRDPVSLI
410 420 430 440 450
RLFFVADING LEFHPDALKR VTRSLSLIDN DLRENEEANR LFLSILTSKR
460 470 480 490 500
DPALILRRMN EAGVLGRFIP EFGKIVSMMQ FNMYHHYTVD EHLIRAVEVL
510 520 530 540 550
SEIDKGRAED IHPLTNKLMP NIEDRDALYV AVLLHDIAKG REEDHSEAGA
560 570 580 590 600
AVARKLCPRF GLSPKQTELV VWLIAEHLTM SMVAQTRDLT DRKTIIDFAD
610 620 630 640 650
RVQSLDRLKM LLILTVCDIR AVGPGVWNGW KGQLLRTLYY ETELLLSGGF
660 670 680 690 700
SEVSRKERAE AAAEALEHAL ADWSQKERKA YVKLHYQPYL LSVPLEDQIR
710 720 730 740 750
HTQFMRESDK AGKVLATMVR TDSFHAITEI TVLSPDHPRL LTVIAGACAA
760 770 780 790 800
AGANIADAQI FTTSDGRALD TIHVSREFPD DADELRRAAT IGKMIEDVLA
810 820 830 840 850
GRKRLPEVIA TRTKNRRKNK AFVIPPSVII TNSLSNKFTV IEVECLDRPG
860 870 880 890 900
LLSEITAVLS DLSLDIQSAR ITTFGEKVID TFYVADLVGQ KISNENRRAY
910 920 930 940
ITARLKAVMA GEEDEMRERM PSGIIAPAAT RGVAVEKSDT EKKAGSAA
Length:948
Mass (Da):106,423
Last modified:May 30, 2000 - v2
Checksum:i9CCE1A43545213BD
GO

Sequence cautioni

The sequence AAC32290.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47030 Genomic DNA. Translation: AAC32290.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47030 Genomic DNA. Translation: AAC32290.1. Different initiation.

3D structure databases

ProteinModelPortaliQ53245.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-393-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. O'Connell K.P., Raffel S.J., Saville B.J., Handelsman J.
    Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CIAT899.

Entry informationi

Entry nameiGLND_RHITR
AccessioniPrimary (citable) accession number: Q53245
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 26, 2014
This is version 78 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

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.